MARCKS

Myristoylated alanine-rich C-kinase substrate is a is_associated_with::protein that in humans is encoded by the MARCKS is_associated_with::gene. It plays important roles in cell shape, is_associated_with::cell motility, is_associated_with::secretion, transmembrane transport, and regulation of the is_associated_with::cell cycle. Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin.

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

Interactions
MARCKS has been shown to interact with is_associated_with::TOB1 and with is_associated_with::NMT2.