Calpactin II, also known as S100A10 or p11, is a protein that plays a role in several cellular processes. It is a member of the S100 protein family, which are calcium-binding proteins that regulate numerous activities within cells.
Calpactin II is composed of two subunits and is primarily found in the cytoplasm of various cell types, including epithelial and endothelial cells. It acts as a molecular chaperone, assisting in the folding and stabilization of other proteins. It has been shown to interact with several target proteins, such as annexins and membrane receptors, influencing their function and localization.
One of the key functions of calpactin II is its involvement in the regulation of membrane trafficking and vesicle transport. It has been found to be essential for the correct targeting of vesicles to the plasma membrane, contributing to cell surface receptor recycling and exocytosis. Additionally, calpactin II has been implicated in cell motility and adhesion processes, being involved in the formation of focal adhesions and cytoskeletal rearrangements.
Furthermore, calpactin II has been associated with various pathological conditions. Its overexpression has been observed in certain cancers, and it has been proposed as a potential diagnosis and prognosis marker. In addition, it has been linked to inflammatory diseases and neurodegenerative disorders, suggesting its involvement in the pathophysiology of these conditions.
In summary, calpactin II is a calcium-binding protein that plays a role in several cellular processes, including protein folding, membrane trafficking, cell adhesion, and motility. Its dysregulation has been associated with various diseases, making it an intriguing target for further research and potential therapeutic interventions.
