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Biophyschem/Sandbox

MARCKS (myristoylated alanine-rich C-kinase substrate) is a 32 kDa protein that interacts with both Ca2+/calmodulin and protein kinase C. MARCKS was first discovered in 1982 as a substrate for PKC. As such, MARCKS is also involved in growth control, differentiation, secretion and metabolism. It has also been determined that MARCKS is implicated in regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and neurosecretion.

MARCKS proteins (myristoylated alanine-rich C-kinase substrate) play important roles in cell shape, cell motility, secretion, transmembrane transport, and regulation of the cell cycle. Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin.

They are acidic proteins with high proportions of alanine, glycine, proline, and glutamic acid. They are membrane-bound through a lipid anchor at the N-terminus, and a polybasic domain in the middle. They are regulated by Ca2+/calmodulin and protein kinase C. In their unphosphorylated form, they bind to actin filaments, causing them to crosslink, and sequester acidic membrane phospholipids such as PIP2.

Category:Peripheral membrane proteins