구.추천논문
- 조회3,640
Abstract
Youngdae Yoon1, Xiuqi Zhang1 and Wonhwa Cho2
From the Department of Chemistry, University of Illinois, Chicago, Illinois 60607
2 To whom correspondence should be addressed: Dept. of Chemistry (M/C 111), University of Illinois, 845 W. Taylor St., Chicago, IL 60607-7061.
1 Both authors contributed equally to this work.
Abstract
Cellular proteins containing Bin/amphiphysin/Rvs (BAR) domains play a key role in clathrin-mediated endocytosis. Despite extensive structural and functional studies of BAR domains, it is still unknown how exactly these domains interact with the plasma membrane containing phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) and whether they function by a universal mechanism or by different mechanisms. Here we report that PtdIns(4,5)P2 specifically induces partial membrane penetration of the N-terminal amphiphilic α-helix (H0) of two representative N-BAR domains from Drosophila amphiphysin (dAmp-BAR) and rat endophilin A1 (EndoA1-BAR). Our quantitative fluorescence imaging analysis shows that PtdIns(4,5)P2-dependent membrane penetration of H0 is important for self-association of membrane-bound dAmp-BAR and EndoA1-BAR and their membrane deformation activity. EndoA1-BAR behaves differently from dAmp-BAR because the former has an additional amphiphilic α-helix that penetrates the membrane in a PtdIns(4,5)P2-independent manner. Depletion of PtdIns(4,5)P2 from the plasma membrane of HEK293 cells abrogated the membrane deforming activity of EndoA1-BAR and dAmp-BAR. Collectively, these studies suggest that the local PtdIns(4,5)P2 concentration in the plasma membrane may regulate the membrane interaction and deformation by N-BAR domain-containing proteins during clathrin-mediated endocytosis.
Endocytosis, Lipids, Membrane Structure, Membrane Trafficking, Phosphoinositides
* This work was supported, in whole or in part, by National Institutes of Health Grant GM68849.
논문정보
- Research article
- 2012년 08월 (BRIC 등록일 2014-09-23)
- 국외 연구진
- 구・추천논문
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