Journal
JOURNAL OF CELL BIOLOGY
Volume 172, Issue 1, Pages 55-66Publisher
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200510016
Keywords
-
Categories
Funding
- NCI NIH HHS [CA 46128, P01 CA046128] Funding Source: Medline
- NCRR NIH HHS [P41 RR011823, P41 RR11823-10] Funding Source: Medline
- NIGMS NIH HHS [GM 35370, R37 GM035370, R01 GM035370, R01 GM054712, R01GM54712] Funding Source: Medline
Ask authors/readers for more resources
Rab guanosine triphosphatases regulate intracellular membrane traffic by binding specific effector proteins. The yeast Rab Sec4p plays multiple roles in the polarized transport of post-Golgi vesicles to, and their subsequent fusion with, the plasma membrane, suggesting the involvement of several effectors. Yet, only one Sec4p effector has been documented to date: the exocyst protein Sec15p. The exocyst is an octameric protein complex required for tethering secretory vesicles, which is a prerequisite for membrane fusion. In this study, we describe the identification of a second Sec4p effector, Sro7p, which is a member of the lethal giant larvae tumor suppressor family. Sec4-GTP binds to Sro7p in cell extracts as well as to purified Sro7p, and the two proteins can be coimmunoprecipitated. Furthermore, we demonstrate the formation of a ternary complex of Sec4-GTP, Sro7p, and the t-SNARE Sec9p. Genetic data support our conclusion that Sro7p functions downstream of Sec4p and further imply that Sro7p and the exocyst share partially overlapping functions, possibly in SNARE regulation.
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