Class VI myosin, motor domain (IPR036114)

Short name: MYSc_Myo6

Overlapping homologous superfamilies

Domain relationships


Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model [PMID: 22940248, PMID: 20094053]. Myosin VI mediates cargo transport and also serves as an anchor that supports cellular architectures by physically connecting cytoskeletons with its binding targets, such as membranes. It has being implicated in a myriad of functions: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis, playing roles in deafness and retinal development among others [PMID: 17187061, PMID: 15146066, PMID: 23340379, PMID: 24106123]. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homologue 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments [PMID: 20094053].

Myosin VI contains an N-terminal motor domain followed by a short neck (also called the lever arm), a hypothetical coiled-coil domain in the middle, and a C-terminal globular cargo-binding domain (CBD) [PMID: 19665975]. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.