MYO1F

MYO1F (Myosin-1F), a member of the myosin superfamily of actin-associated motor proteins, functions as an unconventional myosin involved in membrane-cytoskeleton interactions and intracellular trafficking. Also termed myosin IC or myosin-Ic, it contains a conserved motor domain for actin binding and ATP hydrolysis, coupled with a lipid-binding TH1 domain for membrane anchoring. MYO1F facilitates immune cell motility by regulating actin dynamics at the leading edge of migrating leukocytes, particularly neutrophils, through coordination with adhesion molecules and chemokine signaling. It is implicated in leukocyte adhesion deficiency type III (LAD-III)-like syndromes and inflammatory disorders due to its role in β2-integrin activation. Recent studies highlight its involvement in cancer metastasis via modulation of tumor cell invasiveness. While no MYO1F-targeted therapies are clinically approved, preclinical research explores its potential as a biomarker for immune dysregulation and a therapeutic target for inflammatory diseases. Current investigations focus on small-molecule inhibitors of myosin motor activity to attenuate pathological cell migration.

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Recombinant Human Unconventional myosin-If (MYO1F), partial