Program in Membrane Biology and Renal Unit, Massachusetts General Hospital, and Department of Pathology, Harvard Medical School, Boston, Massachusetts 02114
![]() |
ABSTRACT |
---|
![]() ![]() ![]() ![]() |
---|
Epithelial cells in the kidney have highly specialized transport mechanisms that differ among the many tubule segments, and among the different cell types that are present in some regions. The purpose of this brief review is to examine some of the major intracellular mechanisms by which the membrane proteins that participate in these differentiated cellular functions are addressed, sorted, and delivered to specific membrane domains of epithelial cells. Unraveling these processes is important not only for our understanding of normal cellular function but is also critical for the interpretation of pathophysiological dysfunction in the context of newly generated molecular and cellular information concerning hereditary and acquired transporter abnormalities. Among the topics covered are sorting signals on proteins, role of the cytoskeleton, vesicle coat proteins, the fusion machinery, and exo- and endocytosis of recycling proteins. Examples of these events in renal epithelial cells are highlighted throughout this review and are related to the physiology of the kidney.
protein sorting; epithelial polarity; cytoskeleton; vesicle trafficking; membrane recycling
![]() |
ARTICLE |
---|
![]() ![]() ![]() ![]() |
---|
THROUGHOUT THE LAST DECADE, dramatic progress has been
made in identifying many membrane-associated proteins that participate in the multitude of complex, vectorial transport processes that are
essential for kidney function. These include, but are not limited to,
aquaporins, sodium-hydrogen exchangers, urea transporters, amino acid
transporters, glucose transporters, anion exchangers, thiazide and
bumetanide-sensitive NaCl and
Na+-K+-2Cl cotransporters,
chloride channels, etc. In addition, a host of other important membrane
proteins, including receptors, enzymes, adhesion molecules, and
junctional proteins, have also been identified and localized in renal
epithelial cells (20). These discoveries have been paralleled by the
identification of human diseases that are linked to mutations in the
genes encoding a variety of epithelial cell membrane proteins,
including CLC5 and the cystic fibrosis transmembrane conductance
regulator chloride channels (32, 64), aquaporins (37),
H+-ATPase subunits (66), and sodium channels (25, 54). In some cases, the activity of the protein is directly affected by the
mutation, whereas in other cases the mutation results in a failure of
the intracellular machinery to deliver an otherwise functional protein
to its correct location within the epithelial cell. These latter
pathophysiologies can be grouped together as "diseases of protein
sorting." In addition, some kidney diseases result from acquired
defects. These include lithium-induced diuresis resulting from
downregulation of aquaporin-2 (AQP2) (78) and cadmium-induced
Fanconi-like syndrome, the latter of which results from defective
apical membrane protein recycling in the proximal tubule (59). Because
normal epithelial cell function depends on accurate delivery of this
vast array of membrane components to particular domains of the cell
surface, and because defective targeting can lead to disease, it is
crucial to understand how each cell type interprets intrinsic sorting
signals that are embedded within the amino acid sequence of each
protein. This review briefly considers several of the steps that can be
involved in the process of sorting, addressing, and delivering proteins
to their target membranes (Fig. 1) and
examines how these processes may be related to some aspects of kidney
physiology.
|
Intrinsic Protein Sorting Signals
It has long been realized that specific sorting information is located within the sequence of both transmembrane and cytosolic proteins that determines their ultimate destination within a cell. On the basis of the early observation that different viruses could bud from either the apical (influenza virus) or the basolateral (vesicular stomatitis virus) pole of epithelial cells (43, 93), it was subsequently determined that the viral coat proteins themselves, when transfected alone into cells, also showed a similar polarity of membrane insertion (133). These key data implied that the coat proteins themselves contained targeting information that was sufficient to direct them to a specific membrane domain of the cell. A considerable amount of work has been performed in a variety of systems to dissect protein sequences to identify the nature of their intrinsic targeting information. Among the key findings are the existence of tyrosine-based signals that direct proteins to the basolateral plasma membrane and that also play a role in concentrating proteins into clathrin-coated pits for endocytosis. These motifs include YXRF in the transferrin receptor (34), and NPXY in the low-density lipoprotein receptor and gp330/megalin (30). Many other membrane proteins contain similar motifs. A COOH-terminal dileucine motif (LL) has also been implicated in directing proteins into the clathrin-mediated endocytotic pathway, although endocytosis of the GLUT-4 glucose transporter also involves interaction of the COOH terminus with distinct motifs in the NH2 terminus of the protein (35, 121). Other proteins such as the vasopressin V2 receptor also contain a COOH-terminal dileucine motif (9). Finally, basolateral targeting of the polymeric Ig receptor involves a unique 14-amino-acid sequence in the COOH terminus that has not so far been detected on other proteins (28). However, the sorting signal of many other basolateral proteins remains to be identified, suggesting that nonidentical amino acid sequences can have similar properties and contain similar targeting information. In much the same way, nonidentical hydrophobic stretches of amino acids act as signal sequences to direct the translocation of membrane and secreted proteins across the membrane of the rough endoplasmic reticulum (124).Although it was originally believed that basolateral sorting was the default pathway, and that apical proteins would contain recognizable signals, amino acid-based apical sorting motifs have proven very elusive. However, proteins that are tethered to the lipid bilayer by a glycosylphosphatidylinositol (GPI) anchor rather than by a traditional transmembrane domain are in most (but not all) cases delivered apically (23, 134). GPI-linked proteins are probably sorted into specific, apically directed carrier vesicles at the level of the trans-Golgi network, after interaction with so-called glycolipid rafts in Golgi membranes (55). This may involve an interaction with the protein caveolin, a component of cell-surface pinocytotic invaginations (caveolae) as well as post-Golgi vesicles (96, 109). However, it is noteworthy that caveolae themselves are almost exclusively found on basolateral plasma membrane domains in epithelial cells, an observation that is not compatible with a proposed role in concentrating (mainly apical) GPI-anchored proteins in the plasma membrane (11, 74, 123).
Some proteins, including aquaporin 1, are delivered to both apical and basolateral plasma membranes of epithelial cells, including proximal tubule cells (84, 101) and absorptive cells in the efferent ducts of the male reproductive tract (21). When transfected into LLC-PK1 cells, AQP1 also distributes to both apical and basolateral membranes (68). Whether this distribution reflects the absence of any specific signal, or the presence of a signal that allows insertion into both membrane domains, remains to be established.
One of the first targeting signals to be recognized on any protein was the mannose-6-phosphate residue on lysosomal hydrolases. This posttranslational modification allows these hydrolases to interact with mannose-6-phosphate receptors in the Golgi and to be packaged into vesicles that deliver these hydrolases to lysosomes (24, 113). However, glycosylation per se does not seem to be necessary for the correct targeting of most glycosylated proteins. For example, AQP1 and AQP2 are heavily glycosylated, but absence of glycosylation has little or no effect on either targeting or on water channel function (7, 120). There are scattered reports describing an effect of sugar residues on targeting, but whether this is a widespread requirement remains to be determined (8, 104).
The Cytoskeleton
Microtubules.
The role of microtubules in epithelial cell function and protein
trafficking is well established (20). Microtubule disruption by
colchicine or nocodazole perturbs the delivery of both newly synthesized and recycling proteins to the cell surface and causes a
marked shift in the distribution of many membrane proteins from their
usual surface location onto scattered intracellular vesicles (20). This
process affects rapidly recycling proteins more than membrane proteins
that have a longer residence time at the cell surface (Fig.
