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Marcks  -  myristoylated alanine rich protein kinase...

Mus musculus

Synonyms: MARCKS, Macs, Myristoylated alanine-rich C-kinase substrate, PKCSL
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Disease relevance of Marcks

  • Recent studies using gene disruption in vivo have demonstrated the importance of both MARCKS and MLP to the development of the central nervous system; specifically, mice lacking either protein exhibit a high frequency of neural tube defects [1].
  • In this report we show that macrophage extracts contain a protease which specifically cleaves human MARCKS, expressed in a cell-free system or in E. coli, between Lys-6 and Thr-7 [2].
  • On a 129B6(N3) background, the Macs mutation produced IP-MF hyperplasia, a significant increase in hippocampal PKCepsilon expression, and proficient spatial learning relative to wild-type controls [3].
  • Phosphorylation of the MARCKS family of protein kinase C substrates in human B chronic lymphocytic leukemia cells [4].
  • We isolated a phage clone from a mouse genomic library that spanned the entire coding sequence of the mouse MARCKS protein [5].

Psychiatry related information on Marcks

  • We have previously demonstrated that 50% reductions in MARCKS expression in heterozygous Marcks mutant mice produce robust deficits in spatial reversal learning, but not contextual fear conditioning, suggesting that only specific aspects of hippocampal function are impaired by reduction in MARCKS expression [6].

High impact information on Marcks


Chemical compound and disease context of Marcks

  • Amounts of MARCKS protein, measured by [3H]myristate labeling and western blotting, were severalfold higher in rat C6 glioma and human HTB-11 (SK-N-SH) neuroblastoma cells than in HTB-10 (SK-N-MC) or mouse N1E-115 neuroblastoma cells [10].
  • Pretreating the glioma cells with ionomycin prevented TPA-stimulated PKCs from phosphorylating the MARCKS protein [11].

Biological context of Marcks


Anatomical context of Marcks

  • Disruption of Marcks in mice leads to a number of developmental defects within the central nervous system that are completely prevented by expression of an epitope-tagged wild-type human MARCKS transgene [13].
  • Interestingly, the affinity of MRP for acidic lipid membranes is 20-30-fold smaller than reported for murine MARCKS (Kim, J., Shishido, T., Jiang, X., Aderem, A. A., and McLaughlin, S. (1994) J. Biol. Chem. 269, 28214-28219) [14].
  • MARCKS proteins are myristoylated proteins associated with membranes and the actin cytoskeleton [15].
  • We investigated alterations of cellular distribution and phosphorylation of MARCKS in the hippocampus following kainic acid (KA)-induced seizures [16].
  • Moreover, immunoreactivities of phosphorylated MARCKS were co-localized in the activated microglia with those of the above isoforms of PKC [16].

