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- W2788838766 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." @default.
- W2788838766 created "2018-03-06" @default.
- W2788838766 creator A5005105101 @default.
- W2788838766 creator A5051681936 @default.
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- W2788838766 date "2018-02-21" @default.
- W2788838766 modified "2023-10-08" @default.
- W2788838766 title "The MYO6 interactome reveals adaptor complexes coordinating early endosome and cytoskeletal dynamics" @default.
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- W2788838766 doi "https://doi.org/10.15252/embr.201744884" @default.
- W2788838766 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5891429" @default.
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