6E5N

Solution structure of human Myosin VI isoform 3 (1050-1131) in complex with Clathrin light chain a (46-61)

Summary for 6E5N

• Entry DOI: 10.2210/pdb6e5n/pdb
• NMR Information: BMRB: 30500
• Descriptor: Unconventional myosin-VI, Clathrin light chain A (2 entities in total)
• Functional Keywords: myosin, clathrin, trafficking, endocytosis, motor protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 12365.18

Authors

Buel, G.R.,Walters, K.J. (deposition date: 2018-07-20, release date: 2019-11-20, Last modification date: 2024-05-15)

Primary citation

Biancospino, M.,Buel, G.R.,Nino, C.A.,Maspero, E.,Scotto di Perrotolo, R.,Raimondi, A.,Redlingshofer, L.,Weber, J.,Brodsky, F.M.,Walters, K.J.,Polo, S.
Clathrin light chain A drives selective myosin VI recruitment to clathrin-coated pits under membrane tension.
Nat Commun, 10:4974-4974, 2019

PubMed 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.

PubMed: 31672988
DOI: 10.1038/s41467-019-12855-6

Experimental method

SOLUTION NMR