ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation.

Loading...
Thumbnail Image

Date

2005-01-17

Journal Title

Journal ISSN

Volume Title

Repository Usage Stats

223
views
200
downloads

Citation Stats

Abstract

Examining how key components of coat protein I (COPI) transport participate in cargo sorting, we find that, instead of ADP ribosylation factor 1 (ARF1), its GTPase-activating protein (GAP) plays a direct role in promoting the binding of cargo proteins by coatomer (the core COPI complex). Activated ARF1 binds selectively to SNARE cargo proteins, with this binding likely to represent at least a mechanism by which activated ARF1 is stabilized on Golgi membrane to propagate its effector functions. We also find that the GAP catalytic activity plays a critical role in the formation of COPI vesicles from Golgi membrane, in contrast to the prevailing view that this activity antagonizes vesicle formation. Together, these findings indicate that GAP plays a central role in coupling cargo sorting and vesicle formation, with implications for simplifying models to describe how these two processes are coupled during COPI transport.

Department

Description

Provenance

Citation

Published Version (Please cite this version)

10.1083/jcb.200404008

Publication Info

Lee, SY, JS Yang, W Hong, RT Premont and VW Hsu (2005). ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation. J Cell Biol, 168(2). pp. 281–290. 10.1083/jcb.200404008 Retrieved from https://hdl.handle.net/10161/10775.

This is constructed from limited available data and may be imprecise. To cite this article, please review & use the official citation provided by the journal.


Unless otherwise indicated, scholarly articles published by Duke faculty members are made available here with a CC-BY-NC (Creative Commons Attribution Non-Commercial) license, as enabled by the Duke Open Access Policy. If you wish to use the materials in ways not already permitted under CC-BY-NC, please consult the copyright owner. Other materials are made available here through the author’s grant of a non-exclusive license to make their work openly accessible.