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  The name of this protein is derived from Myristoylated Alanine Rich C Kinase Substrate as it was first identified as a major substrate for protein kinase C (Aderem, 1992). MARKS is present in neuronal tissue at 10mm (Blackshear, 1993). The protein becomes redistributed from the cytoplasmic face of the plasma-membrane to the cytosol upon phosphorylation by protein kinase C after stimulation of a number of cell types by a number of agonists. More recently it has been discovered that MARCKS is a calcium/calmodulin sensitive actin filament crosslinking protein, also controlled by phosphorylation.  The affinity of the protein for actin is approximately halved upon phosphorylation. Weak bundling activity is seen at high concentrations of MARCKS and this bundling activity is also seen with a synthetic lysine rich peptide corresponding to residues 155-173 of the protein.   The actin binding region of MARKS (Hartwig et al, 1992) has been determined to be:-  KRFSFKKSKLSGFSFKKN.

The role of MARCKS in cell spreading (Manenti et al, 1997; Myat et al, 1997; Yue et al, 2000), through focal contact formation. MARCKS is found at the focal contacts of cultured cells. MARCKS interacts with PIP2 (Rauch et al, 2002), and apparently sequesters it through non-specific electrostatic interaction (Wang et al, 2002). 


Aderem, A. (1992). Signal transduction and the actin cytoskeleton: the roles of MARCKS and profilin. Trends in Biochemistry 17, 438-443.

Blackshear, P.J. (1993). J.Biol.Chem. 268, 1501-1504.

Disatnik, M.-H., Boutel, S. C., Lee, C. H., Mochy-Rosen, D. & Rando, T. A. (2002) Sequential activation of individual PKC isozymes in integrin-mediated muscle cell spreading: a role for MARCKS in an integrin signaling pathways. J.Cell Sci. 115, 2151-2163.

Hartwig, J. H., Thelen, M., Rosen, A., Janmey, P. A., Nairn, A. C. & Aderem, A. (1992) Marcks is an actin filament cross-linking protein regulated by protein-kinase-c and calcium calmodulin. Nature. 356, 618-622.

Manenti, S., Malecaze, F. & Darbon, J. M. (1997) The major myritoylated PKC substrate (MARCKS) is involved in cell spreading , tyrosine phosphorylation of paxillin, and focal contact formation. FEBS letters. 419, 95-98.

Morash, S.C., Byers, D.M. & Cook, H.W. (2000). Activation of phospholipase D by PKC and GTPgS in human neuroblastoma cells overexpressing MARCKS. Biochim.Biophys.Acta. 1487, 177-189.

Myat, M. M., Anderson, S., Allen, L. A. & Aderem, A. (1997) MARCKS regulates membrane ruffling and cell spreading. Curr. Biol. 7, 611-614.

Rauch, M. E., Ferguson, C. G., Prestwich, G. D. & Cafiso, D. S. (2002) Myristoylated alanine rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers.  J.Biol.Chem. 277, 14068-14076.

Wang, J., Gambhir, A., Hangyas-Mihalyne, G., Murray, D., Golebiewska, U. & McLaughlin, S. (2002) Lateral Sequestration of Phosphatidylinositol 4,5-Bisphosphate by the Basic Effector Domain of Myristoylated Alanine-rich C Kinase Substrate Is Due to Nonspecific Electrostatic Interactions, J. Biol. Chem. 277, 34401-34412.

Yue, L., Lu, S., Garces, J., Jin, T. & Li, J. (2000). Protein Kinase C-regulated dynamitin-macrophage-enriched Myristolyated Alanine-Rich C Kinase Substrate interaction is involved in macrophage cell spreading. J.Biol.Chem. 275, 23948-23956.

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