2) (18). Endocytosis continues at least
during the initial stages of microtubule disruption, but the
internalized proteins can no longer be effectively recycled back to the
cell surface in the absence of polymerized microtubules. This results in the intracellular accumulation of rapidly recycling proteins such as
AQP2 (100), the H+-ATPase (19), and gp330/megalin (51). The
functional consequences of microtubule disruption on epithelial
transport in various tissues include inhibition of vasopressin-induced
water permeability (38, 63, 65, 86, 91, 117), inhibition of luminal
acidification (115), and inhibition of phosphate transport (39).
|
The actin cytoskeleton. Actin filaments also play a role in the intracellular movement of vesicles and organelles via accessory proteins such as myosin ATPases (31). It has been proposed that whereas microtubules are responsible for "long-range" transport processes in the cell, actin filaments are involved in the final steps of access of vesicles to the underside of the plasma membrane (4, 41, 94). An additional role of the actin-based cortical cell web might actually be to restrict unregulated access of vesicles to the membrane by forming a physical barrier that impedes vesicle movement. Only after an appropriate stimulus (e.g., a rise in intracellular calcium) that results in activation of actin-severing or remodeling proteins such as gelsolin can the barrier be loosened to permit vesicles to move toward the plasma membrane. This hypothesis is supported by experimental data from several cell types that have demonstrated an increase in exocytosis after experimental or physiological actin depolymerization (46, 56, 57, 85, 118).
Actin also serves as a major element in an intracellular scaffold that is erected around many membrane proteins. One version of this scaffold involves several interacting proteins, including ankyrin and spectrin/fodrin (53, 82). Na+-K+-ATPase and AE1 (the band 3 anion exchanger) are just two of the membrane proteins that are cross-linked to the actin cytoskeleton in this way (82). This system serves to retain proteins within specific membrane domains. Proteins that are tethered in this fashion are probably not actively recycling.PDZ-domain binding proteins.
A large and increasing number of proteins have been identified as
"PDZ-domain" proteins. These proteins, named after the initials of the first family members to be described (PSD-95, a mammalian postsynaptic density protein; the disks large protein of
Drosophila; and the tight-junction protein ZO-1) have long (up
to 100) amino acid stretches that form binding pockets for PDZ-binding
domains located on other proteins (40). The PDZ-binding domains are usually at the extreme COOH terminus of the protein and include the
motif DTAL. PDZ-binding proteins appear to be maintained in specific
cell surface domains by interacting with PDZ proteins, which themselves
usually possess a binding domain that allows indirect interaction with
the actin cytoskeleton. This provides another form of actin-based
scaffolding system for maintaining proteins in specific cell-surface
domains. Because PDZ proteins contain more than one binding pocket, it
is thought that clusters of different but functionally related membrane
proteins can be clustered together in an efficient unit by this type of
interaction. Many PDZ-binding proteins have been identified, including
the cystic fibrosis transmembrane conductance regulator (111, 125), potassium channels (26, 69, 70), the -adrenergic receptor (52), and
nitric oxide synthase (105), to name only a few.
The B1 H+-ATPase, 56-kDa subunit is a PDZ-binding protein. We have recently found that the 56-kDa B1 subunit of the vacuolar ATPase is a PDZ-binding protein that can associate with the PDZ protein known as NHE-RF (13). NHE-RF was originally discovered and named because of its interaction with, and regulation of, the NHE3 sodium-hydrogen exchanger in the apical membrane of proximal tubule epithelial cells (128, 129). Our recent data show that NHE-RF is indeed colocalized with NHE3 in the brush-border membrane, but in addition, we found that NHE-RF is colocalized with the H+-ATPase in B-intercalated cells of the kidney but is expressed in much lower amounts in the A cell (13). This raises the possibility that the variable phenotype of the B cell, which can have an apical, basolateral, or bipolar H+-ATPase distribution (15), is in some way regulated by a PDZ-domain scaffolding interaction via the 56-kDa H+-ATPase subunit. Interestingly, we reported previously that the 56-kDa subunit of the H+-ATPase was associated with AQP2-containing endosomes in collecting duct principal cells, which did not contain some of the other H+-ATPase subunits, including the 16-kDa transmembrane proteolipid subunit c (102). Because the 56-kDa B1 subunit has no transmembrane domain, we postulated that it must be attached to the endosome membrane by interaction with other proteins. Our present data raise the possibility that this association could be via an as yet unidentified PDZ-domain protein that is located on these endosomes. It is also intriguing that a different isoform of the 56-kDa subunit, the B2 isoform, is expressed in the proximal tubule and that this isoform has a COOH-terminal truncation that removes the PDZ-binding motif (81). The functional significance of this cell-specific isoform expression remains to be determined.
Vesicle Coat Proteins
Vesicle transport is an integral part of all steps of the biosynthetic and recycling pathways that result in the delivery of proteins to the plasma membrane, and their recovery into the cytoplasm by endocytosis. Some of the vesicles that participate in various parts of the pathway are well defined, whereas others are poorly defined. The most recognizable vesicles are those that have distinct morphological characteristics, usually a "coat" of material on their cytoplasmic surface, detectable by various electron microscopic procedures (Fig. 3).
|
Clathrin. The first coat protein to be identified was clathrin, a coat protein associated with endocytotic coated pits and vesicles, and with some vesicles that bud from the trans-Golgi network (47, 49, 88). Although the precise role of clathrin is not completely understood, it forms a geometric lattice around the invaginating membrane domain and may be involved in the actual formation of the vesicle, as well as in anchoring specific membrane proteins in the forming vesicle to allow their efficient internalization, via a cross-linking interaction with specific "adaptor" proteins (61). In the kidney, the proximal tubule has a very extensive apical clathrin coat that is responsible for much of the endocytosis of filtered proteins in this nephron segment (92). The promiscuous receptor gp330/megalin is concentrated in these proximal tubule clathrin-coated pits and plays a major role in the receptor-mediated endocytosis of many filtered ligands (33, 36). In the collecting duct, the internalization step of vasopressin-stimulated AQP2 membrane recycling is believed to occur via apical clathrin-coated pits (17, 22, 116). Although no clear evidence that AQP2 accumulates in coated pits has yet been obtained in the kidney, preliminary studies by fracture labeling on AQP2-transfected LLC-PK1 cells have shown that AQP2 can cluster into structures on the cell surface that resemble coated pits in freeze-fracture replicas (119).
Caveolin. Caveolin was originally identified as a component of post-Golgi vesicles and was named VIP21 (vesicle integral protein of 21 kDa) (71). It was subsequently found in association with caveolae, which are 60- to 90-nm vesicles or invaginations located at the plasma membrane of many cell types (96). As discussed earlier, caveolae are membrane domains that may be involved in the accumulation, trafficking, and internalization of a select group of proteins that associate with glycolipid-rich regions of the membrane (87). However, any hypothesis concerning their role must take into account the almost unique occurrence of caveolae on the basolateral surface of epithelial cells, and their scarcity at the apical plasma membrane (11, 123). In the kidney, caveolae are most abundant in distal tubule epithelial cells and in collecting duct principal cells. They appear to be absent from proximal tubules and intercalated cells (11). The calcium ATPase has been localized to caveolae in the distal tubule by immunogold electron microscopy (42). By fractionation methods, a whole host of other membrane-associated proteins, including GTP-binding proteins that are involved in signal transduction, have been found in association with Triton X-100-insoluble membrane domains in which the protein caveolin is also enriched (73, 103). However, other data have shown that caveolae isolated by affinity purification with anticaveolin antibodies contain a much more restricted set of proteins (114). Thus the relationship among Triton X-100-insoluble domains, caveolae, and the respective proteins that they contain is still a matter of some dispute.
