Journal
JOURNAL OF CELL SCIENCE
Volume 124, Issue 12, Pages 2032-2040Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.086264
Keywords
EFC domain; F-BAR domain; Caveolae; Membrane sculpting
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Funding
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Japan Science and Technology Corporation (J.S.T.)
- Uehara Memorial Foundation
- Mochida Memorial Foundation for Medical and Pharmaceutical Research
- Inamori Foundation
- Grants-in-Aid for Scientific Research [22770185] Funding Source: KAKEN
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Caveolae are flask-shaped invaginations of the plasma membrane that are associated with tumor formation, pathogen entry and muscular dystrophy, through the regulation of lipids, signal transduction and endocytosis. Caveolae are generated by the fusion of caveolin-1-containing vesicles with the plasma membrane, which then participate in endocytosis via dynamin. Proteins containing membrane-sculpting F-BAR (or EFC) domains organize the membrane in clathrin-mediated endocytosis. Here, we show that the F-BAR protein PACSIN2 sculpts the plasma membrane of the caveola. The PACSIN2 F-BAR domain interacts directly with caveolin-1 by unmasking autoinhibition of PACSIN2. Furthermore, the membrane invaginations induced by the PACSIN2 F-BAR domain contained caveolin-1. Knockdown of PACSIN2 resulted in abnormal morphology of caveolin-1-associated plasma membranes, presumably as a result of decreased recruitment of dynamin-2 to caveolin-1. These results indicate that PACSIN2 mediates membrane sculpting by caveolin-1 in caveola morphology and recruits dynamin-2 for caveola fission.
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