Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport Journal Article


Authors: McNew, J. A.; Coe, J. G. S.; Søgaard, M.; Zemelman, B. V.; Wimmer, C.; Hong, W.; Söllner, T. H.
Article Title: Gos1p, a Saccharomyces cerevisiae SNARE protein involved in Golgi transport
Abstract: Specific transport between secretory compartments requires that vesicular carriers contain targeting proteins known as SNAREs. Ten v-SNAREs have been identified in the genome of the yeast Saccharomyces cerevisiae by sequence analysis. We report here the characterization of Gos1p, a v-SNARE localized to the Golgi compartment and likely homolog of the mammalian protein GOS-28/GS28. Gos1p is a type II membrane protein with characteristic SNARE sequence hallmarks and is functionally a SNARE protein. Gos1p was originally identified as a 28 kDa protein in an immunoprecipitate of the cis-Golgi t-SNARE Sed5p. This interaction between Sed5p and Gos1p is direct as demonstrated by in vitro binding with recombinant proteins. Deletion of GOS1 results in viable haploids with modest growth and secretory defects. Close examination of the secretory phenotype of GOS1-disrupted cells suggests that Gos1p may play a role in multiple transport steps, specifically ER-Golgi and/or intra-Golgi transport. Copyright (C) 1998 Federation of European Biochemical Societies.
Keywords: nonhuman; mammalia; cell division; membrane proteins; hela cells; endoplasmic reticulum; saccharomyces cerevisiae; membrane protein; saccharomyces cerevisiae proteins; cell transport; mutagenesis; biological transport; hsp70 heat-shock proteins; golgi complex; fungal proteins; genes, fungal; snare protein; qa-snare proteins; qb-snare proteins; golgi apparatus; active transport; humans; priority journal; article; carboxypeptidase c; golgi transport; carboxypeptidases; gos1p
Journal Title: FEBS Letters
Volume: 435
Issue: 1
ISSN: 0014-5793
Publisher: Wiley Blackwell  
Date Published: 1998-09-11
Start Page: 89
End Page: 95
Language: English
DOI: 10.1016/s0014-5793(98)01044-8
PUBMED: 9755865
PROVIDER: scopus
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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  1. Thomas H Sollner
    65 Sollner
  2. James A Mcnew
    21 McNew
  3. Christian Georg Wimmer
    5 Wimmer