3G9H

Crystal structure of the C-terminal mu homology domain of Syp1

3G9H の概要

• エントリーDOI: 10.2210/pdb3g9h/pdb
• 関連するPDBエントリー: 3G9G
• 分子名称: Suppressor of yeast profilin deletion, 2-(2-{2-[2-(2-METHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHANOL (3 entities in total)
• 機能のキーワード: syp1, mu, adaptor, endocytosis, phosphoprotein
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Bud neck: P25623
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35943.54

構造登録者

Reider, A.,Barker, S.,Mishra, S.,Im, Y.J.,Maldonado-Baez, L.,Hurley, J.,Traub, L.,Wendland, B. (登録日: 2009-02-13, 公開日: 2009-09-22, 最終更新日: 2024-02-21)

主引用文献

Reider, A.,Barker, S.L.,Mishra, S.K.,Im, Y.J.,Maldonado-Baez, L.,Hurley, J.H.,Traub, L.M.,Wendland, B.
Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.
Embo J., 28:3103-3116, 2009

PubMed Abstract: 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 (muHDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The muHD 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.

PubMed: 19713939
DOI: 10.1038/emboj.2009.248

実験手法

X-RAY DIFFRACTION (2.8 Å)