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The MYO6 interactome using BioID

ABSTRACT: The intracellular function 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 (BioID) to map the interactome of the unique minus end-directed actin motor MYO6. Our analysis identified several distinct MYO6-adaptor modules including two complexes containing RHO GEFs which we screened using further BioID baits (LRCH3, DOCK7, GIPC1 and ARHGEF12). These complexes emphasise the multifunctionality of MYO6 provides the first in vivo interactome of a myosin motor protein, highlighting the power of this approach in uncovering dynamic and functionally diverse myosin motor complexes.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Retinal Pigment Epithelial Cell

DISEASE(S): Disease Free

SUBMITTER: Tom O'Loughlin

LAB HEAD: Dr. Folma Buss

PROVIDER: PXD008686 | Pride | 2018-02-27

REPOSITORIES: Pride

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			Action	DRS
	BirA_190517_070617.raw	Raw
	BirA_27336.raw	Raw
	BirA_27337.raw	Raw
	BirA_27338.raw	Raw
	BirA_280517_070617.raw	Raw

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Publications

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

O'Loughlin Thomas T Masters Thomas A TA Buss Folma F

EMBO reports 20180221 4

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 m ...[more]

PMID: 29467281

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