Cited by 425Cellular transport and secretionFungal and yeast genetics researchAutophagy in Disease and Therapy

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New Component of the Vacuolar Class C-Vps Complex Couples Nucleotide Exchange on the Ypt7 Gtpase to Snare-Dependent Docking and Fusion

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Wurmser, Andrew E., Sato, Trey K., Emr, Scott D.·2000·The Journal of Cell Biology

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Abstract

The class C subset of vacuolar protein sorting (Vps) proteins (Vps11, Vps18, Vps16 and Vps33) assembles into a vacuole/prevacuole-associated complex. Here we demonstrate that the class C-Vps complex contains two additional proteins, Vps39 and Vps41. The COOH-terminal 148 amino acids of Vps39 direct its association with the class C-Vps complex by binding to Vps11. A previous study has shown that a large protein complex containing Vps39 and Vps41 functions as a downstream effector of the active, GTP-bound form of Ypt7, a rab GTPase required for the fusion of vesicular intermediates with the vacuole (Price, A., D. Seals, W. Wickner, and C. Ungermann. 2000. J. Cell Biol. 148:1231–1238). Here we present data that indicate that this complex also functions to stimulate nucleotide exchange on Ypt7. We show that Vps39 directly binds the GDP-bound and nucleotide-free forms of Ypt7 and that purified Vps39 stimulates nucleotide exchange on Ypt7. We propose that the class C-Vps complex both promotes Vps39-dependent nucleotide exchange on Ypt7 and, based on the work of Price et al., acts as a Ypt7 effector that tethers transport vesicles to the vacuole. Thus, the class C-Vps complex directs multiple reactions during the docking and fusion of vesicles with the vacuole, each of which contributes to the overall specificity and efficiency of this transport process.

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Authors: Wurmser, A. E., Sato, T. K., & Emr, S. D.
Affiliations: Howard Hughes Medical Institute (US)
ORCID: Sato, Trey K.
Emr, Scott D.
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2000-10-30
Volume: 151
Issue: 3
Pages: 551-562
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.151.3.551
PMC: PMC2185595
OpenAlex: W2132005005
Cited by: 425
References: 48
Citations by year: 2026: 4 · 2025: 8 · 2024: 10 · 2023: 12 · 2022: 7 · 2021: 12 · 2020: 10 · 2019: 13 · 2018: 8 · 2017: 16 · 2016: 16 · 2015: 15 · 2014: 23 · 2013: 17 · 2012: 28
FWCI: 8.09
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01ca058689-10)
National Cancer Institute (CA 58689)
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 › Cell Biology › Autophagy in Disease and Therapy
Keywords: VPS39, VPS41, Ypt7, Rab GTPases, nucleotide exchange, vacuole fusion, vesicle docking, SNARE proteins, vacuolar protein sorting, yeast vacuole, protein complex formation
MeSH terms: Amino Acid Sequence, Biological Transport, Carrier Proteins, Fungal Proteins, Guanosine Triphosphate, Membrane Fusion, Membrane Proteins, Models, Biological, Molecular Sequence Data, Mutation, Nuclear Proteins, Protein Binding, Saccharomyces cerevisiae, Substrate Specificity, Vacuoles, Sequence Alignment, RNA-Binding Proteins, Conserved Sequence, Protein Structure, Tertiary, Genes, Essential, rab GTP-Binding Proteins, Two-Hybrid System Techniques, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, Adaptor Proteins, Vesicular Transport, Macromolecular Substances, SNARE Proteins

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New Component of the Vacuolar Class C-Vps Complex Couples Nucleotide Exchange on the Ypt7 Gtpase to Snare-Dependent Docking and Fusion

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