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.
Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension / M. Biancospino, G.R. Buel, C.A. Nino, E. Maspero, R.S. di Perrotolo, A. Raimondi, L. Redlingshofer, J. Weber, F.M. Brodsky, K.J. Walters, S. Polo. - In: NATURE COMMUNICATIONS. - ISSN 2041-1723. - 10:1(2019 Oct). [10.1038/s41467-019-12855-6]
Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension
M. BiancospinoPrimo
;E. Maspero;A. Raimondi;S. Polo
Ultimo
2019
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.File | Dimensione | Formato | |
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