Myosin
superfamily of motor proteins

Myosins () are a family of motor proteins (though most often protein complexes) best known for their roles in muscle contraction and in a wide range of other motility processes in eukaryotes. They are ATP-dependent and responsible for actin-based motility.
The first myosin (M2) to be discovered was in 1864 by Wilhelm Kühne. Kühne had extracted a viscous protein from skeletal muscle that he held responsible for keeping the tension state in muscle. He called this protein myosin. The term has been extended to include a group of similar ATPases found in the cells of both striated muscle tissue and smooth muscle tissue.
Following the discovery in 1973 of enzymes with myosin-like function in Acanthamoeba castellanii, a global range of divergent myosin genes have been discovered throughout the realm of eukaryotes.
Although myosin was originally thought to be restricted to muscle cells (hence myo-(s) + -in), there is no single "myosin"; rather it is a very large superfamily of genes whose protein products share the basic properties of actin binding, ATP hydrolysis (ATPase enzyme activity), and force transduction. Virtually all eukaryotic cells contain myosin isoforms. Some isoforms have specialized functions in certain cell types (such as muscle), while other isoforms are ubiquitous.
The public source identifies “Myosin” as superfamily of motor proteins. This brief keeps that definition visible, then builds a research path around Myosin, superfamily and motor.
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This entry incorporates text from “Myosin” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.