scholarly journals The Exosome Secretory Pathway Transports Amyloid Precursor Protein Carboxyl-terminal Fragments from the Cell into the Brain Extracellular Space

2012 ◽  
Vol 287 (51) ◽  
pp. 43108-43115 ◽  
Author(s):  
Rocio Perez-Gonzalez ◽  
Sebastien A. Gauthier ◽  
Asok Kumar ◽  
Efrat Levy
Keyword(s):  
Amyloid Precursor Protein ◽  
Extracellular Space ◽  
Secretory Pathway ◽  
Precursor Protein ◽  
Carboxyl Terminal ◽  
The Brain ◽  
Brain Extracellular Space

scholarly journals Distinct anterograde trafficking pathways of BACE1 and amyloid precursor protein from the TGN and the regulation of amyloid-β production

2020 ◽  
Vol 31 (1) ◽  
pp. 27-44 ◽  
Author(s):  
Jing Zhi A. Tan ◽  
Lou Fourriere ◽  
Jingqi Wang ◽  
Franck Perez ◽  
Gaelle Boncompain ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Secretory Pathway ◽  
Amyloid Β ◽  
Precursor Protein ◽  
Primary Neurons ◽  
App Processing

The anterograde trafficking of BACE1 and the potential processing of amyloid precursor protein along the secretory pathway remain poorly defined. Our findings reveal that Golgi exit of BACE1 and APP in primary neurons is tightly regulated, resulting in their segregation along different transport routes, which limits APP processing.

scholarly journals APP-BP1, a Novel Protein That Binds to the Carboxyl-terminal Region of the Amyloid Precursor Protein

1996 ◽  
Vol 271 (19) ◽  
pp. 11339-11346 ◽  
Author(s):  
Nienwen Chow ◽  
Julie R. Korenberg ◽  
Xiao-Ning Chen ◽  
Rachael L. Neve
Keyword(s):  
Amyloid Precursor Protein ◽  
Terminal Region ◽  
Precursor Protein ◽  
Carboxyl Terminal ◽  
Novel Protein

scholarly journals Adaptor protein 2–mediated endocytosis of the β-secretase BACE1 is dispensable for amyloid precursor protein processing

2012 ◽  
Vol 23 (12) ◽  
pp. 2339-2351 ◽  
Author(s):  
Yogikala Prabhu ◽  
Patricia V. Burgos ◽  
Christina Schindler ◽  
Ginny G. Farías ◽  
Javier G. Magadán ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Amyloid Precursor Protein ◽  
Secretory Pathway ◽  
Brefeldin A ◽  
Adaptor Protein ◽  
Proteolytic Processing ◽  
Precursor Protein ◽  
Amyloid Precursor Protein Processing ◽  
Intermediate Compartment ◽  
Golgi Network

The β-site amyloid precursor protein (APP)–cleaving enzyme 1 (BACE1) is a transmembrane aspartyl protease that catalyzes the proteolytic processing of APP and other plasma membrane protein precursors. BACE1 cycles between the trans-Golgi network (TGN), the plasma membrane, and endosomes by virtue of signals contained within its cytosolic C-terminal domain. One of these signals is the DXXLL-motif sequence DISLL, which controls transport between the TGN and endosomes via interaction with GGA proteins. Here we show that the DISLL sequence is embedded within a longer [DE]XXXL[LI]-motif sequence, DDISLL, which mediates internalization from the plasma membrane by interaction with the clathrin-associated, heterotetrameric adaptor protein 2 (AP-2) complex. Mutation of this signal or knockdown of either AP-2 or clathrin decreases endosomal localization and increases plasma membrane localization of BACE1. Remarkably, internalization-defective BACE1 is able to cleave an APP mutant that itself cannot be delivered to endosomes. The drug brefeldin A reversibly prevents BACE1-catalyzed APP cleavage, ruling out that this reaction occurs in the endoplasmic reticulum (ER) or ER–Golgi intermediate compartment. Taken together, these observations support the notion that BACE1 is capable of cleaving APP in late compartments of the secretory pathway.

Cytotoxicity mediated by conditional expression of a carboxyl-terminal derivative of the β-amyloid precursor protein

1994 ◽  
Vol 26 (1-2) ◽  
pp. 207-217 ◽  
Author(s):  
Bryce L. Sopher ◽  
Ken-ichiro Fukuchi ◽  
Annette C. Smith ◽  
Kathy A. Leppig ◽  
Clement E. Furlong ◽  
...  
Keyword(s):  
Amyloid Precursor Protein ◽  
Precursor Protein ◽  
Conditional Expression ◽  
Β Amyloid ◽  
Carboxyl Terminal
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