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Gene Review

Marcks  -  myristoylated alanine rich protein kinase...

Rattus norvegicus

Synonyms: KINC, MARCKS, Macs, Myristoylated alanine-rich C-kinase substrate, Protein kinase C substrate 80 kDa protein
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Disease relevance of Marcks


Psychiatry related information on Marcks

  • The data suggest that a biphasic modulation of protein kinase C and MARCKS by Abeta(1-40) combined with anoxic stress may play a role in Alzheimer's disease pathology [1].

High impact information on Marcks

  • Essential role for the PKC target MARCKS in maintaining dendritic spine morphology [6].
  • MARCKS associates with membranes via the combined action of myristoylation and a polybasic effector domain, which binds phospholipids and/or F-actin, unless phosphorylated by PKC [6].
  • We investigated the role of MARCKS (myristoylated, alanine-rich C-kinase substrate) in dendrites of 3-week-old hippocampal cultures [6].
  • Furthermore, depletion of MARCKS by MARCKS-AON treatment of neurons resulted in a significant decrease in Ang II-stimulated accumulation of TH and DbetaH immunoreactivities and [3H]NE uptake activity in synaptosomes [7].
  • These observations demonstrate that phosphorylation of MARCKS by PKCbeta and its redistribution from varicosities to neurites is important in Ang II-induced synaptic accumulation of TH, DbetaH, and NE [7].

Biological context of Marcks

  • On the other side, proteins affecting signal transduction and cytoskeleton-related proteins (heterotrimeric G-proteins, protein kinase C, MARCKS, tubulin), were not enriched within detergent-resistant fractions during cell differentiation, but were recovered within this fraction in mature neurons [8].
  • These results suggest that MARCKS is a target of PKG, and PKG-dependent phosphorylation of MARCKS results in its degradation to reduce its protein levels in the cells [9].
  • In addition, possible degradation products of MARCKS were observed after transfection of PKG or stimulation with 8pCPT-cGMP [9].
  • However, cells expressing MARCKS ED mutants were irregularly shaped and stress fibers were either shorter or less abundant, and cell adhesion and viability were not affected [10].
  • Like control cells, those expressing wild type MARCKS were elongated and possessed longitudinally oriented stress fibers, although these cells were more prone to detach from the substratum and undergo cell death upon phorbol ester treatment [10].

Anatomical context of Marcks


Associations of Marcks with chemical compounds


Physical interactions of Marcks

  • Inhibitors of actin polymerization and calmodulin binding enhance protein kinase C-induced translocation of MARCKS in C6 glioma cells [16].

