Journal
TRENDS IN CELL BIOLOGY
Volume 18, Issue 9, Pages 397-404Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2008.06.007
Keywords
-
Categories
Funding
- National Institutes of Health [GM54712]
- G. Harold and Leila Y. Mathers Charitable Foundation
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM054712] Funding Source: NIH RePORTER
Ask authors/readers for more resources
Temporal and spatial regulation of membrane-trafficking events is crucial to both membrane identity and overall cell polarity. Small GTPases of the Rab, Rai and Rho protein families have been implicated as important regulators of vesicle docking and fusion events. This review focuses on how these GTPases interact with the exocyst complex, which is a multi-subunit tethering complex involved in the regulation of cell-surface transport and cell polarity. The Rab and Rai GTPases are thought to function in exocyst assembly and vesicle-tethering processes, whereas the Rho family GTPases seem to function in the local activation of the exocyst complex to facilitate downstream vesicle-fusion events. The localized activation of the exocyst by Rho GTPases is likely to have an important role in spatial regulation of exocytosis.
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