JCB logo
Keystone Symposia
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 3 January 2006. doi:10.1083/jcb.200510016
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 1, 55-66
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Grosshans, B. L.
Right arrow Articles by Novick, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Grosshans, B. L.
Right arrow Articles by Novick, P.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p

Bianka L. Grosshans1, Anna Andreeva2, Akanksha Gangar2, Sherry Niessen3,4,5, John R. Yates, III3,4,5, Patrick Brennwald2, and Peter Novick1

1 Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520
2 Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599
3 Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037
4 Department of Chemistry, The Scripps Research Institute, La Jolla, CA 92037
5 The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037

Correspondence to Peter Novick: peter.novick{at}yale.edu

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.

Abbreviations used in this paper: GEF, guanine nucleotide exchange factor; GDP, guanosine 5'-diphosphate; lgl, lethal giant larvae; SC, synthetic complete; YPD, yeast peptone dextrose.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents