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The MYO6 interactome reveals adaptor complexes coordinating early endosome and cytoskeletal dynamics.

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Masters, Thomas A 


The intracellular functions of myosin motors requires a number of adaptor molecules, which control cargo attachment, but also fine-tune motor activity in time and space. These motor-adaptor-cargo interactions are often weak, transient or highly regulated. To overcome these problems, we use a proximity labelling-based proteomics strategy to map the interactome of the unique minus end-directed actin motor MYO6. Detailed biochemical and functional analysis identified several distinct MYO6-adaptor modules including two complexes containing RhoGEFs: the LIFT (LARG-Induced F-actin for Tethering) complex that controls endosome positioning and motility through RHO-driven actin polymerisation; and the DISP (DOCK7-Induced Septin disPlacement) complex, a novel regulator of the septin cytoskeleton. These complexes emphasise the role of MYO6 in coordinating endosome dynamics and cytoskeletal architecture. This study provides the first in vivo interactome of a myosin motor protein and highlights the power of this approach in uncovering dynamic and functionally diverse myosin motor complexes.



BioID, MYO6, endosome, functional proteomics, interactome, Actin Cytoskeleton, Carrier Proteins, Cytoskeleton, Endosomes, Humans, Models, Biological, Multiprotein Complexes, Mutation, Myosin Heavy Chains, Protein Binding, Protein Interaction Mapping, Protein Interaction Maps

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Springer Science and Business Media LLC
Biotechnology and Biological Sciences Research Council (BB/K001981/1)
Medical Research Council (MR/K000888/1)
Isaac Newton Trust (Minute 16.38(a))
Medical Research Council (MR/N000048/1)
Biotechnology and Biological Sciences Research Council (BB/R001316/1)
Wellcome Trust (100140/Z/12/Z)
British Heart Foundation (PG/15/12/31280)
Wellcome Trust (093026/Z/10/Z)