Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension.
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.
Mesh Terms:
Actins, Adaptor Proteins, Signal Transducing, Caco-2 Cells, Cell Culture Techniques, Clathrin Light Chains, Clathrin-Coated Vesicles, Coated Pits, Cell-Membrane, Cysts, Endocytosis, Humans, Magnetic Resonance Spectroscopy, Microfilament Proteins, Myosin Heavy Chains, Protein Binding, Protein Conformation, Protein Isoforms
Actins, Adaptor Proteins, Signal Transducing, Caco-2 Cells, Cell Culture Techniques, Clathrin Light Chains, Clathrin-Coated Vesicles, Coated Pits, Cell-Membrane, Cysts, Endocytosis, Humans, Magnetic Resonance Spectroscopy, Microfilament Proteins, Myosin Heavy Chains, Protein Binding, Protein Conformation, Protein Isoforms
Nat Commun
Date: Dec. 31, 2018
PubMed ID: 31672988
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