A furin-like convertase mediates propeptide cleavage of BACE, the Alzheimer's beta -secretase.

Brian D. Bennett, Paul Denis, Mitsuru Haniu, David B. Teplow, Steve Kahn, Jean-Claude Louis, Martin Citron, and Robert Vassar

Page 37713: Fig. 1, A and B, was incomplete. The corrected figure is shown below.


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Fig. 1.   A, schematic structure of BACE-HA showing signal peptide (SP), propeptide domain (PD), active site motifs (DTG and DSG), transmembrane domain (TM), and hemagglutinin epitope tag (HA). Numbers refer to amino acid positions; asterisks denote N-linked glycosylation sites; and the arrow indicates the D93A active site mutation. The signal peptide and propeptide domain sequence is shown below in brackets, with the underlined RLPR representing the furin recognition motif, and the thin arrow indicating the propeptide domain cleavage site at Glu-46. B, appropriate propeptide cleavage of the active site mutant D93A BACE-HA. D93A BACE-HA from transfected 293 cells labeled with [3H]threonine (left) or [3H]phenylalanine (right) was radiosequenced. The figures show radiactivity in counts/min per sequencing cycle. The D93A BACE-HA radiosequences show a major peak of [3H]threonine in cycle 2 and a major peak of [3H]phenylalanine in cycle 15, consistent with mature BACE starting at Glu-46. Radiosequencing of wild-type BACE reveals the same Glu-46 start site (data not shown). The N-terminal sequence of mature BACE is shown below, with the cycle 2 threonine and the cycle 15 phenylalanine indicated by numbers.





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