Got1p and Sft2p: membrane proteins involved in traffic to the Golgi complex
Open accessAbstract
Traffic through the yeast Golgi complex depends on a member of the syntaxin family of SNARE proteins, Sed5p, present in early Golgi cisternae. Sft2p is a non-essential tetra-spanning membrane protein, found mostly in the late Golgi, that can suppress some sed5 alleles. We screened for mutations that show synthetic lethality with sft2 and found one that affects a previously uncharacterized membrane protein, Got1p, as well as new alleles of sed5 and vps3. Got1p is an evolutionarily conserved non-essential protein with a membrane topology similar to that of Sft2p. Immunofluorescence and subcellular fractionation indicate that it is present in early Golgi cisternae. got1 mutants, but not sft2 mutants, show a defect in an in vitro assay for ER-Golgi transport at a step after vesicle tethering to Golgi membranes. In vivo, inactivation of both Got1p and Sft2p results in phenotypes ascribable to a defect in endosome-Golgi traffic, while their complete removal results in an ER-Golgi transport defect. Thus the presence of either Got1p or Sft2p is required for vesicle fusion with the Golgi complex in vivo. We suggest that Got1p normally facilitates Sed5p-dependent fusion events, while Sft2p performs a related function in the late Golgi.
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The Sed5-Sft2 prediction, together with genetic evidence, suggests SNARE localization or function may involve additional mechanisms via interactions with transmembrane protein regulators.
“this prediction, together with genetic evidence (83), suggests SNARE localization or function may be subject to additional mechanisms via interactions with transmembrane protein regulators.”
From Computed structures of core eukaryotic protein complexes (2021) · cites this paper as [83]
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Computed structures of core eukaryotic protein complexes
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- Authors
- Conchon, S., Cao, X., Barlowe, C., & Pelham, H. R. B.
- Affiliations
- MRC Laboratory of Molecular Biology (GB)
- Dartmouth College (US)
- Corresponding author
- Pelham, Hugh R.B.
- Venue
- The EMBO Journal
- Published
- 1999-07-15
- Volume
- 18
- Issue
- 14
- Pages
- 3934-3946
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC1171469
- OpenAlex
- W2138399917
- Cited by
- 85
- References
- 49
- Citations by year
- 2026: 1 · 2025: 2 · 2023: 5 · 2022: 2 · 2021: 3 · 2020: 5 · 2019: 3 · 2018: 2 · 2017: 5 · 2016: 5 · 2015: 3 · 2014: 1 · 2013: 3 · 2012: 5
- FWCI
- 1.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission
- National Institutes of Health (GM52549)
- National Institute of General Medical Sciences (GM52549)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
- Keywords
- Golgi apparatus, SNARE proteins, vesicle fusion, ER-Golgi transport, synthetic lethality, Saccharomyces cerevisiae, vesicle tethering
- MeSH terms
- Alleles, Amino Acid Sequence, Animals, Biological Transport, Cloning, Molecular, Endoplasmic Reticulum, Fungal Proteins, Genes, Fungal, Genes, Lethal, Genetic Complementation Test, Golgi Apparatus, Membrane Fusion, Membrane Proteins, Molecular Sequence Data, Mutation, Phenotype, Endosomes, Saccharomyces cerevisiae, Conserved Sequence, COS Cells, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Qa-SNARE Proteins
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