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- W2105478531 abstract "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 Arf1Delta17N-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 gcs1Delta 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." @default.
- W2105478531 created "2016-06-24" @default.
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- W2105478531 date "2006-04-01" @default.
- W2105478531 modified "2023-10-15" @default.
- W2105478531 title "The Gcs1 Arf-GAP Mediates Snc1,2 v-SNARE Retrieval to the Golgi in Yeast" @default.
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- W2105478531 doi "https://doi.org/10.1091/mbc.e05-09-0832" @default.
- W2105478531 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1415299" @default.
- W2105478531 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16452633" @default.
- W2105478531 hasPublicationYear "2006" @default.
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