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Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation
Author(s) -
Reider Amanda,
Barker Sarah L,
Mishra Sanjay K,
Im Young Jun,
MaldonadoBáez Lymarie,
Hurley James H,
Traub Linton M,
Wendland Beverly
Publication year - 2009
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2009.248
Subject(s) - endocytic cycle , signal transducing adaptor protein , biology , microbiology and biotechnology , endocytosis , transmembrane protein , transmembrane domain , internalization , clathrin adaptor proteins , membrane protein , membrane , signal transduction , biochemistry , receptor
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 μ homology domains (μHDs). In vitro and in vivo assays confirmed membrane‐tubulation activity for muniscin EFC/F‐BAR domains. The μHD 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.