Biancospino, M; Buel, GR; Niño, CA; Maspero, E; di Perrotolo, RS; Raimondi, A; Redlingshöfer, L; ... Polo, S; + view all Biancospino, M; Buel, GR; Niño, CA; Maspero, E; di Perrotolo, RS; Raimondi, A; Redlingshöfer, L; Weber, J; Brodsky, FM; Walters, KJ; Polo, S; - view fewer (2019) Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension. Nature Communications , 10 (1) , Article 4974. 10.1038/s41467-019-12855-6.

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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.

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