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Myosin X is an unconventional myosin motor, which is functional as a dimer. The dimerization of myosin X is thought to be antiparallel. [53] This behavior has not been observed in other myosins. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments.
Myosin-9 also known as myosin, heavy chain 9, non-muscle or non-muscle myosin heavy chain IIa (NMMHC-IIA) is a protein which in humans is encoded by the MYH9 gene. [5] [6]Non-muscle myosin IIA (NM IIA) is expressed in most cells and tissues where it participates in a variety of processes requiring contractile force, such as cytokinesis, cell migration, polarization and adhesion, maintenance of ...
Myo10 is a member of an evolutionarily ancient group of myosins whose tails contain MyTH4-FERM domains and that have been shown to have important functions in cellular protrusions based on actin bundles such as filopodia, microvilli, and inner ear stereocilia.
Myosin VIIA is protein that in humans is encoded by the MYO7A gene. [5] Myosin VIIA is a member of the unconventional myosin superfamily of proteins. [ 6 ] Myosins are actin binding molecular motors that use the enzymatic conversion of ATP - ADP + inorganic phosphate (Pi) to provide the energy for movement.
4624 17888 Ensembl ENSG00000197616 ENSMUSG00000040752 UniProt P13533 Q02566 RefSeq (mRNA) NM_002471 NM_001164171 NM_010856 RefSeq (protein) NP_002462 NP_001157643 NP_034986 Location (UCSC) Chr 14: 23.38 – 23.41 Mb Chr 14: 55.18 – 55.2 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Myosin heavy chain, α isoform (MHC-α) is a protein that in humans is encoded by the MYH6 gene ...
Myosin-Ic is a protein that in humans is encoded by the MYO1C gene. [5] [6] This gene encodes a member of the unconventional myosin protein family, which are actin-based molecular motors. The protein is found in the cytoplasm, and one isoform with a unique N-terminus is also found in the nucleus.
Myosin filaments have club-shaped myosin heads that project toward the actin filaments, [1] [3] [5] and provide attachment points on binding sites for the actin filaments. The myosin heads move in a coordinated style; they swivel toward the center of the sarcomere, detach and then reattach to the nearest active site of the actin filament.
The enzyme is composed of three subunits: the catalytic region (protein phosphatase 1, or PP1), the myosin binding subunit (MYPT1), and a third subunit (M20) of unknown function. The catalytic region uses two manganese ions as catalysts to dephosphorylate the light-chains on myosin, which causes a conformational change in the myosin and relaxes ...