3G9G

Crystal Structure of the N-terminal EFC/F-BAR domain of Syp1

Summary for 3G9G

• Entry DOI: 10.2210/pdb3g9g/pdb
• Related: 3G9H
• Descriptor: Suppressor of yeast profilin deletion (2 entities in total)
• Functional Keywords: syp1, bar domain, fch, adaptor, endocytosis, phosphoprotein
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Bud neck: P25623
• Total number of polymer chains: 1
• Total formula weight: 33487.34

Authors

Reider, A.,Barker, S.,Mishra, S.,Im, Y.J.,Maldonado-Baez, L.,Hurley, J.,Traub, L.,Wendland, B. (deposition date: 2009-02-13, release date: 2009-09-22, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)