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Intracellular Itinerary of Internalised β‐Secretase, BACE1 , and Its Potential Impact on β‐Amyloid Peptide Biogenesis
Author(s) -
Chia Pei Zhi Cheryl,
Toh Wei Hong,
Sharples Robyn,
Gasnereau Isabelle,
Hill Andrew F.,
Gleeson Paul A.
Publication year - 2013
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/tra.12088
Subject(s) - endosome , microbiology and biotechnology , amyloid precursor protein , intracellular , amyloid precursor protein secretase , biogenesis , biology , p3 peptide , alzheimer's disease , biochemistry , gene , medicine , disease , pathology
BACE1 cleavage of the amyloid precursor protein ( APP ) is the initial step in the formation of the amyloidogenic Aβ peptide. This article reports that cell surface BACE1 is internalised by the AP2 /clathrin‐dependent pathway and traffics to early endosomes then recycling endosomes. In contrast, internalised wild‐type APP traffics to late endosomes/lysosomes. A BACE / TGN38 chimera that recycles via the TGN is more efficient in Aβ production than wild‐type BACE1 indicating that the recycling itinerary of BACE1 influences Aβ biogenesis.