Interdependent assembly of specific regulatory lipids and membrane fusion proteins into the vertex ring domain of docked vacuoles
Journal of Cell Biology, ISSN: 0021-9525, Vol: 167, Issue: 6, Page: 1087-1098
2004
- 191Citations
- 51Usage
- 89Captures
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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
- Citations191
- Citation Indexes191
- CrossRef191
- 178
- Usage51
- Downloads42
- Abstract Views9
- Captures89
- Readers89
- 89
Article Description
Membrane microdomains are assembled by lipid partitioning (e.g., rafts) or by protein-protein interactions (e.g., coated vesicles). During docking, yeast vacuoles assemble "vertex" ring-shaped microdomains around the periphery of their apposed membranes. Vertices are selectively enriched in the Rab GTPase Ypt7p, the homotypic fusion and vacuole protein sorting complex (HOPS)-VpsC Rab effector complex, SNAREs, and actin. Membrane fusion initiates at vertex microdomains. We now find that the "regulatory lipids" ergosterol, diacylglycerol and 3- and 4-phosphoinositides accumulate at vertices in a mutually interdependent manner. Regulatory lipids are also required for the vertex enrichment of SNAREs, Ypt7p, and HOPS. Conversely, SNAREs and actin regulate phosphatidylinositol 3-phosphate vertex enrichment. Though the PX domain of the SNARE Vam7p has direct affinity for only 3-phosphoinositides, all the regulatory lipids which are needed for vertex assembly affect Vam7p association with vacuoles. Thus, the assembly of the vacuole vertex ring microdomain arises from interdependent lipid and protein partitioning and binding rather than either lipid partitioning or protein interactions alone.
Bibliographic Details
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=11244258475&origin=inward; http://dx.doi.org/10.1083/jcb.200409068; http://www.ncbi.nlm.nih.gov/pubmed/15611334; https://rupress.org/jcb/article/167/6/1087/51535/Interdependent-assembly-of-specific-regulatory; https://digitalcommons.dartmouth.edu/facoa/1452; https://digitalcommons.dartmouth.edu/cgi/viewcontent.cgi?article=2455&context=facoa; https://dx.doi.org/10.1083/jcb.200409068; http://www.jcb.org/cgi/doi/10.1083/jcb.200409068; https://rupress.org/jcb/article-pdf/167/6/1087/920464/jcb16761087.pdf; http://www.jcb.org/lookup/doi/10.1083/jcb.200409068; http://jcb.rupress.org/lookup/doi/10.1083/jcb.200409068; http://jcb.rupress.org/content/167/6/1087; http://jcb.rupress.org/content/167/6/1087.abstract; http://jcb.rupress.org/content/167/6/1087.full.pdf; http://jcb.rupress.org/cgi/doi/10.1083/jcb.200409068
Rockefeller University Press
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