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Cited by 206

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

The Docking Stage of Yeast Vacuole Fusion Requires the Transfer of Proteins from a Cis-Snare Complex to a Rab/Ypt Protein

Open access
Price, Albert, Seals, Darren, Wickner, William, Ungermann, Christian·2000·The Journal of Cell Biology

Abstract

The homotypic fusion of yeast vacuoles requires Sec18p (NSF)-driven priming to allow vacuole docking, but the mechanism that links priming and docking is unknown. We find that a large multisubunit protein called the Vam2/6p complex is bound to cis-paired SNAP receptors (SNAREs) on isolated vacuoles. This association of the Vam2/6p complex with the cis-SNARE complex is disrupted during priming. The Vam2/6p complex then binds to Ypt7p, a guanosine triphosphate binding protein of the Rab family, to initiate productive contact between vacuoles. Thus, cis-SNARE complexes can contain Rab/Ypt effectors, and these effectors can be mobilized by NSF/Sec18p-driven priming, allowing their direct association with a Rab/Ypt protein to activate docking.

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Metadata

Authors
Price, A., Seals, D., Wickner, W., & Ungermann, C.
Venue
The Journal of Cell Biology
Published
2000-03-20
Volume
148
Issue
6
Pages
1231-1238
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2045466386
Cited by
206
References
3
FWCI
8.00
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: The Docking Stage of Yeast Vacuole Fusion Requires the Transfer of Proteins from a Cis-Snare Complex to a Rab/Ypt Protein. https://app.cochat.ai/papers/10.1083/jcb.148.6.1231
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Price, A., Seals, D., Wickner, W., & Ungermann, C. (2000). The Docking Stage of Yeast Vacuole Fusion Requires the Transfer of Proteins from a Cis-Snare Complex to a Rab/Ypt Protein. The Journal of Cell Biology. https://doi.org/10.1083/jcb.148.6.1231

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.