-COP and the coatomer complex.
A type of non-clathrin-coated vesicle was identified in the Golgi
region of cells by electron microscopy and was subsequently found to
have a distinct coat formed of several protein subunits that together
are called the coatomer complex. One of the first to be identified was
-COP, and other COP components rapidly followed (97). These vesicles
are now believed to be involved in intracisternal transport of proteins
among Golgi cisternae, as well as between the Golgi and the rough
endoplasmic reticulum (89). A specific set of coat components has been
identified on vesicles budding from the rough endoplasmic reticulum
(5). COP proteins have also been found on endosomes in some cells, and
their role may be extended to some aspects of endosome function (130).
Assembly of the COP coat is believed to be required for vesicle budding to occur, in some as yet unspecified way, and this assembly process requires the activity of ADP-ribosylation factor proteins, and phospholipase D isoforms (95, 108).
The H+-ATPase coat.
Vesicles involved in the trafficking of the H+-ATPase to
and from the cell surface of intercalated cells, as well as other proton secreting "mitochondria-rich" cells, have a distinct coat that contains the cytoplasmic subunits (the V1 domain) of
the enzyme (14). We have shown that these vesicles do not contain clathrin (16), caveolin (11), or -COP (10), and the conclusion is
that they represent a novel class of transport vesicle that is capable
of undergoing both exo- and endocytosis by using an as yet unidentified
mechanism. However, cellubrevin, which is an analog of the synaptic
vesicle protein synaptobrevin, may be involved in the fusion of these
vesicles with the plasma membrane, as will be discussed below. Our
present hypothesis is that some of the subunits of the V1
domain of the H+-ATPase are involved in the recycling of
these vesicles and that they interact with other components of the
trafficking and sorting machinery to achieve this end.
The SNARE Hypothesis and Membrane Fusion
Work performed initially on synaptic vesicles and yeast has identified several homologous proteins that associate with plasma membranes and intracellular vesicles to form a so-called fusion machine (27, 98). These proteins interact to allow selective and specific fusion between vesicles and their target membranes to occur. Most fusion events so far examined involve a similar battery of proteins. One group of proteins that participate in this process are called SNAREs [or SNAP receptors, where SNAP is an acronym for soluble NEM-sensitive factor (NSF) attachment protein]. The SNAREs that are associated with vesicles are known as v-SNARES, and those on target membranes such as the plasma membrane are t-SNAREs. Membrane-associated SNAREs form a lock and key that is activated by soluble proteins, including NSF, various SNAP isoforms, and small-molecular-weight GTPases (90, 127). In synaptic vesicles, the v-SNARE is known as vesicle-associated membrane protein (VAMP) or synaptobrevin. Cellubrevin is a more ubiquitous homolog found in many nonneuronal cells (79), including proton-secreting mitochondria-rich cells (10). The t-SNAREs include the syntaxin family of proteins, and different syntaxins have different cellular and membrane distributions. Many proteins associated with this fusion machinery have been identified and may play a key role in aquaporin insertion in principal cells of the kidney (58, 76, 77, 83) and in proton-secreting epithelial cells in the kidney and the male reproductive tract (10, 12). Recent data have shown that tetanus toxin, which cleaves cellubrevin and synaptobrevin, inhibits apical proton secretion in inner medullary collecting duct cells in culture (3) and in isolated vas deferens from the reproductive tract (12). The proposed mechanism is via an inhibition of cellubrevin-dependent exocytosis of H+-ATPase-containing vesicles, leading to a progressive loss of plasma membrane H+-ATPase in these cells.However, although SNARE proteins have a role to play in membrane fusion events, the participation of other components is also essential. In fact, the precise role of the SNARE proteins is very controversial at the moment. A recent study showing that v-SNAREs and t-SNAREs are promiscuous, and do not pair in precise patterns, implies that these proteins are probably not responsible for the specificity of membrane fusion events (131). It is now appreciated that small-molecular-weight G proteins of the Rab family and so-called "tethering proteins" interact to bind membranes together before the input from SNARE proteins (126) and may be more involved in determining specificity (48). These tethering factors are large proteins, such as giantin and early endosome antigen 1 (EEA1), and their tethering function requires Rab activity. For example, endosome-endosome fusion requires EEA1 and the GTP-bound form of rab 5 under normal conditions (112). Furthermore, tethering proteins themselves interact with a variety of additional proteins that complicate the picture even more. The reader is referred to recent reviews for a more detailed description of these issues (48, 126). Thus the emerging picture is that the specificity of membrane targeting requires the sequential interaction of tethering factors, rab GTPases, and SNAREs.
Membrane Recycling
Many membrane proteins are rapidly recycled between intracellular vesicles and the cell surface whereas others have longer residence times at the cell surface. Protein recycling has important implications for epithelial cell function. It allows surface receptors to internalize their ligands, which may include hormones, nutrients, and toxins. It allows the cell to control the cell-surface expression of proteins via variations in the rate of endocytosis and exocytosis of any given protein. The renal proximal tubule can modulate a variety of apical proteins in this way, including megalin/gp330 (33, 51), phosphate transporters (60), and the H+-ATPase (2). The collecting duct recycles AQP2 between intracellular vesicles and the cell surface in response to vasopressin (1, 44, 122), whereas recycling and polarized expression of the H+-ATPase is modulated by systemic acid-base conditions (6, 75, 99, 107). These processes are subject to a complex series of control mechanisms, some of which have been discussed above. They often require some posttranslational modification of the transported protein to be activated. For example, phosphorylation is a key event in AQP2 trafficking (45, 67) and is also required for internalization and transcytosis of the polymeric Ig receptor in epithelial cells (29). The recycling of proteins can be interrupted by interventions that neutralize intracellular acidic compartments (80). We have shown that bafilomycin inhibits AQP2 recycling in transfected LLC-PK1 cells and causes an extensive accumulation of AQP2 in the trans-Golgi region of the cell (50). A similar inhibition of AQP2 recycling is caused by low temperature (50). Protein recycling is also inhibited by microtubule disruption (20). These processes are illustrated for AQP2 in Fig. 4.
|
Why some cellular transport functions are modulated by the insertion and removal of cell surface transporters, and others by "gating" transporters that are already present at the cell surface, is not entirely clear. Presumably, different physiological control mechanisms and appropriate response times are best suited to one mechanism vs. another. However, these two processes are not mutually exclusive, and control of vectorial transport can be achieved both by increased or decreased transporter expression at the plasma membrane as well as by rapid activation/inhibition of cell-surface proteins. It should also be noted that the cellular content of some transporters is chronically regulated at the transcriptional level, leading to increased protein expression. For example, AQP2 mRNA transcription is increased by elevated cAMP via a cAMP-responsive element in the promoter region of the gene (62, 132). Thus both acute and chronic responses to vasopressin regulate cellular and membrane AQP2 expression.
In summary, it is clear that many of the physiological transport processes in the kidney and other transporting epithelia that were elegantly dissected by Carl Gottschalk and his peers can now be at least partially explained at the cell and molecular biological level. Nonetheless, considerable work remains to relate the physiological and pathophysiological regulation and dysregulation of these processes to our present knowledge of transporter structure, function, and intracellular trafficking. It should be expected that mutations in genes encoding "generic" accessory proteins that are involved in protein trafficking and targeting might affect many processes and would be incompatible with cell viability. In contrast, mutations in specific transporter genes are already known to cause disease, and the number of such pathophysiological conditions related to transporter malfunction or missorting (either hereditary or acquired) will certainly increase over the next few years. Ultimately, this knowledge must be applied to the whole-animal level to understand the complex interplay among the multitude of physiological stimuli that affect renal function.
