Calmodulinmyosin

Calmodulinmyosin is a term used to describe a proposed calcium-dependent complex formed between calmodulin and myosin that may regulate motor activity in cells. In this concept, calmodulin, a small calcium-binding protein, binds calcium ions and undergoes a conformational change that enables interaction with myosin. The association is thought to occur with myosin’s regulatory regions, such as the light chain or head domain, potentially influencing ATPase activity and motor function in response to intracellular calcium levels.

In terms of mechanism, calmodulinmyosin would reflect how calcium signaling can modulate contractile or motile processes. In many cells, calcium activates calmodulin, which in turn activates myosin light-chain kinase (MLCK) to phosphorylate the myosin regulatory light chain, thereby enhancing myosin activity. A direct calmodulin–myosin interaction has also been proposed in some contexts, suggesting an additional layer of calcium-responsive regulation that could affect contractility, motility, or cytoskeletal remodeling.

Structure-wise, calmodulin is a two-domain, EF-hand calcium-binding protein, while myosin is a large motor protein with a head, neck, and tail. A calmodulinmyosin complex would presumably involve calcium-activated calmodulin binding to motifs on the myosin molecule, leading to conformational changes that impact function.

The term is not a widely established protein designation in major public databases, and most references to calmodulin’s regulation of myosin are attributed to signaling pathways involving MLCK and related kinases. See also calmodulin, myosin, MLCK, and calcium signaling.