MYO1F is an unconventional class I myosin that serves as a critical regulator of immune cell function and metabolism. In T cells, MYO1F undergoes LCK-mediated phosphorylation at tyrosines 607 and 634 upon TCR stimulation, promoting α-TAT1-mediated acetylation of GAPDH at lysines 84, 86, and 227, which is essential for glycolytic metabolism and T-cell activation 1. The protein functions as a motor protein that positions cGAS at the plasma membrane, where SYK-mediated phosphorylation facilitates KAT2A recruitment for cGAS acetylation, crucial for innate immune signaling and type I interferon production during viral infection 2. MYO1F regulates neutrophil function through STAT3 pathway modulation, with its downregulation by tumor-derived TGF-β1 promoting immunosuppressive neutrophil states that impair immune checkpoint blockade therapy 3. In macrophages and microglia, MYO1F associates with SH3-domain adaptor proteins including CD2AP, ASAP1, and SH3KBP1, localizing to podosomes and phagocytic cups where it regulates phagocytosis 4. The protein also controls filopodia formation, with Taspase1-mediated proteolysis serving as a regulatory mechanism 5. MYO1F expression is elevated in neurodegeneration-associated microglia and serves as a biomarker for coronary artery disease 67.