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- W2982612361 abstract "Abstract Clathrin light chains (CLCa and CLCb) are major constituents of clathrin-coated vesicles. Unique functions for these evolutionary conserved paralogs remain elusive, and their role in clathrin-mediated endocytosis in mammalian cells is debated. Here, we find and structurally characterize a direct and selective interaction between CLCa and the long isoform of the actin motor protein myosin VI, which is expressed exclusively in highly polarized tissues. Using genetically-reconstituted Caco-2 cysts as proxy for polarized epithelia, we provide evidence for coordinated action of myosin VI and CLCa at the apical surface where these proteins are essential for fission of clathrin-coated pits. We further find that myosin VI and Huntingtin-interacting protein 1-related protein (Hip1R) are mutually exclusive interactors with CLCa, and suggest a model for the sequential function of myosin VI and Hip1R in actin-mediated clathrin-coated vesicle budding." @default.
- W2982612361 created "2019-11-08" @default.
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- W2982612361 date "2019-10-31" @default.
- W2982612361 modified "2023-10-04" @default.
- W2982612361 title "Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension" @default.
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- W2982612361 doi "https://doi.org/10.1038/s41467-019-12855-6" @default.
- W2982612361 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6823378" @default.
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