Myosin-5c (MYO5C)

Myosin-5c is a member of the class V myosin family and functions as a motor protein involved in actin-dependent intracellular transport, especially in epithelial and glandular tissues[1][2][3][5]. It is composed of two heavy chains, each with a motor domain, a neck domain with multiple IQ motifs that bind calmodulin or myosin light chains, a coiled-coil dimerization domain, and a globular tail domain that interacts with cargo adaptors, often Rab family proteins[1][2]. MYO5C is particularly abundant in secretory and epithelial cells (e.g., pancreas, colon, mammary, thyroid)[2][3]. Unlike MYO5A and MYO5B, MYO5C operates as a low duty ratio, non-processive motor, suggesting it is adapted for ensemble-based cargo transport or organelle tethering, rather than individual, long-distance processive transport[1][2][4]. It plays important roles in vesicle transport, secretory granule trafficking, and membrane receptor localization (e.g., transferrin receptor, Rab8, Rab27b)[3][5]. The small molecule pentabromopseudilin is a known inhibitor of MYO5C motor activity, acting allosterically[1][2]. Currently, MYO5C is not recognized as a therapeutic drug target or associated with direct disease modulation, but it is critical for secretory processes in glandular and epithelial cells[2][3][5].

Other names

Unconventional myosin-VcMYO5Cmyosin 5CMGC74969unconventional myosin-Vcmyosin-Vc

Allosteric inhibition of motor function by binding near the actin and nucleotide binding site (PBP)[1][2]