Associations of Marcks with chemical compounds


Physical interactions of Marcks


Enzymatic interactions of Marcks


Regulatory relationships of Marcks


Other interactions of Marcks


Analytical, diagnostic and therapeutic context of Marcks


  1. Promoter sequence, expression, and fine chromosomal mapping of the human gene (MLP) encoding the MARCKS-like protein: identification of neighboring and linked polymorphic loci for MLP and MACS and use in the evaluation of human neural tube defects. Stumpo, D.J., Eddy, R.L., Haley, L.L., Sait, S., Shows, T.B., Lai, W.S., Young, W.S., Speer, M.C., Dehejia, A., Polymeropoulos, M., Blackshear, P.J. Genomics (1998) [Pubmed]
  2. Myristoylation-dependent N-terminal cleavage of the myristoylated alanine-rich C kinase substrate (MARCKS) by cellular extracts. Braun, T., McIlhinney, R.A., Vergères, G. Biochimie (2000) [Pubmed]
  3. Effect of reduced myristoylated alanine-rich C kinase substrate expression on hippocampal mossy fiber development and spatial learning in mutant mice: transgenic rescue and interactions with gene background. McNamara, R.K., Stumpo, D.J., Morel, L.M., Lewis, M.H., Wakeland, E.K., Blackshear, P.J., Lenox, R.H. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  4. Phosphorylation of the MARCKS family of protein kinase C substrates in human B chronic lymphocytic leukemia cells. Carballo, E., Colomer, D., Vives Corrons, J.L., Blackshear, P.J., Gil, J. Leukemia (1995) [Pubmed]
  5. Chromosomal mapping of the human (MACS) and mouse (Macs) genes encoding the MARCKS protein. Blackshear, P.J., Tuttle, J.S., Oakey, R.J., Seldin, M.F., Chery, M., Philippe, C., Stumpo, D.J. Genomics (1992) [Pubmed]
  6. Myristoylated alanine rich C kinase substrate (MARCKS) heterozygous mutant mice exhibit deficits in hippocampal mossy fiber-CA3 long-term potentiation. Hussain, R.J., Stumpo, D.J., Blackshear, P.J., Lenox, R.H., Abel, T., McNamara, R.K. Hippocampus. (2006) [Pubmed]
  7. MacMARCKS, a novel member of the MARCKS family of protein kinase C substrates. Li, J., Aderem, A. Cell (1992) [Pubmed]
  8. A MARCKS-related peptide blocks mucus hypersecretion in a mouse model of asthma. Singer, M., Martin, L.D., Vargaftig, B.B., Park, J., Gruber, A.D., Li, Y., Adler, K.B. Nat. Med. (2004) [Pubmed]
  9. Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia. Rosen, A., Keenan, K.F., Thelen, M., Nairn, A.C., Aderem, A. J. Exp. Med. (1990) [Pubmed]
  10. Differential expression of MARCKS and other calmodulin-binding protein kinase C substrates in cultured neuroblastoma and glioma cells. Rosé, S.D., Cook, H.W., Palmer, F.B., Ridgway, N.D., Byers, D.M. J. Neurochem. (1994) [Pubmed]
  11. Ca2+ x calmodulin prevents myristoylated alanine-rich kinase C substrate protein phosphorylation by protein kinase Cs in C6 rat glioma cells. Chakravarthy, B.R., Isaacs, R.J., Morley, P., Whitfield, J.F. J. Biol. Chem. (1995) [Pubmed]
  12. v-Jun targets showing an expression pattern that correlates with the transformed cellular phenotype. Iacovoni, J.S., Cohen, S.B., Berg, T., Vogt, P.K. Oncogene (2004) [Pubmed]
  13. Neuroanatomical development in the absence of PKC phosphorylation of the myristoylated alanine-rich C-kinase substrate (MARCKS) protein. Scarlett, C.O., Blackshear, P.J. Brain Res. Dev. Brain Res. (2003) [Pubmed]
  14. The myristoyl moiety of myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein is embedded in the membrane. Vergères, G., Manenti, S., Weber, T., Stürzinger, C. J. Biol. Chem. (1995) [Pubmed]
  15. Poly(ADP-ribose) modulates the properties of MARCKS proteins. Schmitz, A.A., Pleschke, J.M., Kleczkowska, H.E., Althaus, F.R., Vergères, G. Biochemistry (1998) [Pubmed]
  16. Cell type-specific upregulation of myristoylated alanine-rich C kinase substrate and protein kinase C-alpha, -beta I, -beta II, and -delta in microglia following kainic acid-induced seizures. Eun, S.Y., Kim, E.H., Kang, K.S., Kim, H.J., Jo, S.A., Kim, S.J., Jo, S.H., Kim, S.J., Blackshear, P.J., Kim, J. Exp. Mol. Med. (2006) [Pubmed]
  17. Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes. Vergères, G., Ramsden, J.J. Biochem. J. (1998) [Pubmed]
  18. Inhibition of mucin secretion with MARCKS-related peptide improves airway obstruction in a mouse model of asthma. Agrawal, A., Rengarajan, S., Adler, K.B., Ram, A., Ghosh, B., Fahim, M., Dickey, B.F. J. Appl. Physiol. (2007) [Pubmed]
  19. Macrophage-enriched myristoylated alanine-rich C kinase substrate and its phosphorylation is required for the phorbol ester-stimulated diffusion of beta 2 integrin molecules. Zhou, X., Li, J. J. Biol. Chem. (2000) [Pubmed]
  20. Conventional PKC-alpha, novel PKC-epsilon and PKC-theta, but not atypical PKC-lambda are MARCKS kinases in intact NIH 3T3 fibroblasts. Uberall, F., Giselbrecht, S., Hellbert, K., Fresser, F., Bauer, B., Gschwendt, M., Grunicke, H.H., Baier, G. J. Biol. Chem. (1997) [Pubmed]
  21. MARCKS-related protein binds to actin without significantly affecting actin polymerization or network structure. Myristoylated alanine-rich C kinase substrate. Wohnsland, F., Steinmetz, M.O., Aebi, U., Vergères, G. J. Struct. Biol. (2000) [Pubmed]
  22. p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113. Schönwasser, D.C., Palmer, R.H., Herget, T., Parker, P.J. FEBS Lett. (1996) [Pubmed]
  23. Biologically active milli-calpain associated with caveolae is involved in a spatially compartmentalised signalling involving protein kinase C alpha and myristoylated alanine-rich C-kinase substrate (MARCKS). Goudenege, S., Poussard, S., Dulong, S., Cottin, P. Int. J. Biochem. Cell Biol. (2005) [Pubmed]
  24. Bombesin, endothelin and platelet-derived growth factor induce rapid translocation of the myristoylated alanine-rich C-kinase substrate in Swiss 3T3 cells. Herget, T., Rozengurt, E. Eur. J. Biochem. (1994) [Pubmed]
  25. In vivo effects of doxorubicin on kinase C in cultured cells. Otsuka, M., Shigeoka, H., Yang, H.C. Cancer Chemother. Pharmacol. (1992) [Pubmed]
  26. Phosphorylated MARCKS: a novel centrosome component that also defines a peripheral subdomain of the cortical actin cap in mouse eggs. Michaut, M.A., Williams, C.J., Schultz, R.M. Dev. Biol. (2005) [Pubmed]
  27. Molecular cloning, expression and chromosomal localisation of the mouse Rev3l gene, encoding the catalytic subunit of polymerase zeta. Van Sloun, P.P., Romeijn, R.J., Eeken, J.C. Mutat. Res. (1999) [Pubmed]
  28. Induction of protein kinase C substrates, Myristoylated alanine-rich C kinase substrate (MARCKS) and MARCKS-related protein (MRP), by amyloid beta-protein in mouse BV-2 microglial cells. Murphy, A., Sunohara, J.R., Sundaram, M., Ridgway, N.D., McMaster, C.R., Cook, H.W., Byers, D.M. Neurosci. Lett. (2003) [Pubmed]
  29. Cloning and molecular characterization of the murine macrophage "68-kDa" protein kinase C substrate and its regulation by bacterial lipopolysaccharide. Seykora, J.T., Ravetch, J.V., Aderem, A. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  30. Differential expression and regulation of myristoylated alanine-rich C kinase substrate (MARCKS) in the hippocampus of C57/BL6J and DBA/2J mice. McNamara, R.K., Vasquez, P.A., Mathe, A.A., Lenox, R.H. J. Neurochem. (2003) [Pubmed]
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