Back to Search
Start Over
Masking of Transmembrane-Based Retention Signals Controls ER Export of γ-Secretase.
- Source :
- Traffic; Feb2010, Vol. 11 Issue 2, p250-258, 9p, 1 Color Photograph, 4 Black and White Photographs, 1 Diagram
- Publication Year :
- 2010
-
Abstract
- γ-Secretase is critically involved in the Notch pathway and in Alzheimer's disease. The four subunits of γ-secretase assemble in the endoplasmic reticulum (ER) and unassembled subunits are retained/retrieved to the ER by specific signals. We here describe a novel ER-retention/retrieval signal in the transmembrane domain (TMD) 4 of presenilin 1, a subunit of γ-secretase. TMD4 also is essential for complex formation, conferring a dual role for this domain. Likewise, TMD1 of Pen2 is bifunctional as well. It carries an ER-retention/retrieval signal and is important for complex assembly by binding to TMD4. The two TMDs directly interact with each other and mask their respective ER-retention/retrieval signals, allowing surface transport of reporter proteins. Our data suggest a model how assembly of Pen2 into the nascent γ-secretase complex could mask TMD-based ER-retention/retrieval signals to allow plasma membrane transport of fully assembled γ-secretase. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 13989219
- Volume :
- 11
- Issue :
- 2
- Database :
- Complementary Index
- Journal :
- Traffic
- Publication Type :
- Academic Journal
- Accession number :
- 47285696
- Full Text :
- https://doi.org/10.1111/j.1600-0854.2009.01014.x