- MARCKS
Myristoylated alanine-rich protein kinase C substrate, also known as MARCKS, is a human
gene .cite web | title = Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4082| accessdate = ]PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4082| accessdate = ]References
Further reading
PBB_Further_reading
citations =
*cite journal | author=Blackshear PJ |title=The MARCKS family of cellular protein kinase C substrates. |journal=J. Biol. Chem. |volume=268 |issue= 3 |pages= 1501–4 |year= 1993 |pmid= 8420923 |doi=
*cite journal | author=Aderem A |title=The MARCKS family of protein kinase-C substrates. |journal=Biochem. Soc. Trans. |volume=23 |issue= 3 |pages= 587–91 |year= 1996 |pmid= 8566422 |doi=
*cite journal | author=Herget T, Brooks SF, Broad S, Rozengurt E |title=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. |journal=Eur. J. Biochem. |volume=209 |issue= 1 |pages= 7–14 |year= 1992 |pmid= 1396720 |doi=
*cite journal | author=Sakai K, Hirai M, Kudoh J, "et al." |title=Molecular cloning and chromosomal mapping of a cDNA encoding human 80K-L protein: major substrate for protein kinase C. |journal=Genomics |volume=14 |issue= 1 |pages= 175–8 |year= 1992 |pmid= 1427823 |doi=
*cite journal | author=Hartwig JH, Thelen M, Rosen A, "et al." |title=MARCKS is an actin filament crosslinking protein regulated by protein kinase C and calcium-calmodulin. |journal=Nature |volume=356 |issue= 6370 |pages= 618–22 |year= 1992 |pmid= 1560845 |doi= 10.1038/356618a0
*cite journal | author=Harlan DM, Graff JM, Stumpo DJ, "et al." |title=The human myristoylated alanine-rich C kinase substrate (MARCKS) gene (MACS). Analysis of its gene product, promoter, and chromosomal localization. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14399–405 |year= 1991 |pmid= 1860846 |doi=
*cite journal | author=Graff JM, Stumpo DJ, Blackshear PJ |title=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. |journal=J. Biol. Chem. |volume=264 |issue= 20 |pages= 11912–9 |year= 1989 |pmid= 2473066 |doi=
*cite journal | author=Herget T, Oehrlein SA, Pappin DJ, "et al." |title=The myristoylated alanine-rich C-kinase substrate (MARCKS) is sequentially phosphorylated by conventional, novel and atypical isotypes of protein kinase C. |journal=Eur. J. Biochem. |volume=233 |issue= 2 |pages= 448–57 |year= 1995 |pmid= 7588787 |doi=
*cite journal | author=Taniguchi H, Manenti S, Suzuki M, Titani K |title=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. |journal=J. Biol. Chem. |volume=269 |issue= 28 |pages= 18299–302 |year= 1994 |pmid= 8034575 |doi=
*cite journal | author=Rao PH, Murty VV, Gaidano G, "et al." |title=Subregional mapping of 8 single copy loci to chromosome 6 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=66 |issue= 4 |pages= 272–3 |year= 1994 |pmid= 8162705 |doi=
*cite journal | author=Taniguchi H, Manenti S |title=Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids. |journal=J. Biol. Chem. |volume=268 |issue= 14 |pages= 9960–3 |year= 1993 |pmid= 8486722 |doi=
*cite journal | author=Palmer RH, Schönwasser DC, Rahman D, "et al." |title=PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163. |journal=FEBS Lett. |volume=378 |issue= 3 |pages= 281–5 |year= 1996 |pmid= 8557118 |doi=
*cite journal | author=Swierczynski SL, Blackshear PJ |title=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. |journal=J. Biol. Chem. |volume=271 |issue= 38 |pages= 23424–30 |year= 1996 |pmid= 8798548 |doi=
*cite journal | author=Spizz G, Blackshear PJ |title=Identification and characterization of cathepsin B as the cellular MARCKS cleaving enzyme. |journal=J. Biol. Chem. |volume=272 |issue= 38 |pages= 23833–42 |year= 1997 |pmid= 9295331 |doi=
*cite journal | author=Qi Q, Rajala RV, Anderson W, "et al." |title=Molecular cloning, genomic organization, and biochemical characterization of myristoyl-CoA:protein N-myristoyltransferase from Arabidopsis thaliana. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9673–83 |year= 2000 |pmid= 10734119 |doi=
*cite journal | author=Jin Cho S, La M, Ahn JK, "et al." |title=Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation. |journal=Biochem. Biophys. Res. Commun. |volume=283 |issue= 2 |pages= 273–7 |year= 2001 |pmid= 11327693 |doi= 10.1006/bbrc.2001.4773
*cite journal | author=Li Y, Martin LD, Spizz G, Adler KB |title=MARCKS protein is a key molecule regulating mucin secretion by human airway epithelial cells in vitro. |journal=J. Biol. Chem. |volume=276 |issue= 44 |pages= 40982–90 |year= 2001 |pmid= 11533058 |doi= 10.1074/jbc.M105614200
*cite journal | author=Rauch ME, Ferguson CG, Prestwich GD, Cafiso DS |title=Myristoylated alanine-rich C kinase substrate (MARCKS) sequesters spin-labeled phosphatidylinositol 4,5-bisphosphate in lipid bilayers. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 14068–76 |year= 2002 |pmid= 11825894 |doi= 10.1074/jbc.M109572200PBB_Controls
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