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- W1976750249 abstract "Epsins are endocytic proteins with a structured epsin N-terminal homology (ENTH) domain that binds phosphoinositides and a poorly structured C-terminal region that interacts with ubiquitin and endocytic machinery, including clathrin and endocytic scaffolding proteins. Yeast has two redundant genes encoding epsins, ENT1 and ENT2 ; deleting both genes is lethal. We demonstrate that the ENTH domain is both necessary and sufficient for viability of ent1 Δ ent2 Δ cells. Mutational analysis of the ENTH domain revealed a surface patch that is essential for viability and that binds guanine nucleotide triphosphatase-activating proteins for Cdc42, a critical regulator of cell polarity in all eukaryotes. Furthermore, the epsins contribute to regulation of specific Cdc42 signaling pathways in yeast cells. These data support a model in which the epsins function as spatial and temporal coordinators of endocytosis and cell polarity." @default.
- W1976750249 created "2016-06-24" @default.
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- W1976750249 date "2006-03-06" @default.
- W1976750249 modified "2023-09-26" @default.
- W1976750249 title "Epsin N-terminal homology domains perform an essential function regulating Cdc42 through binding Cdc42 GTPase-activating proteins" @default.
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- W1976750249 doi "https://doi.org/10.1073/pnas.0510513103" @default.
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