![]() |
ACKNOWLEDGEMENTS |
---|
I thank the innumerable excellent colleagues with whom I have had the pleasure of working over the past few years, but especially my current colleagues and collaborators Seth Alper, Sylvie Breton, Steven Gluck, Ivan Sabolic, and Alan Verkman, without whom these studies would not have been possible. I wish to thank Dennis Ausiello, now Chief of Medicine at Massachusetts General Hospital, for his continual friendship and support, Lelio Orci for support and excellent mentorship and training during my 10 years in Geneva, Switzerland, and my wife, Andrea, and children Eleanor, Chris, and Marielle for sharing me with science and soccer for so many years. Finally, I am deeply grateful to the APS Renal Section for honoring me with the Carl Gottschalk Distinguished Lecture Award.
![]() |
FOOTNOTES |
---|
The studies from our own laboratory that are described have received continuous support from the National Institute of Diabetes and Digestive and Kidney Diseases since 1986 (Grants DK-38452 and DK-42956), and from the Swiss National Science Foundation before 1986.
Address for reprint requests and other correspondence: D. Brown, Renal Unit, Massachusetts General Hospital East, 149 13th St., Charlestown, MA 02129 (E-mail: brown{at}receptor.mgh.harvard.edu).
![]() |
REFERENCES |
---|
![]() ![]() ![]() ![]() |
---|
1.
Agre, P.,
D. Brown,
and
S. Nielsen.
Aquaporin water channels: unanswered questions and unresolved controversies.
Curr. Opin. Cell Biol.
7:
472-483,
1995[ISI][Medline].
2.
Al-Awqati, Q.
Plasticity in epithelial polarity of renal intercalated cells: targeting of the H+-ATPase and band 3.
Am. J. Physiol. Cell Physiol.
270:
C1571-C1580,
1996
3.
Alexander, E. A.,
T. Shih,
and
J. H. Schwartz.
H+ secretion is inhibited by clostridial toxins in an inner medullary collecting duct cell line.
Am. J. Physiol. Renal Physiol.
273:
F1054-F1057,
1997
4.
Allan, V. J.,
and
T. A. Schroer.
Membrane motors.
Curr. Opin. Cell Biol.
11:
476-482,
1999[ISI][Medline].
5.
Barlowe, C.,
L. Orci,
T. Yeung,
M. Hosobuchi,
S. Hamamoto,
N. Salama,
M. F. Rexach,
M. Ravazzola,
M. Amherdt,
and
R. Scheckman.
COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum.
Cell
77:
895-907,
1994[ISI][Medline].
6.
Bastani, B.,
H. Purcell,
P. Hemken,
D. Trigg,
and
S. Gluck.
Expression and distribution of renal vacuolar proton-translocating adenosine triphosphatase in response to chronic acid and alkali loads in the rat.
J. Clin. Invest.
88:
126-136,
1991[ISI][Medline].
7.
Baumgarten, R.,
M. H. van De Pol,
J. F. Wetzels,
C. H. van Os,
and
P. M. Deen.
Glycosylation is not essential for vasopressin-dependent routing of aquaporin-2 in transfected Madin-Darby canine kidney cells.
J. Am. Soc. Nephrol.
9:
1553-1559,
1998[Abstract].
8.
Benting, J. H.,
A. G. Rietveld,
and
K. Simons.
N-glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin-Darby canine kidney cells.
J. Cell Biol.
146:
313-320,
1999
9.
Birnbaumer, M.,
A. Seibold,
S. Gilbert,
M. Ishido,
C. Barberis,
A. Antaramian,
P. Brabet,
and
W. Rosenthal.
Molecular cloning of the receptor for human antidiuretic hormone.
Nature
357:
333-335,
1992[ISI][Medline].
10.
Breton, S.,
E. Heller,
and
D. Brown.
Distribution of the vesicle-associated proteins -COP and cellubrevin in the kidney and epididymis (Abstract).
J. Am. Soc. Nephrol.
8:
58A,
1997.
11.
Breton, S.,
M. P. Lisanti,
R. Tyszkowski,
M. McLaughlin,
and
D. Brown.
Basolateral distribution of caveolin-1 in the kidney. Absence from H+- ATPase-coated endocytic vesicles in intercalated cells.
J. Histochem. Cytochem.
46:
205-214,
1998
12.
Breton, S.,
N. N. Nsumu,
T. Galli,
P. J. S. Smith,
and
D. Brown.
"SNARE" vesicle fusion proteins are involved in proton secretion in the epididymis/vas deferens (Abstract).
J. Am. Soc. Nephrol.
9:
3A,
1998.
13.
Breton, S., T. Wiederhold, V. Marshansky, V. Ramesh, and D. Brown. The PDZ-domain protein NHE-RF interacts with the B1 subunit
of the H+ATPase and colocalizes with proton pumps in type B
intercalated cells (Abstract). J. Am. Soc. Nephrol. In
press.
14.
Brown, D.,
and
S. Breton.
Mitochondria-rich, proton-secreting epithelial cells.
J. Exp. Biol.
199:
2345-2358,
1996
15.
Brown, D.,
S. Hirsch,
and
S. Gluck.
An H+ATPase is present in opposite plasma membrane domains in subpopulations of kidney epithelial cells.
Nature
331:
622-624,
1988[ISI][Medline].
16.
Brown, D.,
and
L. Orci.
The "coat" of kidney intercalated cell tubulovesicles does not contain clathrin.
Am. J. Physiol. Cell Physiol.
250:
C605-C608,
1986
17.
Brown, D.,
and
L. Orci.
Vasopressin stimulates formation of coated pits in rat kidney collecting ducts.
Nature
302:
253-255,
1983[ISI][Medline].
18.
Brown, D.,
and
I. Sabolic.
Endosomal pathways for water channel and proton pump recycling in kidney epithelial cells.
J. Cell Sci. Suppl.
17:
49-59,
1993.
19.
Brown, D.,
I. Sabolic,
and
S. Gluck.
Colchicine-induced redistribution of proton pumps in kidney epithelial cells.
Kidney Int.
40, Suppl.33:
S79-S83,
1991[ISI].
20.
Brown, D.,
and
J. L. Stow.
Protein trafficking and polarity in kidney epithelium: from cell biology to physiology.
Physiol. Rev.
76:
245-297,
1996
21.
Brown, D.,
J. M. Verbavatz,
G. Valenti,
B. Lui,
and
I. Sabolic.
Localization of the CHIP28 water channel in reabsorptive segments of the rat male reproductive tract.
Eur. J. Cell Biol.
61:
264-273,
1993[ISI][Medline].
22.
Brown, D.,
P. Weyer,
and
L. Orci.
Vasopressin stimulates endocytosis in kidney collecting duct epithelial cells.
Eur. J. Cell Biol.
46:
336-340,
1988[ISI][Medline].
23.
Brown, D. A.,
and
J. K. Rose.
Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface.
Cell
68:
533-544,
1992[ISI][Medline].
24.
Brown, W. J.,
and
M. G. Farquhar.
The mannose-6-phosphate receptor for lysosomal enzymes is concentrated in cis Golgi cisternae.
