LAUSR

Myosin VI is a minus end-directed actin motor protein that fulfils several roles in the cell. The interaction of myosin VI with its cellular cargoes is dictated by the presence of binding domains at the C-terminus of the protein. In this review, we describe how alternative splicing and structural and conformational changes modulate the plasticity of the myosin VI interactome. Recent findings highlight how the various partners can cooperate or compete for binding to allow a precise temporal and spatial regulation of myosin VI recruitment to different cellular compartments, where its motor or anchor function is needed.