MARCKS

MARCKS
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
Aliases MARCKS, 80K-L, MACS, PKCSL, PRKCSL, myristoylated alanine rich protein kinase C substrate
External IDs HomoloGene: 135584 GeneCards: MARCKS
RNA expression pattern




More reference expression data
Orthologs
Species Human Mouse
Entrez

4082

n/a

Ensembl

ENSG00000277443

n/a

UniProt

P29966

n/a

RefSeq (mRNA)

NM_002356

n/a

RefSeq (protein)

NP_002347.5

n/a

Location (UCSC) Chr 6: 113.86 – 113.86 Mb n/a
PubMed search [1] n/a
Wikidata
View/Edit Human

Myristoylated alanine-rich C-kinase substrate is a protein that in humans is encoded by the MARCKS gene.[2][3][4] It plays important roles in cell shape, cell motility, secretion, transmembrane transport, regulation of the cell cycle, and neural development.[5] Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin.

They are acidic proteins with high proportions of alanine, glycine, proline, and glutamic acid. They are membrane-bound through a lipid anchor at the N-terminus, and a polybasic domain in the middle. They are regulated by Ca2+/calmodulin and protein kinase C. In their unphosphorylated form, they bind to actin filaments, causing them to crosslink, and sequester acidic membrane phospholipids such as PIP2.

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.[4]

Interactions

MARCKS has been shown to interact with TOB1[6] and with NMT2.[7]

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A (May 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.
  3. ↑ Blackshear PJ (Feb 1993). "The MARCKS family of cellular protein kinase C substrates". J Biol Chem. 268 (3): 1501–4. PMID 8420923.
  4. 1 2 "Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate".
  5. ↑ PRIETO, DANIEL; ZOLESSI, FLAVIO R. (August 2016). "Functional Diversification of the Four MARCKS Family Members in Zebrafish Neural Development". Journal of Experimental Zoology Part B: Molecular and Developmental Evolution. doi:10.1002/jez.b.22691.
  6. ↑ Jin Cho, S; La M; Ahn J K; Meadows G G; Joe C O (May 2001). "Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation". Biochem. Biophys. Res. Commun. United States. 283 (2): 273–7. doi:10.1006/bbrc.2001.4773. ISSN 0006-291X. PMID 11327693.
  7. ↑ Selvakumar, P.; Lakshmikuttyamma, A.; Sharma, RK. (2009). "Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2.". J Biomed Biotechnol. 2009: 907614. doi:10.1155/2009/907614. PMID 19746168.

Further reading

  • 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. doi:10.1111/j.1432-1033.1992.tb17255.x. 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. doi:10.1016/S0888-7543(05)80301-5. PMID 1427823. 
  • 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. doi:10.1111/j.1432-1033.1995.448_2.x. 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. doi:10.1159/000133710. 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. doi:10.1016/0014-5793(95)01454-3. 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. doi:10.1074/jbc.271.38.23424. 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. doi:10.1074/jbc.272.38.23833. 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. doi:10.1074/jbc.275.13.9673. 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. 
  • Sergio Alonso; Undine Dietrich; Chris Händel; Josef A. Käs; Markus Bär (2011). "Oscillations in the Lateral Pressure of Lipid Monolayers Induced by Nonlinear Chemical Dynamics of the Second Messengers MARCKS and Protein Kinase C". Biophysical Journal. 100 (4): 939–947. doi:10.1016/j.bpj.2010.12.3702. PMC 3037601Freely accessible. PMID 21320438. 
  • Jürgen Lippoldt; Chris Händel; Undine Dietrich; Josef A. Käs (2014). "Dynamic membrane structure induces temporal pattern formation". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1838 (10): 2380–90. doi:10.1016/j.bbamem.2014.05.018. PMID 24866013. 
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