ArticleThe Journal of biological chemistry2010
Myosin 1G is an abundant class I myosin in lymphocytes whose localization at the plasma membrane depends on its ancient divergent pleckstrin homology (PH) domain (Myo1PH).
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 68 citations in OpenAlex.
- Myo1g Mediates NKR-P1C Expression in Primary Mouse NK Cells and Participates in Cytotoxicity.Immunology · 2026Article
- Tobacco Smoke Exposure From Prenatal To Adolescent Periods Drives IBD Pathogenesis: Dynamic DNA Methylation Signatures Across Lifespan Stages.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Myosin Class I Genes Follow a Cell Type-Specific Transcription Pattern in Human Haematopoietic Cell Lines.International journal of molecular sciences · 2026Article
- The MYO1F interactome reveals ASAP1, CD2AP and SH3KBP1 as novel adaptor proteins in podosomes and phagosomes.Journal of cell science · 2025Article
- MYO1G promoter hypomethylation correlates with its mRNA expression, lymphocyte infiltration, and immunotherapy response in melanoma.Frontiers in oncology · 2025Article
- Class I Myosins, molecular motors involved in cell migration and cancer.Cell adhesion & migration · 2022Article
- Review
- Detection of Myosin 1g Overexpression in Pediatric Leukemia by Novel Monoclonal Antibodies.International journal of molecular sciences · 2022Article
- Article
- Myo1g is required for efficient adhesion and migration of activated B lymphocytes to inguinal lymph nodes.Scientific reports · 2021Article
- Myosin 1g and 1f: A Prospective Analysis in NK Cell Functions.Frontiers in immunology · 2021Review
- Long-Tailed Unconventional Class I Myosins in Health and Disease.International journal of molecular sciences · 2020Review
- Basic-hydrophobic sites are localized in conserved positions inside and outside of PH domains and affect localization ofMolecular biology of the cell · 2020Article
- The Expressions and Mechanisms of Sarcomeric Proteins in Cancers.Disease markers · 2020Review
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Article
- Roles of Myosin-Mediated Membrane Trafficking in TGF-β Signaling.International journal of molecular sciences · 2019Review
- Adhesion force and attachment lifetime of the KIF16B-PX domain interaction with lipid membranes.Molecular biology of the cell · 2017Article
- The dynamics of smoking-related disturbed methylation: a two time-point study of methylation change in smokers, non-smokers and former smokers.BMC genomics · 2017Article
- Myosin-1 inhibition by PClP affects membrane shape, cortical actin distribution and lipid droplet dynamics in early Zebrafish embryos.PloS one · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Class I myosins, which link F-actin to membrane, are largely undefined in lymphocytes. Mass spectrometric analysis of lymphocytes identified two short tail forms: (Myo1G and Myo1C) and one long tail (Myo1F). We investigated Myo1G, the most abundant in T-lymphocytes, and compared key findings with Myo1C and Myo1F. Myo1G localizes to the plasma membrane and associates in an ATP-releasable manner to the actin-containing insoluble pellet. The IQ+tail region of Myo1G (Myo1C and Myo1F) is sufficient for membrane localization, but membrane localization is augmented by the motor domain. The minimal region lacks IQ motifs but includes: 1) a PH-like domain; 2) a "Pre-PH" region; and 3) a "Post-PH" region. The Pre-PH predicted alpha helices may contribute electrostatically, because two conserved basic residues on one face are required for optimal membrane localization. Our sequence analysis characterizes the divergent PH domain family, Myo1PH, present also in long tail myosins, in eukaryotic proteins unrelated to myosins, and in a probable ancestral protein in prokaryotes. The Myo1G Myo1PH domain utilizes the classic lipid binding site for membrane association, because mutating either of two basic residues in the "signature motif" destroys membrane localization. Mutation of each basic residue of the Myo1G Myo1PH domain reveals another critical basic residue in the beta3 strand, which is shared only by Myo1D. Myo1G differs from Myo1C in its phosphatidylinositol 4,5-bisphosphate dependence for membrane association, because membrane localization of phosphoinositide 5-phosphatase releases Myo1C from the membrane but not Myo1G. Thus Myo1PH domains likely play universal roles in myosin I membrane association, but different isoforms have diverged in their binding specificity.
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Registered trials
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