Cell
36:
295-307,
1984[ISI][Medline].
25.
Bubien, J. K.,
I. I. Ismailov,
B. K. Berdiev,
T. Cornwell,
R. P. Lifton,
C. M. Fuller,
J. M. Achard,
D. J. Benos,
and
D. G. Warnock.
Liddle's disease: abnormal regulation of amiloride-sensitive Na+ channels by beta-subunit mutation.
Am. J. Physiol. Cell Physiol.
270:
C208-C213,
1996
26.
Burke, N. A.,
K. Takimoto,
D. Li,
W. Han,
S. C. Watkins,
and
E. S. Levitan.
Distinct structural requirements for clustering and immobilization of K+ channels by PSD-95.
J. Gen. Physiol.
113:
71-80,
1999
27.
Cameron, P.,
O. Mundigi,
and
P. de Camilli.
Traffic of synaptic vesicle proteins in polarized and nonpolarized cells.
J. Cell Sci. Suppl.
17:
193-200,
1993.
28.
Casanova, J. E.,
G. Apodaca,
and
K. E. Mostov.
An autonomous signal for basolateral sorting in the cytoplasmic domain of the polymeric immunoglobulin receptor.
Cell
66:
65-75,
1991[ISI][Medline].
29.
Casanova, J. E.,
P. P. Breitfeld,
S. A. Ross,
and
K. E. Mostov.
Phosphorylation of the polymeric immunoglobulin receptor required for its efficient transcytosis.
Science
248:
742-745,
1990[ISI][Medline].
30.
Chen, W. J.,
J. L. Goldstein,
and
M. S. Brown.
NPXY, a sequence often found in cytoplasmic tails, is required for coated pit-mediated internalization of the low density lipoprotein receptor.
J. Biol. Chem.
265:
3116-3123,
1990
31.
Cheney, R. E.,
and
M. S. Mooseker.
Unconventional myosins.
Curr. Opin. Cell Biol.
4:
27-35,
1992[Medline].
32.
Cheng, S. H.,
R. J. Gregory,
J. Marshall,
S. Paul,
D. W. Souza,
G. A. White,
C. R. O'Riordan,
and
A. E. Smith.
Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis.
Cell
63:
827-834,
1990[ISI][Medline].
33.
Christensen, E. I.,
H. Birn,
P. Verroust,
and
S. K. Moestrup.
Membrane receptors for endocytosis in the renal proximal tubule.
Int. Rev. Cytol.
180:
237-284,
1998[ISI][Medline].
34.
Collawn, J. F.,
M. Stangel,
L. A. Kuhn,
V. Esekogwu,
S. Jing,
I. S. Trowbridge,
and
J. A. Tainer.
Transferrin receptor internalization sequence YXRF implicates a tight turn as the structural recognition motif for endocytosis.
Cell
63:
1061-1072,
1990[ISI][Medline].
35.
Corvera, S.,
A. Chawla,
R. Chakrabarti,
M. Joly,
J. Buxton,
and
M. P. Czech.
A double leucine within the GLUT4 glucose transporter COOH-terminal domain functions as an endocytosis signal.
J. Cell Biol.
126:
979-989,
1994[Abstract].
36.
Czekay, R. P.,
R. A. Orlando,
L. Woodward,
M. Lundstrom,
and
M. G. Farquhar.
Endocytic trafficking of megalin/RAP complexes: dissociation of the complexes in late endosomes.
Mol. Biol. Cell
8:
517-532,
1997[Abstract].
37.
Deen, P. M.,
and
N. V. Knoers.
Vasopressin type-2 receptor and aquaporin-2 water channel mutants in nephrogenic diabetes insipidus.
Am. J. Med. Sci.
316:
300-309,
1998[ISI][Medline].
38.
Dousa, T. P.,
and
L. D. Barnes.
Effects of colchicine and vinblastine on the cellular action of vasopressin in the mammalian kidney. A possible role of microtubules.
J. Clin. Invest.
54:
252-262,
1974[ISI][Medline].
39.
Dousa, T. P.,
C. G. Duarte,
and
F. G. Knox.
Effect of colchicine on urinary phosphate and regulation by parathyroid hormone.
Am. J. Physiol.
231:
61-65,
1976[ISI][Medline].
40.
Fanning, A. S.,
and
J. Anderson.
Protein-protein interactions: PDZ domain networks.
Curr. Biol.
6:
1385-1388,
1996[ISI][Medline].
41.
Fath, K. R.,
S. N. Mamajiwalla,
and
D. R. Burgess.
The cytoskeleton in development of cell polarity.
J. Cell Sci. Suppl.
17:
65-73,
1993.
42.
Fujimoto, T.
Calcium pump of the plasma membrane is localized in caveolae.
J. Cell Biol.
120:
1147-1157,
1993[Abstract].
43.
Fuller, S.,
C. H. von Bonsdorff,
and
K. Simons.
Vesicular stomatitis virus infects and matures only through the basolateral surface of the polarized epithelial cell line, MDCK.
Cell
38:
65-77,
1984[ISI][Medline].
44.
Fushimi, K.,
and
F. Marumo.
Water channels.
Curr. Opin. Nephrol. Hyper.
4:
392-397,
1995[Medline].
45.
Fushimi, K.,
S. Sasaki,
and
F. Marumo.
Phsophorylation of serine 256 is required for cAMP-dependent regulatory exocytosis of the aquaporin-2 water channel.
J. Biol. Chem.
272:
14800-14804,
1997
46.
Gasman, S.,
S. Chasserot-Golaz,
M. R. Popoff,
D. Aunis,
and
M. F. Bader.
Trimeric G proteins control exocytosis in chromaffin cells. Go regulates the peripheral actin network and catecholamine secretion by a mechanism involving the small GTP-binding protein Rho.
J. Biol. Chem.
272:
20564-20571,
1997
47.
Goldstein, J. L.,
R. G. W. Anderson,
and
M. S. Brown.
Coated pits, coated vesicles and receptor-mediated endocytosis.
Nature
279:
679-685,
1979[ISI][Medline].
48.
Gonzalez, L., Jr.,
and
R. H. Scheller.
Regulation of membrane trafficking: structural insights from a Rab/effector complex.
Cell
96:
755-758,
1999[ISI][Medline].
49.
Griffiths, G.,
and
K. Simons.
The trans Golgi network: sorting at the exit site of the Golgi complex.
Science
234:
438-443,
1986[ISI][Medline].
50.
Gustafson, C. E.,
T. Katsura,
M. McKee,
R. Bouley,
J. E. Casanova,
and
D. Brown.
Recycling of AQP2 occurs through a temperature- and bafilomycin-sensitive trans-Golgi-associated compartment in LLC-PK1 cells.
Am. J. Physiol. Renal Physiol.
278:
F317-F326,
2000
51.
Gutmann, E. J.,
J. L. Niles,
R. T. McCluskey,
and
D. Brown.
Colchicine-induced redistribution of an apical membrane glycoprotein (gp330) in proximal tubules.
Am. J. Physiol. Cell Physiol.
257:
C397-C407,
1989
52.
Hall, R. A.,
R. T. Premont,
C. W. Chow,
J. T. Blitzer,
J. A. Pitcher,
A. Claing,
R. H. Stoffel,
L. S. Barak,
S. Shenolikar,
E. J. Weinman,
S. Grinstein,
and
R. J. Lefkowitz.
The 2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange.
Nature
392:
626-630,
1998[ISI][Medline].
53.
