Myosin light-chain kinase (MLCK) is an enzyme that phosphorylates the regulatory light chain of myosin, leading to muscle contraction in smooth muscle cells. It plays a crucial role in regulating various cellular processes such as cell migration, cytokinesis, and smooth muscle contraction by modulating the activity of myosin. Dysregulation of MLCK activity has been linked to diseases such as asthma, hypertension, and certain types of cancer.
Calcium binds to the messenger protein Calmodulin. The calcium-calmodulin complex then activates myosin light chain kinase (MLCK), which phosphorylates myosin to allow it to bind to actin - producing contraction.
Myosin makes up the THICK filaments, and actin makes up the thin filaments of myofibrils.
Actin and myosin
The thick protein filaments in a cell are primarily made of a protein called myosin. Myosin filaments are involved in muscle contraction and various other cellular processes such as cell motility and cytokinesis.
Myosin is responsible for actin-based muscular mobility/contraction.
myosin crossbridge binding
Myosin
The release of ADP and P from the myosin heads causes the myosin heads to change shape.
ATP (adenosine triphosphate) is the main substance that causes the myosin head to change shape during muscle contraction. When ATP binds to the myosin head, it energizes the myosin molecule and allows it to detach from actin, resetting the myosin head for the next contraction cycle.
Myosin and Actin
myosin cross-bridges