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| myosin II | |
|---|---|
| Name | Myosin II |
| Organism | Homo sapiens |
myosin II is a conventional class of motor protein central to eukaryotic cell contractility, cytokinesis, and motility. It couples ATP hydrolysis to mechanical force generation along actin filaments, playing key roles in processes studied across cell biology, developmental biology, and physiology. Research on myosin II intersects with work at major institutions and in landmark studies that shaped molecular motors and cytoskeletal dynamics.
The hexameric architecture of myosin II consists of two heavy chains and four light chains, with defined motor domains, neck regions and a coiled-coil tail, described in studies from Max Planck Society, Harvard University, Stanford University, Massachusetts Institute of Technology, and University of Cambridge. Mammalian genomes encode multiple heavy chain isoforms such as skeletal, cardiac and nonmuscle variants that were characterized by groups at National Institutes of Health, Cold Spring Harbor Laboratory, Howard Hughes Medical Institute, Yale University, and University of Oxford. Isoform diversity arises from gene families including MYH genes, alternative splicing events reported by teams at European Molecular Biology Laboratory, Wellcome Trust Sanger Institute, Johns Hopkins University, University of California, San Francisco, and University of Tokyo. Structural determination using crystallography and cryo-EM was advanced by collaborations among European Synchrotron Radiation Facility, Argonne National Laboratory, Swiss Light Source, EMBL-EBI, and National Institute of Standards and Technology.
The ATPase-driven conformational cycle couples nucleotide binding, hydrolysis and product release to lever-arm rotation and force production, elaborated in seminal work from laboratories at Nobel Committee, University of California, Berkeley, Columbia University, University of Chicago, and Duke University. Kinetic schemes integrate transient-state measurements from groups at Max Planck Institute for Biophysical Chemistry, Brandeis University, University of Pennsylvania, Princeton University, and Cornell University. Rate-limiting phosphate release and ADP dissociation steps were probed using stopped-flow and single-molecule techniques at Lund University, ETH Zurich, Imperial College London, University of Michigan, and Scripps Research. Comparisons among isoforms informed by datasets from National Center for Biotechnology Information, European Bioinformatics Institute, Broad Institute, Wellcome Trust, and Japanese Society for the Promotion of Science clarified duty ratio and processivity differences.
Myosin II drives contractile ring constriction during cytokinesis, stress fiber contractility, and cortical tension influencing cell migration and morphogenesis, topics advanced by investigators at Rockefeller University, University of California, San Diego, Karolinska Institutet, University of Edinburgh, and Vanderbilt University. In developmental contexts, myosin II activity shapes tissue folding and gastrulation as shown in studies affiliated with European Molecular Biology Laboratory, Princeton University, Harvard Medical School, University of Cambridge, and University of California, Los Angeles. Its roles in wound healing, immune cell migration, and neuronal growth cone dynamics were reported from National Institutes of Health, Kings College London, Mount Sinai Hospital, University of Toronto, and McGill University. Mechanical coupling to adhesion complexes links myosin II function to focal adhesion maturation and mechanotransduction investigated at ETH Zurich, University of Heidelberg, Universidad de Barcelona, Weizmann Institute of Science, and Seoul National University.
Activity is modulated by phosphorylation of regulatory light chains and heavy chain tail regions by kinases such as myosin light chain kinase and Rho-associated kinase, elucidated by teams at NIH Clinical Center, Max Planck Institute, University College London, Yale School of Medicine, and University of Texas Southwestern Medical Center. Phosphatases including myosin phosphatase from studies at Friedrich Miescher Institute, University of Freiburg, Johns Hopkins University, University of California, Irvine, and Brown University counterbalance kinase activity. Other modifications including ubiquitination and SUMOylation were described in reports from Broad Institute, Cold Spring Harbor Laboratory, EMBL, Karolinska Institutet, and Boston Children's Hospital. Signaling pathways involving RhoA, ROCK, MLCK and Ca2+-calmodulin integrate inputs from receptors and second messengers analyzed by researchers at Max Delbrück Center, University of Groningen, National Yang-Ming University, McMaster University, and University of Sydney.
Tail-mediated antiparallel coiled-coil interactions drive bipolar filament assembly, which organizes into higher-order contractile arrays studied with electron microscopy and super-resolution imaging at Lawrence Berkeley National Laboratory, EMBL-EBI, Yale University, University of California, Santa Barbara, and University of Illinois Urbana-Champaign. Interactions with actin, tropomyosin, and crosslinkers like alpha-actinin and filamin were characterized by groups at University of Washington, University of Copenhagen, Cold Spring Harbor Laboratory, Max Planck Institute of Molecular Cell Biology and Genetics, and University of Geneva. Chaperones required for proper folding and assembly were identified in work from NIH, Fred Hutchinson Cancer Center, University of North Carolina at Chapel Hill, Pasteur Institute, and Shanghai Jiao Tong University.
Mutations, misregulation or altered expression of myosin II isoforms are implicated in cardiomyopathies, skeletal myopathies, neuropathies and cancer cell invasion, reported in clinical and basic studies from Mayo Clinic, Cleveland Clinic, Johns Hopkins Hospital, Great Ormond Street Hospital, and Memorial Sloan Kettering Cancer Center. Links to disorders such as hypertrophic cardiomyopathy and myosin storage myopathies emerged from genetic screening consortia at 1000 Genomes Project, ClinVar, Ensembl, DECIPHER Project, and Human Phenotype Ontology. Pharmacological modulation by small molecules and clinical candidates has been pursued in collaborations involving Pfizer, Bristol-Myers Squibb, Novartis, AstraZeneca, and GSK.
Biochemical ATPase assays, in vitro motility assays, optical trapping, single-molecule fluorescence, cryo-electron microscopy and live-cell imaging are core techniques refined at Max Planck Institute for Biophysical Chemistry, HHMI, European Molecular Biology Laboratory, Brookhaven National Laboratory, and Lawrence Livermore National Laboratory. Genetic and genomic approaches including CRISPR, RNAi screens and transcriptomics have been applied by consortia at Broad Institute, Wellcome Sanger Institute, Allen Institute for Brain Science, ENCODE Project Consortium, and GTEx Project. Databases and structural repositories maintained by RCSB PDB, UniProt, EMBL-EBI, NCBI, and Protein Data Bank in Europe support ongoing research.
Category:Motor proteins