Related Experiment Video
Updated: Feb 14, 2026

Wholemount Immunohistochemistry for Revealing Complex Brain Topography
Published on: April 5, 2012
The MYO6 interactome reveals adaptor complexes coordinating early endosome and cytoskeletal dynamics
Thomas O'Loughlin1, Thomas A Masters2, Folma Buss1
1Cambridge Institute for Medical Research, Wellcome Trust/MRC Building, Cambridge, UK to277@cam.ac.uk fb207@cam.ac.uk.
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.
Related Concept Videos
Cytoskeletal Coordination in Cell Migration
Coordination Number and Geometry
Coordination Compounds and Nomenclature
Maturation of Endosomes
Changes in location
The maturing endosome moves along microtubules from the periphery of the cell towards the perinuclear region. This movement of the...
Lattice Centering and Coordination Number
Types of Unit Cells
Imagine taking a large number of identical...
The Early Endosome: Endocytosis of Transferrin

