Myosin-1F (MYO1F)

Myosin-1F (MYO1F) is a long-tailed unconventional class I myosin motor protein primarily expressed in immune cells, including neutrophils, macrophages, mast cells, and T lymphocytes[1][2][4][5]. It contains a motor domain that binds actin and hydrolyzes ATP, followed by a neck region with an IQ domain, and a tail that includes pleckstrin homology (PH), tail homology 1 (TH1), tail homology 2 (TH2), and Src homology 3 (SH3) domains, facilitating protein-protein interactions, membrane binding, and cytoskeletal remodeling[1][2][4]. MYO1F is localized near the plasma membrane, co-localizes with cortical actin, and interacts with phosphoinositides, playing crucial roles in regulating integrin expression and adhesion molecule trafficking, facilitating immune cell migration and cytotoxic synapse formation. Deficiency or dysfunction of MYO1F impairs proper leukocyte migration, reduces adhesion molecule regulation, and is implicated in increased susceptibility to infection, altered inflammatory responses, and potentially tumor progression through changes in cell migration and adhesion. Recent research links MYO1F to neuroinflammation through its regulation of the MAPK and AKT pathways in activated microglia[3]. No specific drugs are currently described to directly interact with MYO1F.

Other names

Myosin IFMYO1FUnconventional myosin-IfMyosin-IfMyosin-Iemyosin-ID

Not established for any drugs; mechanistic data relate to interactions with cytoskeletal and signaling pathways (e.g., integrins, 3BP2, Cdc42, Vav1)