Hammerton, R. W.,
K. A. Krzeminski,
R. W. Mays,
T. A. Ryan,
D. A. Wollner,
and
W. J. Nelson.
Mechanism for regulating cell surface distribution of Na+K+ATPase in polarized epithelial cells.
Science
254:
847-850,
1991[ISI][Medline].
54.
Hansson, J. H.,
L. Schild,
Y. Lu,
T. A. Wilson,
I. Gautschi,
R. Shimkets,
C. Nelson-Williams,
B. C. Rossier,
and
R. P. Lifton.
A de novo missense mutation of the beta subunit of the epithelial sodium channel causes hypertension and Liddle syndrome, identifying a proline-rich segment critical for regulation of channel activity.
Proc. Natl. Acad. Sci. USA.
92:
11495-11499,
1995[Abstract].
55.
Harder, T.,
and
K. Simons.
Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains.
Curr. Opin. Cell Biol.
9:
534-542,
1997[ISI][Medline].
56.
Hartwig, J. H.,
D. A. Ausiello,
and
D. Brown.
Vasopressin-induced changes in the three-dimensional structure of toad bladder apical surface.
Am. J. Physiol. Cell Physiol.
253:
C707-C720,
1987
57.
Hays, R. M.,
J. Condeelis,
Y. Gao,
H. Simon,
G. Ding,
and
N. Franki.
The effect of vasopressin on the cytoskeleton of the epithelial cell.
Pediatr. Nephrol.
7:
672-679,
1993[ISI][Medline].
58.
Hays, R. M.,
N. Franki,
H. Simon,
and
Y. Gao.
Antidiuretic hormone and exocytosis: lessons from neurosecretion.
Am. J. Physiol. Cell Physiol.
267:
C1507-C1524,
1994
59.
Herak-Kramberger, C. M.,
D. Brown,
and
I. Sabolic.
Cadmium inhibits vacuolar H+-ATPase and endocytosis in rat kidney cortex.
Kidney Int.
53:
1713-1726,
1998[ISI][Medline].
60.
Herak-Kramberger, C. M.,
B. Spindler,
J. Biber,
H. Murer,
and
I. Sabolic.
Renal type II Na/Pi-cotransporter is strongly impaired whereas the Na/sulphate-cotransporter and aquaporin 1 are unchanged in cadmium-treated rats.
Pflügers Arch.
432:
336-344,
1996[ISI][Medline].
61.
Hirst, J.,
and
M. S. Robinson.
Clathrin and adaptors.
Biochim. Biophys. Acta
1404:
173-193,
1998[ISI][Medline].
62.
Hozawa, S.,
E. J. Holtzman,
and
D. A. Ausiello.
cAMP motifs regulating transcription in the aquaporin 2 gene.
Am. J. Physiol. Cell Physiol.
270:
C1695-C1702,
1996
63.
Iyengar, R.,
K. G. Lepper,
and
D. S. Mailman.
Involvement of microtubules and microfilaments in the action of vasopressin in canine renal medulla.
J. Supramolec. Struct.
5:
521-530,
1976[ISI][Medline].
64.
Jentsch, T. J.,
T. Friedrich,
A. Schriever,
and
H. Yamada.
The CLC chloride channel family.
Pflügers Arch.
437:
783-795,
1999[ISI][Medline].
65.
Kachadorian, W. A.,
S. J. Ellis,
and
J. Muller.
Possible roles for microtubules and microfilaments in ADH action on toad urinary bladder.
Am. J. Physiol. Renal Fluid Electrolyte Physiol.
236:
F14-F20,
1979
66.
Karet, F. E.,
K. E. Finberg,
R. D. Nelson,
A. Nayir,
H. Mocan,
S. A. Sanjad,
J. Rodriguez-Soriano,
F. Santos,
C. W. Cremers,
A. Di Pietro,
B. I. Hoffbrand,
J. Winiarski,
A. Bakkaloglu,
S. Ozen,
R. Dusunsel,
P. Goodyer,
S. A. Hulton,
D. K. Wu,
A. B. Skvorak,
C. C. Morton,
M. J. Cunningham,
V. Jha,
and
R. P. Lifton.
Mutations in the gene encoding B1 subunit of H+-ATPase cause renal tubular acidosis with sensorineural deafness.
Nature Genet.
21:
84-90,
1999[ISI][Medline].
67.
Katsura, T.,
C. E. Gustafson,
D. A. Ausiello,
and
D. Brown.
Protein kinase A phosophorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells.
Am. J. Physiol. Renal Physiol.
272:
F817-F822,
1997[Abstract].
68.
Katsura, T.,
J. M. Verbavatz,
J. Farinas,
T. Ma,
D. A. Ausiello,
A. S. Verkman,
and
D. Brown.
Constitutive and regulated membrane expression of aquaporin 1 and aquaporin 2 water channels in stably transfected LLC-PK1 epithelial cells.
Proc. Natl. Acad. Sci. USA
92:
7212-7216,
1995[Abstract].
69.
Kim, E.,
M. Niethammer,
A. Rothschild,
Y. N. Jan,
and
M. Sheng.
Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases.
Nature
378:
85-88,
1995[ISI][Medline].
70.
Kurschner, C.,
P. G. Mermelstein,
W. T. Holden,
and
D. J. Surmeier.
CIPP, a novel multivalent PDZ domain protein, selectively interacts with Kir4.0 family members, NMDA receptor subunits, neurexins, and neuroligins.
Mol. Cell. Neurosci.
11:
161-172,
1998[ISI][Medline].
71.
Kurzchalia, T. V.,
P. Dupree,
and
S. Monier.
VIP21-caveolin, a protein of the trans-Golgi network and caveolae.
FEBS Lett.
346:
88-91,
1994[ISI][Medline].
72.
Lafont, F.,
J. K. Burkhardt,
and
K. Simons.
Involvement of microtubule motors in basolateral and apical transport in kidney cells.
Nature
372:
801-803,
1994[ISI][Medline].
73.
Li, S.,
T. Okamoto,
M. Chun,
M. Sargiacomo,
J. E. Casanova,
S. H. Hansen,
I. Nishimoto,
and
M. P. Lisanti.
Evidence for a regulated interaction between heterotrimeric G proteins and caveolin.
J. Biol. Chem.
270:
15693-15701,
1995
74.
Lipardi, C.,
R. Mora,
V. Colomer,
S. Paladino,
L. Nitsch,
E. Rodriguez-Boulan,
and
C. Zurzolo.
Caveolin transfection results in caveolae formation but not apical sorting of glycosylphosphatidylinositol (GPI)-anchored proteins in epithelial cells.
J. Cell Biol.
140:
617-626,
1998
75.
Madsen, K. M.,
J. W. Verlander,
J. Kim,
and
C. C. Tisher.
Morphological adaptation of the collecting duct to acid-base disturbances.
Kidney Int.
40, Suppl.33:
S57-S63,
1991[ISI].
76.
Mandon, B.,
C. L. Chou,
S. Nielsen,
and
M. A. Knepper.
Syntaxin-4 is localized to the apical plasma membrane of rat renal collecting duct cells: possible role in aquaporin-2 trafficking.
J. Clin. Invest.
98:
906-913,
1996
77.
Mandon, B.,
S. Nielsen,
B. K. Kishore,
and
M. A. Knepper.
Expression of syntaxins in rat kidney.
Am. J. Physiol. Renal Physiol.
273:
F718-F730,
1997[ISI][Medline].
78.
