Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting

Yosuke Senju, Yuzuru Itoh, Kazunori Takano, Sayaka Hamada, Shiro Suetsugu

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

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 FBAR 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.

Original languageEnglish
Pages (from-to)2032-2040
Number of pages9
JournalJournal of cell science
Volume124
Issue number12
DOIs
Publication statusPublished - Jun 15 2011
Externally publishedYes

Keywords

  • Caveolae
  • EFC domain
  • F-BAR domain
  • Membrane sculpting

ASJC Scopus subject areas

  • Cell Biology

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