The MYO6 interactome reveals adaptor complexes coordinating early endosome and cytoskeletal dynamics.
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Peer-reviewed
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Abstract
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.
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1469-3178
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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)