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Myristoylated alanine-rich protein kinase C substrate (MARCKS) is a highly conserved, membrane-associated protein that plays a central role in the regulation of the actin cytoskeleton and various cellular processes. It regulates actin filament crosslinking and structural modulation of the actin cytoskeleton, impacting cell shape, motility, chemotaxis, adhesion, phagocytosis, exocytosis, and endo/exocytosis in neurons and other cells. It also sequesters phosphatidylinositol-4,5-bisphosphate (PIP2) at lipid rafts in quiescent cells; PKC-mediated phosphorylation releases PIP2 for signaling functions such as immune response modulation. It plays roles in neural development including neurite outgrowth and synaptic plasticity, and is also involved in vesicle/granule exocytosis.
Phosphorylation by PKC or binding to calcium-calmodulin inhibits MARCKS association with both actin filaments and plasma membrane.
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