Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 10, Pages 3820-3825Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1117949109
Keywords
trans-Golgi network; recycling endosomes; exocytosis; epithelial cells; protein sorting
Categories
Funding
- National Institutes of Health [EY08538, GM34107]
- European Molecular Biology Organization
- Dyson Foundation
- Research to Prevent Blindness Foundation
- Eunice Kennedy Shriver National Institute of Child Health and Human Development
Ask authors/readers for more resources
The coxsackie and adenovirus receptor (CAR) plays key roles in epithelial barrier function at the tight junction, a localization guided in part by a tyrosine-based basolateral sorting signal, (318)YNQV(321). Sorting motifs of this type are known to route surface receptors into clathrin-mediated endocytosis through interaction with the medium subunit (mu 2) of the clathrin adaptor AP-2, but how they guide new and recycling membrane proteins basolaterally is unknown. Here, we show that YNQV functions as a canonical YXX Phi motif, with both Y318 and V321 required for the correct basolateral localization and biosynthetic sorting of CAR, and for interaction with a highly conserved pocket in the medium subunits (mu 1A and mu 1B) of the clathrin adaptors AP-1A and AP-1B. Knock-down experiments demonstrate that AP-1A plays a role in the biosynthetic sorting of CAR, complementary to the role of AP-1B in basolateral recycling of this receptor. Our study illustrates how two clathrin adaptors direct basolateral trafficking of a plasma membrane protein through interaction with a canonical YXX Phi motif.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available