Marples, D.,
S. Christensen,
E. I. Christensen,
P. D. Ottosen,
and
S. Nielsen.
Lithium-induced downregulation of aquaporin-2 water channel expression in rat kidney medulla.
J. Clin. Invest.
95:
1838-1845,
1995[ISI][Medline].
79.
McMahon, H. T.,
Y. A. Ushkaryov,
L. Edelmann,
E. Link,
T. Binz,
H. Niemann,
R. Jahn,
and
T. C. Sudhof.
Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein.
Nature
364:
346-349,
1993[ISI][Medline].
80.
Mellman, I.,
R. Fuchs,
and
A. Helenius.
Acidification of the endocytic and exocytic pathways.
Annu. Rev. Biochem.
55:
663-700,
1986[ISI][Medline].
81.
Nelson, R. D.,
X. L. Guo,
K. Masood,
D. Brown,
M. Kalkbrenner,
and
S. Gluck.
Selectively amplified expression of an isoform of the vacuolar H+-ATPase 56-kilodalton subunit in renal intercalated cells.
Proc. Natl. Acad. Sci. USA
89:
3541-3545,
1992[Abstract].
82.
Nelson, W. J.,
and
R. W. Hammerton.
A membrane-cytoskeletal complex containing Na+, K+-ATPase, ankyrin, and fodrin in Madin-Darby canine kidney (MDCK) cells: implications for the biogenesis of epithelial cell polarity.
J. Cell Biol.
108:
893-902,
1989[Abstract].
83.
Nielsen, S.,
D. Marples,
H. Birn,
M. Mohtashami,
N. O. Dalby,
M. Trimble,
and
M. Knepper.
Expression of VAMP-2-like protein in kidney collecting duct intracellular vesicles. Colocalization with Aquaporin-2 water channels.
J. Clin. Invest.
96:
1834-1844,
1995[ISI][Medline].
84.
Nielsen, S.,
B. L. Smith,
E. I. Christensen,
M. A. Knepper,
and
P. Agre.
CHIP28 water channels are localized in constitutively waterpermeable segments of the nephron.
J. Cell Biol.
120:
371-383,
1993[Abstract].
85.
Obberghen, E. v.,
G. Somers,
G. Devis,
G. D. Vaughan,
F. Malaisse-Lagae,
L. Orci,
and
W. J. Malaisse.
Dynamics of insulin release and microtubular-microfilamentous system. I. Effect of cytochalasin B.
J. Clin. Invest.
52:
1041-1051,
1973[ISI][Medline].
86.
Parisi, M.,
M. Pisam,
J. Merot,
J. Chevalier,
and
J. Bourguet.
The role of microtubules and microfilaments in the hydrosmotic response to antidiuretic hormone.
Biochim. Biophys. Acta
817:
F707-F715,
1985.
87.
Parton, R. G.
Caveolae and caveolins.
Curr. Opin. Cell Biol.
8:
542-548,
1996[ISI][Medline].
88.
Pearse, B. M. F.
Clathrin: a unique protein associated with intracellular transfer of membrane by coated vesicles.
Proc. Natl. Acad. Sci. USA
73:
1255-1259,
1976[Abstract].
89.
Pelham, H. R.
The dynamic organisation of the secretory pathway.
Cell Struct. Funct.
21:
413-419,
1996[ISI][Medline].
90.
Pfeffer, S. R.
Transport vesicle docking: SNAREs and associates.
Annu. Rev. Cell Dev. Biol.
12:
441-461,
1996[ISI][Medline].
91.
Phillips, M. E.,
and
A. Taylor.
Effect of nocodazole on the water permeability response to vasopressin in rabbit collecting tubules in vitro.
J. Physiol. (Lond.)
411:
529-544,
1989[Abstract].
92.
Rodman, J. S.,
D. Kerjaschki,
E. Merisko,
and
M. G. Farquhar.
Presence of an extensive clathrin coat on the apical plasmalemma of the rat kidney proximal tubule cell.
J. Cell Biol.
98:
1630-1636,
1984[Abstract].
93.
Rodriguez-Boulan, E.,
K. T. Paskiet,
and
D. D. Sabatini.
Assembly of enveloped viruses in Madin-Darby canine kidney cells: polarized budding from single attached cells and from clusters of cells in suspension.
J. Cell Biol.
96:
866-874,
1983[Abstract].
94.
Rogers, S. L.,
and
V. I. Gelfand.
Myosin cooperates with microtubule motors during organelle transport in melanophores.
Curr. Biol.
8:
161-164,
1998[ISI][Medline].
95.
Roth, M. G.,
K. Bi,
N. T. Ktistakis,
and
S. Yu.
Phospholipase D as an effector for ADP-ribosylation factor in the regulation of vesicular traffic.
Chem. Phys. Lipids
98:
141-152,
1999[ISI][Medline].
96.
Rothberg, K. G.,
J. E. Heuser,
W. C. Donzell,
Y. S. Ying,
J. R. Glenney,
and
R. G. Anderson.
Caveolin, a protein component of caveolae membrane coats.
Cell
68:
673-682,
1992[ISI][Medline].
97.
Rothman, J. E.,
and
L. Orci.
Molecular dissection of the secretory pathway.
Nature
355:
409-415,
1992[ISI][Medline].
98.
Rothman, J. E.,
and
F. T. Wieland.
Protein sorting by transport vesicles.
Science
272:
227-234,
1996[Abstract].
99.
Sabolic, I.,
D. Brown,
A. Stuart-Tilley,
and
S. L. Alper.
Regulation of AE1 anion exchanger and H+-ATPase in rat cortex by acute metabolic acidosis and alkalosis.
Kidney Int.
51:
125-137,
1997[ISI][Medline].
100.
Sabolic, I.,
T. Katsura,
J. M. Verbavatz,
and
D. Brown.
The AQP2 water channel: effect of vasopressin treatment, microtubule disruption, and distribution in neonatal rats.
J. Membr. Biol.
143:
165-175,
1995[ISI][Medline].
101.
Sabolic, I.,
G. Valenti,
J.-M. Verbavatz,
A. N. Van Hoek,
A. S. Verkman,
D. A. Ausiello,
and
D. Brown.
Localization of the CHIP28 water channel in rat kidney.
Am. J. Physiol. Cell Physiol.
263:
C1225-C1233,
1992
102.
Sabolic, I.,
F. Wuarin,
L. B. Shi,
A. S. Verkman,
D. A. Ausiello,
S. Gluck,
and
D. Brown.
Apical endosomes isolated from kidney collecting duct principal cells lack subunits of the proton pumping ATPase.
J. Cell Biol.
119:
111-122,
1992[Abstract].
103.
Sargiacomo, M.,
M. Sudol,
Z. Tang,
and
M. P. Lisanti.
Signal transducing molecules and glycosyl-phosphatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells.
J. Cell Biol.
122:
789-807,
1993[Abstract].
104.
Scheiffele, P.,
J. Peranen,
and
K. Simons.
N-glycans as apical sorting signals in epithelial cells.
Nature
378:
96-98,
1995[ISI][Medline].
105.
Schepens, J.,
E. Cuppen,
B. Wieringa,
and
W. Hendriks.
The neuronal nitric oxide synthase PDZ motif binds to -G(D,E)XV* carboxyterminal sequences.
FEBS Lett.
409:
53-56,
1997[ISI][Medline].
106.
Schroer, T. A.,
and
M. P. Sheetz.
Functions of microtubule-based motors.
Annu. Rev. Physiol.
53:
629-652,
1991[ISI][Medline].
107.
