The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
Sec2p Mediates Nucleotide Exchange on Sec4p and Is Involved in Polarized Delivery of Post-Golgi Vesicles
Open accessAbstract
The small GTPase Sec4p is required for vesicular transport at the post-Golgi stage of yeast secretion. Here we present evidence that mutations in SEC2, itself an essential gene that acts at the same stage of the secretory pathway, cause Sec4p to mislocalize as a result of a random rather than a polarized accumulation of vesicles. Sec2p and Sec4p interact directly, with the nucleotide-free conformation of Sec4p being the preferred state for interaction with Sec2p. Sec2p functions as an exchange protein, catalyzing the dissociation of GDP from Sec4 and promoting the binding of GTP. We propose that Sec2p functions to couple the activation of Sec4p to the polarized delivery of vesicles to the site of exocytosis.
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Cited by
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Spatial regulation of the exocyst complex by Rho1 GTPase
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Metadata
- Authors
- Walch-Solimena, C., Collins, R. N., & Novick, P. J.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 1997-06-30
- Volume
- 137
- Issue
- 7
- Pages
- 1495-1509
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2069329269
- Cited by
- 320
- References
- 58
- FWCI
- 6.89
- Type
- journal article
- Language
- en
- Open access
- green
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- Walch-Solimena, C., Collins, R. N., & Novick, P. J. (1997). Sec2p Mediates Nucleotide Exchange on Sec4p and Is Involved in Polarized Delivery of Post-Golgi Vesicles. The Journal of Cell Biology. https://doi.org/10.1083/jcb.137.7.1495
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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