Journal
EMBO REPORTS
Volume 19, Issue 4, Pages -Publisher
WILEY
DOI: 10.15252/embr.201744884
Keywords
BioID; endosome; functional proteomics; interactome; MYO6
Categories
Funding
- Wellcome Trust
- BBSRC [BB/K001981/1]
- Medical Research Council [MR/K000888/1]
- Wellcome Trust [100140, 093026]
- Isaac Newton Trust Cambridge
- BBSRC [BB/K001981/1, BB/R001316/1] Funding Source: UKRI
- MRC [MR/N000048/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/R001316/1, BB/K001981/1] Funding Source: researchfish
- British Heart Foundation [PG/15/12/31280] Funding Source: researchfish
- Medical Research Council [MR/N000048/1, MR/K000888/1] Funding Source: researchfish
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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 invivo 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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