Structure of Myosin VI/Tom1 complex reveals a cargo recognition mode of Myosin VI for tethering.
Myosin VI plays crucial roles in diverse cellular processes. In autophagy, Myosin VI can facilitate the maturation of autophagosomes through interactions with Tom1 and the autophagy receptors, Optineurin, NDP52 and TAX1BP1. Here, we report the high-resolution crystal structure of the C-terminal cargo-binding domain (CBD) of Myosin VI in complex with ... Tom1, which elucidates the mechanistic basis underpinning the specific interaction between Myosin VI and Tom1, and uncovers that the C-terminal CBD of Myosin VI adopts a unique cargo recognition mode to interact with Tom1 for tethering. Furthermore, we show that Myosin VI can serve as a bridging adaptor to simultaneously interact with Tom1 and autophagy receptors through two distinct interfaces. In all, our findings provide mechanistic insights into the interactions of Myosin VI with Tom1 and relevant autophagy receptors, and are valuable for further understanding the functions of these proteins in autophagy and the cargo recognition modes of Myosin VI.
Mesh Terms:
Actin Cytoskeleton, Autophagosomes, Autophagy, Cell Cycle Proteins, Crystallography, X-Ray, HEK293 Cells, HeLa Cells, Humans, Intracellular Signaling Peptides and Proteins, Membrane Transport Proteins, Models, Molecular, Myosin Heavy Chains, Neoplasm Proteins, Nuclear Proteins, Protein Binding, Protein Interaction Domains and Motifs, Proteins, Transcription Factor TFIIIA
Actin Cytoskeleton, Autophagosomes, Autophagy, Cell Cycle Proteins, Crystallography, X-Ray, HEK293 Cells, HeLa Cells, Humans, Intracellular Signaling Peptides and Proteins, Membrane Transport Proteins, Models, Molecular, Myosin Heavy Chains, Neoplasm Proteins, Nuclear Proteins, Protein Binding, Protein Interaction Domains and Motifs, Proteins, Transcription Factor TFIIIA
Nat Commun
Date: Dec. 01, 2018
PubMed ID: 31371777
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