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Vol. 17, Issue 4, 1845-1858, April 2006

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The Gcs1 Arf-GAP Mediates Snc1,2 v-SNARE Retrieval to the Golgi in Yeast

Micah Robinson ^*, Pak Phi Poon , Christina Schindler , Lois E. Murray , Rachel Kama ^*, Galina Gabriely ^*, Richard A. Singer , Anne Spang , Gerald C. Johnston , and Jeffrey E. Gerst ^*

^* Department of Molecular Genetics, Weizmann Institute of Science, Rehovot 76100, Israel; Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada; Friedrich Miescher Laboratory, Max Planck Society, D-72076 Tuebingen, Germany; and Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada

Submitted September 7, 2005; Revised January 19, 2006; Accepted January 23, 2006
Monitoring Editor: Akihiko Nakano

Gcs1 is an Arf GTPase-activating protein (Arf-GAP) that mediates Golgi-ER and post-Golgi vesicle transport in yeast. Here we show that the Snc1,2 v-SNAREs, which mediate endocytosis and exocytosis, interact physically and genetically with Gcs1. Moreover, Gcs1 and the Snc v-SNAREs colocalize to subcellular structures that correspond to the trans-Golgi and endosomal compartments. Studies performed in vitro demonstrate that the Snc-Gcs1 interaction results in the efficient binding of recombinant Arf117N-Q71L to the v-SNARE and the recruitment of purified coatomer. In contrast, the presence of Snc had no effect on Gcs1 Arf-GAP activity in vitro, suggesting that v-SNARE binding does not attenuate Arf1 function. Disruption of both the SNC and GCS1 genes results in synthetic lethality, whereas overexpression of either SNC gene inhibits the growth of a distinct subset of COPI mutants. We show that GFP-Snc1 recycling to the trans-Golgi is impaired in gcs1 cells and these COPI mutants. Together, these results suggest that Gcs1 facilitates the incorporation of the Snc v-SNAREs into COPI recycling vesicles and subsequent endosome-Golgi sorting in yeast.

Address correspondence to: Jeffrey E. Gerst (jeffrey.gerst{at}weizmann.ac.il).

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