The synaptobrevin homologue Snc2p recruits the exocyst to secretory vesicles by binding to Sec6p
Journal of Cell Biology, ISSN: 0021-9525, Vol: 202, Issue: 3, Page: 509-526
2013
- 43Citations
- 91Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations43
- Citation Indexes43
- 43
- CrossRef41
- Captures91
- Readers91
- 91
Article Description
A screen for mutations that affect the recruitment of the exocyst to secretory vesicles identified genes encoding clathrin and proteins that associate or colocalize with clathrin at sites of endocytosis. However, no significant colocalization of the exocyst with clathrin was seen, arguing against a direct role in exocyst recruitment. Rather, these components are needed to recycle the exocytic vesicle SNAREs Snc1p and Snc2p from the plasma membrane into new secretory vesicles where they act to recruit the exocyst. We observe a direct interaction between the exocyst subunit Sec6p and the latter half of the SNARE motif of Snc2p. An snc2 mutation that specifically disrupts this interaction led to exocyst mislocalization and a block in exocytosis in vivo without affecting liposome fusion in vitro. Overexpression of Sec4p partially suppressed the exocyst localization defects of mutations in clathrin and clathrin-associated components. We propose that the exocyst is recruited to secretory vesicles by the combinatorial signals of Sec4-GTP and the Snc proteins. This could help to confer both specificity and directionality to vesicular traffic. © 2013 Shen et al.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84884239046&origin=inward; http://dx.doi.org/10.1083/jcb.201211148; http://www.ncbi.nlm.nih.gov/pubmed/23897890; https://rupress.org/jcb/article/202/3/509/37391/The-synaptobrevin-homologue-Snc2p-recruits-the; https://dx.doi.org/10.1083/jcb.201211148; http://jcb.rupress.org/content/202/3/509; http://jcb.rupress.org/content/202/3/509.abstract; http://jcb.rupress.org/content/202/3/509.full.pdf; https://rupress.org/jcb/article-pdf/202/3/509/1360488/jcb_201211148.pdf; http://jcb.rupress.org/cgi/doi/10.1083/jcb.201211148; http://jcb.rupress.org/lookup/doi/10.1083/jcb.201211148; http://www.jcb.org/lookup/doi/10.1083/jcb.201211148; https://rupress.org/jcb/article-pdf/202/3/509/699219/jcb_201211148.pdf; http://www.jcb.org/cgi/doi/10.1083/jcb.201211148; http://jcb-dataviewer.rupress.org/jcb/doi/10.1083/jcb.201211148
Rockefeller University Press
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