期刊
EMBO JOURNAL
卷 28, 期 20, 页码 3103-3116出版社
WILEY
DOI: 10.1038/emboj.2009.248
关键词
adaptor; endocytosis; F-BAR; mu HD; Syp1
资金
- U. S. DOE, Basic Energy Sciences, Office of Science [W-31-109-Eng-38]
- NIH [R01 GM60979, R01 DK53249, GM07231]
- Ford Foundation Diversity Fellowship
Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N-terminal domain homologous to the crescent-shaped membrane-tubulating EFC/F-BAR domains and a C-terminal domain homologous to cargo-binding mu homology domains (mu HDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The mu HD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane-tubulation activity that is important for regulating endocytosis. The EMBO Journal (2009) 28, 3103-3116. doi: 10.1038/emboj. 2009.248; Published online 27 August 2009
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据