Overview:

Myristoylated Alanine-Rich C Kinase Substrate (MARCKS) is a member of a family of calmodulin binding proteins thatis a target for phosphorylation by protein kinase C (PKC) (1). MARCKS is concentrated in the synapses of neurons where it appears to function in synaptic vesicle cycling. MARCKS has been shown to bind both actin and calmodulin in vitro (2). Deletion of the MARCKS gene in mice results in embryonic brain defects and death (3). Phosphorylation of Ser152/156 modulates the binding of MARCKS to calmodulin (4).

References:

1. Ouimet, C C. et al: Localization of the MARCKS (87 kDa) protein, a major specific substrate for protein kinase C, in rat brain. 1990 J Neurosci 10:1683-1698.2. Hartwig J H. et al: MARCKS is an a ctin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. Nature 1993356: 618-622.3. Stumpo D J. et al: MARCKS deficiency in mice leads to abnormal brain development and perinatal death. Proc. Nat. Acad. Sci. 1995 92; 944-948.4. Verghese G M. et al: Proteinkinase C-mediated phosphorylation and calmodulin binding of recombinant myristoylatedalanine-rich C kinase substrate (MARCKS) and MARCKS-related protein. J Biol Chem1994 269:9361-9367.