Schwartz, G. J.,
J. Barasch,
and
Q. Al-Awqati.
Plasticity of functional epithelial polarity.
Nature
318:
368-371,
1985[ISI][Medline].
108.
Serafini, T.,
L. Orci,
M. Amherdt,
M. Brunner,
R. A. Kahn,
and
J. E. Rothman.
ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein.
Cell
67:
239-253,
1991[ISI][Medline].
109.
Shaul, P. W.,
and
R. G. Anderson.
Role of plasmalemmal caveolae in signal transduction.
Am. J. Physiol. Lung Cell. Mol. Physiol.
275:
L843-L851,
1998
110.
Sheetz, M. P.
Motor and cargo interactions.
Eur. J. Biochem.
262:
19-25,
1999
111.
Short, D. B.,
K. W. Trotter,
D. Reczek,
S. M. Kreda,
A. Bretscher,
R. C. Boucher,
M. J. Stutts,
and
S. L. Milgram.
An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton.
J. Biol. Chem.
273:
19797-19801,
1998
112.
Simonsen, A.,
R. Lippe,
S. Christoforidis,
J. M. Gaullier,
A. Brech,
J. Callaghan,
B. H. Toh,
C. Murphy,
M. Zerial,
and
H. Stenmark.
EEA1 links PI(3)K function to Rab5 regulation of endosome fusion.
Nature
394:
494-498,
1998[ISI][Medline].
113.
Sly, W. S.,
and
H. D. Fischer.
The phosphomannosyl recognition system for intracellular and intercellular transport of lysosomal enzymes.
J. Cell. Biochem.
18:
67-85,
1982[ISI][Medline].
114.
Stan, R. V.,
W. G. Roberts,
D. Predescu,
K. Ihida,
L. Saucan,
L. Ghitescu,
and
G. E. Palade.
Immunoisolation and partial characterization of endothelial plasmalemmal vesicles (caveolae).
Mol. Biol. Cell.
8:
595-605,
1997[Abstract].
115.
Stetson, D. L.,
and
P. R. Steinmetz.
Role of membrane fusion in CO2 stimulation of proton secretion by turtle bladder.
Am. J. Physiol. Cell Physiol.
245:
C113-C120,
1983
116.
Strange, K.,
M. C. Willingham,
J. S. Handler,
and
H. W. Harris, Jr.
Apical membrane endocytosis via coated pits is stimulated by removal of antidiuretic hormone from isolated, perfused rabbit cortical collecting tubule.
J. Membr. Biol.
103:
17-28,
1988[ISI][Medline].
117.
Taylor, A.
Role of microtubules and microfilaments in the action of vasopressin.
In: Disturbances in Body Fluid Osmolality, edited by T. E. Andreoli,
J. J. Grantham,
and F. C. Rector, Jr.. Bethesda, MD: Am. Physiol. Soc, 1977, chapt. 5, p. 97-124.
118.
Valentijn, K. M.,
F. D. Gumkowski,
and
J. D. Jamieson.
The subapical actin cytoskeleton regulates secretion and membrane retrieval in pancreatic acinar cells.
J. Cell Sci.
112:
81-96,
1999
119.
Van Hoek, A. N.,
C. E. Gustafson,
and
D. Brown.
Label-fracture of aquaporin-2 expressing LLC-PK1 cells: transient appearance of vasopressin-sensitive aquaporins into existing IMP clusters (Abstract).
J. Am. Soc. Nephrol.
9:
27A,
1998.
120.
Van Hoek, A. N.,
M. C. Wiener,
J. M. Verbavatz,
D. Brown,
P. H. Lipniunas,
R. R. Townsend,
and
A. S. Verkman.
Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels.
Biochemistry
34:
2212-2219,
1995[ISI][Medline].
121.
Verhey, K. J.,
J. I. Yeh,
and
M. J. Birnbaum.
Distinct signals in the GLUT4 glucose transporter for internalization and for targeting to an insulin-responsive compartment.
J. Cell Biol.
130:
1071-1079,
1995[Abstract].
122.
Verkman, A. S.,
L. B. Shi,
A. Frigeri,
H. Hasegawa,
J. Farinas,
A. Mitra,
W. Skach,
D. Brown,
H. Van,
A. N. Van Hoek,
and
T. Ma.
Structure and function of kidney water channels.
Kidney Int.
48:
1069-1081,
1995[ISI][Medline].
123.
Vogel, U.,
K. Sandvig,
and
B. van Deurs.
Expression of caveolin-1 and polarized formation of invaginated caveolae in Caco-2 and MDCK II cells.
J. Cell Sci.
111:
825-832,
1998
124.
Walter, P.,
and
V. R. Lingappa.
Mechanism of protein translocation across the endoplasmic reticulum membrane.
Annu. Rev. Cell Biol.
2:
499-516,
1986[ISI].
125.
Wang, S.,
R. W. Raab,
P. J. Schatz,
W. B. Guggino,
and
M. Li.
Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C- terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR).
FEBS Lett.
427:
103-108,
1998[ISI][Medline].
126.
Waters, M. G.,
and
S. R. Pfeffer.
Membrane tethering in intracellular transport.
Curr. Opin. Cell Biol.
11:
453-459,
1999[ISI][Medline].
127.
Weber, T.,
B. V. Zemelman,
J. A. McNew,
B. Westermann,
M. Gmachl,
F. Parlati,
T. H. Sollner,
and
J. E. Rothman.
SNAREpins: minimal machinery for membrane fusion.
Cell
92:
759-772,
1998[ISI][Medline].
128.
Weinman, E. J.,
D. Steplock,
K. Tate,
R. A. Hall,
R. F. Spurney,
and
S. Shenolikar.
Structure-function of recombinant Na/H exchanger regulatory factor (NHE-RF).
J. Clin. Invest.
101:
2199-2206,
1998
129.
Weinman, E. J.,
D. Steplock,
Y. Wang,
and
S. Shenolikar.
Characterization of a protein cofactor that mediates protein kinase A regulation of the renal brush border membrane Na+-H+ exchanger.
J. Clin. Invest.
95:
2143-2149,
1995[ISI][Medline].
130.
Whitney, J. A.,
M. Gomez,
D. Sheff,
T. E. Kreis,
and
I. Mellman.
Cytoplasmic coat proteins involved in endosome function.
Cell
83:
703-713,
1995[ISI][Medline].
131.
Yang, B.,
L. Gonzalez, Jr.,
R. Prekeris,
M. Steegmaier,
R. J. Advani,
and
R. H. Scheller.
SNARE interactions are not selective. Implications for membrane fusion specificity.
J. Biol. Chem.
274:
5649-5653,
1999
132.
Yasui, M.,
S. M. Zelenin,
G. Celsi,
and
A. Aperia.
Adenylate cyclase-coupled vasopressin receptor activates AQP2 promoter via a dual effect on CRE and AP1 elements.
Am. J. Physiol. Renal Physiol.
272:
F443-F450,
1997
133.
Zurzolo, C.,
C. Polistina,
M. Saini,
R. Gentile,
L. Aloj,
G. Migliaccio,
S. Bonatti,
and
L. Nitsch.
Opposite polarity of virus budding and of viral envelope glycoprotein distribution in epithelial cells derived from different tissues.
J. Cell Biol.
117:
551-564,
1992[Abstract].
134.
Zurzolo, C.,
W. van't Hof,
G. van Meer,
and
E. Rodriguez-Boulan.
VIP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphosphatidylinositol-anchored proteins in epithelial cells.
Embo J.
13:
42-53,
1994[Abstract].