| 2006 |
Myo1f-deficient mouse immune cells (neutrophils) exhibit abnormally increased adhesion and reduced motility due to augmented exocytosis of β2 integrin-containing granules; cortical actin co-localizing with Myo1f is reduced in Myo1f-deficient cells, establishing Myo1f as a regulator of cortical actin and integrin trafficking in immune cells. |
Myo1f knockout mouse model, cell adhesion/motility assays, exocytosis measurement, cortical actin imaging |
Science |
High |
17023661
|
| 2019 |
Myo1f interacts physically with the adaptor protein 3BP2 in mast cells; this interaction is modulated by KIT/SCF signaling. Myo1f co-localizes with cortical actin, and Myo1f silencing reduces SCF-dependent mast cell adhesion and migration through fibronectin and decreases surface expression of β1 and β7 integrins. |
Co-immunoprecipitation, shRNA silencing, migration and adhesion assays, flow cytometry, immunofluorescence |
Frontiers in immunology |
Medium |
31143189
|
| 2021 |
MYO1F knockdown in human mast cells reduces IgE-crosslinking- and MRGPRX2-stimulated degranulation; MYO1F is required for full Cdc42 GTPase activation, cortical actin ring reassembly after activation, proper granule localization at the cell membrane, mitochondrial fission, and mitochondrial translocation to exocytic sites; AKT and DRP1 phosphorylation are diminished upon MYO1F knockdown. |
shRNA knockdown, β-hexosaminidase release assay, Cdc42 GTPase activation assay, immunofluorescence, mitochondria imaging, western blot for AKT/DRP1 phosphorylation |
Journal of immunology |
Medium |
33941653
|
| 2021 |
MYO1F acts as an adaptor that recruits both AP2A1 and α-tubulin N-acetyltransferase 1 (α-TAT1) to α-tubulin upon Dectin-1 stimulation, thereby promoting α-tubulin acetylation; this acetylation controls membrane-to-cytoplasm trafficking of SYK and CARD9, which is required for antifungal innate immune gene expression. Myo1f-deficient mice are more susceptible to systemic Candida albicans infection. |
Myo1f knockout mice, co-immunoprecipitation, α-tubulin acetylation assays, SYK/CARD9 trafficking assays, in vivo infection model, inhibitor studies |
Proceedings of the National Academy of Sciences of the United States of America |
High |
34301894
|
| 2023 |
Myo1f deficiency in mice reduces migration of γδT intraepithelial lymphocytes to the small intestine, reduces surface CCR9 and α4β7 integrin expression, impairs polarization of chemokine receptors and integrins, and reduces tyrosine phosphorylation, establishing Myo1f as required for γδT IEL homing and adhesion/migration via integrin and chemokine receptor surface trafficking. |
Myo1f KO mice, in vivo homing assays, in vitro adhesion and migration assays, flow cytometry, immunofluorescence |
Frontiers in immunology |
Medium |
37207213
|
| 2024 |
MYO1F associates with cGAS at the plasma membrane of macrophages; during viral infection, SYK phosphorylates MYO1F, which then recruits lysine acetyltransferase KAT2A to acetylate cGAS at lysines 421, 292, and 131, enabling cGAS activation; membrane-localized cGAS is essential for type I interferon production triggered by virus-cell fusion via Mn2+ release. |
Co-immunoprecipitation, proximity ligation, mutagenesis of phosphorylation/acetylation sites, kinase assays, KO macrophages, viral infection assays, type I IFN measurement |
Molecular cell |
High |
39694035
|
| 2024 |
After TCR stimulation, LCK phosphorylates MYO1F at tyrosines 607 and 634; phosphorylated MYO1F recruits α-TAT1, which acetylates GAPDH at Lys84, 86, and 227, activating GAPDH enzymatic activity and glycolysis required for T-cell effector function. The VAV1-MYO1F fusion protein causes hyperacetylation of GAPDH, aberrant glycolysis, and T-cell proliferation. |
T-cell-specific Myo1f KO mice, site-directed mutagenesis of phosphorylation sites, kinase assay, GAPDH acetylation assay, glycolysis (ECAR) measurement, co-immunoprecipitation, human PTCL patient sample analysis |
Cellular & molecular immunology |
High |
39668163
|
| 2025 |
MYO1F interacts via its SH3 domain with a CASS adaptor module comprising CD2AP, ASAP1, SH3BP2, and SH3KBP1 through multivalent proline-rich motif interactions; a second group of adaptors binds the MYO1F pleckstrin homology (PH) domain; MYO1F and the CASS complex co-localize at actin-rich podosomes and phagocytic cups in macrophages and microglia; MYO1F recruitment to the phagocytic cup requires motor activity and intact PH and SH3 domains. |
In situ proximity labelling proteomics, structural modelling, mutagenesis of SH3/PH domains, immunofluorescence co-localization, functional phagocytosis assays |
Journal of cell science |
High |
41208482
|
| 2025 |
Myo1e and Myo1f localize specifically to the base of podosomes (between podosome core and ventral plasma membrane) in macrophages, primarily via their TH2 domains; knockdown or knockout of Myo1e/f increases podosome size and alters turnover and lateral mobility, indicating a role in attaching core actin filaments to the plasma membrane; Myo1e/f double KO macrophages show reduced 2D and 3D migration despite increased ECM degradation. |
Knockout/knockdown macrophages, live-cell imaging, TIRF microscopy, podosome turnover/mobility assays, 2D/3D migration assays, ECM degradation assay, domain truncation experiments |
bioRxivpreprint |
Medium |
bio_10.1101_2025.04.28.651090
|
| 2025 |
MYO1F normally inhibits neutrophil immunosuppression and proliferation by restraining STAT3 activity; tumor-derived TGF-β1 suppresses Myo1f transcription via SPI1 binding disruption through DNA methylation of intron 8, reducing MYO1F and reprogramming neutrophils into an immunosuppressive state through STAT3-dependent signaling. |
KO/knockdown neutrophil models, STAT3 activity assays, chromatin/methylation analysis, tumor microenvironment functional assays, ICB therapy mouse models |
The Journal of experimental medicine |
Medium |
40202509
|
| 2026 |
Myo1f promotes actin polymerization in monocytes by recruiting EPLINα, which stabilizes F-actin and drives depolymerization of G-actin/MRTFA, causing MRTFA nuclear translocation and transcriptional upregulation of ITGB2 (integrin β2); this mechanism promotes monocyte adhesion to vascular endothelial cells and contributes to atherosclerosis. |
Myo1f KO mice crossed to Apoe-/- atherosclerosis model, bone marrow transplantation, co-immunoprecipitation mass spectrometry, actin polymerization assays, MRTFA nuclear localization imaging, ITGB2 expression assays, MRTFA inhibitor (CCG-1423) treatment |
Redox biology |
Medium |
41610517
|
| 2018 |
A MYO1F p.Gly134Ser mutation (in the motor/ATP-binding domain) causes altered mitochondrial network morphology with increased mitochondrial mass and elevated ROS in thyroid cells; mutant MYO1F confers increased colony formation, invasion, and anchorage-independent growth compared to wild-type MYO1F, and induces proliferation when overexpressed in zebrafish embryos. |
Stable cell line expression of mutant vs. wild-type MYO1F, mitochondrial staining, ROS measurement, colony/invasion assays, zebrafish overexpression model |
International journal of cancer |
Medium |
29672841
|