MARCKS

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Myristoylated alanine-rich protein kinase C substrate
Identifiers
Symbols MARCKS ; 80K-L; FLJ14368; FLJ90045; MACS; MRACKS; PKCSL; PRKCSL
External IDs Template:OMIM5 Template:MGI HomoloGene40623
RNA expression pattern
File:PBB GE MARCKS 201669 s at tn.png
File:PBB GE MARCKS 201668 x at tn.png
File:PBB GE MARCKS 201670 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Myristoylated alanine-rich protein kinase C substrate, also known as MARCKS, is a human gene.[1]

The protein encoded by this gene is a substrate for protein kinase C. It is localized to the plasma membrane and is an actin filament crosslinking protein. Phosphorylation by protein kinase C or binding to calcium-calmodulin inhibits its association with actin and with the plasma membrane, leading to its presence in the cytoplasm. The protein is thought to be involved in cell motility, phagocytosis, membrane trafficking and mitogenesis.[1]

References

  1. 1.0 1.1 "Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate".

Further reading

  • Blackshear PJ (1993). "The MARCKS family of cellular protein kinase C substrates". J. Biol. Chem. 268 (3): 1501–4. PMID 8420923.
  • Aderem A (1996). "The MARCKS family of protein kinase-C substrates". Biochem. Soc. Trans. 23 (3): 587–91. PMID 8566422.
  • Herget T, Brooks SF, Broad S, Rozengurt E (1992). "Relationship between the major protein kinase C substrates acidic 80-kDa protein-kinase-C substrate (80K) and myristoylated alanine-rich C-kinase substrate (MARCKS). Members of a gene family or equivalent genes in different species". Eur. J. Biochem. 209 (1): 7–14. PMID 1396720.
  • Sakai K, Hirai M, Kudoh J; et al. (1992). "Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L protein: major substrate for protein kinase C.". Genomics. 14 (1): 175–8. PMID 1427823.
  • Hartwig JH, Thelen M, Rosen A; et al. (1992). "MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin". Nature. 356 (6370): 618–22. doi:10.1038/356618a0. PMID 1560845.
  • Harlan DM, Graff JM, Stumpo DJ; et al. (1991). "The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization". J. Biol. Chem. 266 (22): 14399–405. PMID 1860846.
  • Graff JM, Stumpo DJ, Blackshear PJ (1989). "Characterization of the phosphorylation sites in the chicken and bovine myristoylated alanine-rich C kinase substrate protein, a prominent cellular substrate for protein kinase C.". J. Biol. Chem. 264 (20): 11912–9. PMID 2473066.
  • Herget T, Oehrlein SA, Pappin DJ; et al. (1995). "The myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase C.". Eur. J. Biochem. 233 (2): 448–57. PMID 7588787.
  • Taniguchi H, Manenti S, Suzuki M, Titani K (1994). "Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinase(s). A mass spectroscopic analysis of the post-translational modifications". J. Biol. Chem. 269 (28): 18299–302. PMID 8034575.
  • Rao PH, Murty VV, Gaidano G; et al. (1994). "Subregional mapping of 8 single copy loci to chromosome 6 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 66 (4): 272–3. PMID 8162705.
  • Taniguchi H, Manenti S (1993). "Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids". J. Biol. Chem. 268 (14): 9960–3. PMID 8486722.
  • Palmer RH, Schönwasser DC, Rahman D; et al. (1996). "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163". FEBS Lett. 378 (3): 281–5. PMID 8557118.
  • Swierczynski SL, Blackshear PJ (1996). "Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the myristoylated alanine-rich protein kinase C substrate protein in intact cells". J. Biol. Chem. 271 (38): 23424–30. PMID 8798548.
  • Spizz G, Blackshear PJ (1997). "Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzyme". J. Biol. Chem. 272 (38): 23833–42. PMID 9295331.
  • Qi Q, Rajala RV, Anderson W; et al. (2000). "Molecular cloning, genomic organization, and biochemical characterization of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis thaliana". J. Biol. Chem. 275 (13): 9673–83. PMID 10734119.
  • Jin Cho S, La M, Ahn JK; et al. (2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochem. Biophys. Res. Commun. 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. PMID 11327693.
  • Li Y, Martin LD, Spizz G, Adler KB (2001). "MARCKS protein is a key molecule regulating mucin secretion by human airway epithelial cells in vitro". J. Biol. Chem. 276 (44): 40982–90. doi:10.1074/jbc.M105614200. PMID 11533058.
  • Rauch ME, Ferguson CG, Prestwich GD, Cafiso DS (2002). "Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers". J. Biol. Chem. 277 (16): 14068–76. doi:10.1074/jbc.M109572200. PMID 11825894.

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