Enzymatic interactions of Marcks


Regulatory relationships of Marcks


Other interactions of Marcks


Analytical, diagnostic and therapeutic context of Marcks


  1. Biphasic modulation of protein kinase C and enhanced cell toxicity by amyloid beta peptide and anoxia in neuronal cultures. Kuperstein, F., Reiss, N., Koudinova, N., Yavin, E. J. Neurochem. (2001) [Pubmed]
  2. Amyloid beta protein (25-35) phosphorylates MARCKS through tyrosine kinase-activated protein kinase C signaling pathway in microglia. Nakai, M., Hojo, K., Yagi, K., Saito, N., Taniguchi, T., Terashima, A., Kawamata, T., Hashimoto, T., Maeda, K., Gschwendt, M., Yamamoto, H., Miyamoto, E., Tanaka, C. J. Neurochem. (1999) [Pubmed]
  3. Arginine vasopressin (AVP) causes the reversible phosphorylation of the myristoylated alanine-rich C kinase substrate (MARCKS) protein in the ovine anterior pituitary: evidence that MARCKS phosphorylation is associated with adrenocorticotropin (ACTH) secretion. Liu, J.P., Engler, D., Funder, J.W., Robinson, P.J. Mol. Cell. Endocrinol. (1994) [Pubmed]
  4. Brain protein kinase C assay using MARCKS substrate reveals no translocation due to profound insulin-induced hypoglycemia. Anderson, L.G., Zhao, D., Dell, K.R., Severson, D.L., Auer, R.N. Brain Res. (1993) [Pubmed]
  5. Myristoylated alanine-rich C-kinase substrate is phosphorylated and translocated by a phorbol ester-insensitive and calcium-independent protein kinase C isoform in C6 glioma cell membranes. Douglas, D.N., Fink, H.S., Ridgway, N.D., Cook, H.W., Byers, D.M. Biochim. Biophys. Acta (1999) [Pubmed]
  6. Essential role for the PKC target MARCKS in maintaining dendritic spine morphology. Calabrese, B., Halpain, S. Neuron (2005) [Pubmed]
  7. Regulation of angiotensin II-induced neuromodulation by MARCKS in brain neurons. Lu, D., Yang, H., Lenox, R.H., Raizada, M.K. J. Cell Biol. (1998) [Pubmed]
  8. Developmental changes in the protein composition of sphingolipid- and cholesterol-enriched membrane domains of rat cerebellar granule cells. Palestini, P., Botto, L., Guzzi, F., Calvi, C., Ravasi, D., Masserini, M., Pitto, M. J. Neurosci. Res. (2002) [Pubmed]
  9. cGMP-dependent phosphorylation and degradation of myristoylated alanine-rich C-kinase substrate. Matsubara, T., Okumura, N., Okumura, A., Nagai, K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  10. Expression of MARCKS effector domain mutants alters phospholipase D activity and cytoskeletal morphology of SK-N-MC neuroblastoma cells. Morash, S.C., Douglas, D., McMaster, C.R., Cook, H.W., Byers, D.M. Neurochem. Res. (2005) [Pubmed]
  11. Cathepsin B-like proteolysis and MARCKS degradation in sub-lethal NMDA-induced collapse of dendritic spines. Graber, S., Maiti, S., Halpain, S. Neuropharmacology (2004) [Pubmed]
  12. Eicosanoid activation of protein kinase C epsilon: involvement in growth cone repellent signaling. Mikule, K., Sunpaweravong, S., Gatlin, J.C., Pfenninger, K.H. J. Biol. Chem. (2003) [Pubmed]
  13. Glucose-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) in isolated rat pancreatic islets. Calle, R., Ganesan, S., Smallwood, J.I., Rasmussen, H. J. Biol. Chem. (1992) [Pubmed]
  14. Characterization of the phosphatidylserine-binding region of rat MARCKS (myristoylated, alanine-rich protein kinase C substrate). Its regulation through phosphorylation of serine 152. Nakaoka, T., Kojima, N., Ogita, T., Tsuji, S. J. Biol. Chem. (1995) [Pubmed]
  15. Phosphorylation of myristoylated alanine-rich protein kinase C substrate by mitogen-activated protein kinase in cultured rat hippocampal neurons following stimulation of glutamate receptors. Ohmitsu, M., Fukunaga, K., Yamamoto, H., Miyamoto, E. J. Biol. Chem. (1999) [Pubmed]
  16. Inhibitors of actin polymerization and calmodulin binding enhance protein kinase C-induced translocation of MARCKS in C6 glioma cells. Douglas, D.N., Fink, H.S., Rosé, S.D., Ridgway, N.D., Cook, H.W., Byers, D.M. Biochim. Biophys. Acta (1997) [Pubmed]
  17. Differential responses of protein kinase C substrates (MARCKS, neuromodulin, and neurogranin) phosphorylation to calmodulin and S100. Sheu, F.S., Huang, F.L., Huang, K.P. Arch. Biochem. Biophys. (1995) [Pubmed]
  18. Differential stimulation of protein kinase C activity by phorbol ester or calcium/phosphatidylserine in vitro and in intact synaptosomes. Robinson, P.J. J. Biol. Chem. (1992) [Pubmed]
  19. Endothelin-1 stimulates myristoylated alanine-rich C-kinase substrate (MARCKS) phosphorylation in rat cerebellar slices. Catalán, R.E., Martínez, A.M., Aragonés, M.D., Hernández, F. Neurosci. Lett. (1995) [Pubmed]
  20. Immunoseparation of Prion protein-enriched domains from other detergent-resistant membrane fractions, isolated from neuronal cells. Botto, L., Masserini, M., Cassetti, A., Palestini, P. FEBS Lett. (2004) [Pubmed]
  21. Involvement of protein kinase C epsilon in thyrotropin-releasing hormone-stimulated phosphorylation of the myristoylated alanine-rich C kinase substrate in rat pituitary clonal cells. Akita, Y., Kawasaki, H., Ohno, S., Suzuki, K., Kawashima, S. Electrophoresis (2000) [Pubmed]
  22. Phosphorylation of AMPA-type glutamate receptors by calcium/calmodulin-dependent protein kinase II and protein kinase C in cultured hippocampal neurons. Tan, S.E., Wenthold, R.J., Soderling, T.R. J. Neurosci. (1994) [Pubmed]
  23. Altered regulation of a major substrate of protein kinase C in rat 6 fibroblasts overproducing PKC beta I. Guadagno, S.N., Borner, C., Weinstein, I.B. J. Biol. Chem. (1992) [Pubmed]
  24. Expression and regulation of 80K/MARCKS, a major substrate of protein kinase C, in the developing rat heart. McGill, C.J., Brooks, G. Cardiovasc. Res. (1997) [Pubmed]
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