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{{ | '''Myristoylated alanine-rich C-kinase substrate''' is a [[protein]] that in humans is encoded by the ''MARCKS'' [[gene]].<ref name="pmid1560845">{{cite journal |vauthors=Hartwig JH, Thelen M, Rosen A, Janmey PA, Nairn AC, Aderem A | 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 |date=May 1992 | pmid = 1560845 | pmc = | doi = 10.1038/356618a0 }}</ref><ref name="pmid8420923">{{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 |date=Feb 1993 | pmid = 8420923 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4082| accessdate = }}</ref> | ||
It plays important roles in cell shape, [[cell motility]], [[secretion]], transmembrane transport, regulation of the [[cell cycle]], and neural development.<ref>{{cite journal|last1=PRIETO|first1=DANIEL|last2=ZOLESSI|first2=FLAVIO R.|title=Functional Diversification of the Four MARCKS Family Members in Zebrafish Neural Development|journal=Journal of Experimental Zoology Part B: Molecular and Developmental Evolution|date=August 2016|doi=10.1002/jez.b.22691|volume=328|pages=119–138}}</ref> Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin. | |||
It is also the name of a [[protein family]], of which MARCKS is the most studied member. They are [[intrinsically disordered proteins]], with an [[acid]]ic pH, with high proportions of [[alanine]], [[glycine]], [[proline]], and [[glutamic acid]]. They are [[Cell membrane|membrane]]-bound through a [[lipid anchor]] at the N-terminus, and a polybasic domain in the middle. They are regulated by Ca<sup>2+</sup>/[[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. | |||
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| 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.<ref name="entrez" | | 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.<ref name="entrez" /> | ||
}} | }} | ||
==Interactions== | |||
MARCKS has been shown to [[Protein-protein interaction|interact]] with [[TOB1]]<ref name=pmid11327693>{{cite journal |last=Jin Cho |first=S |authorlink= |author2=La M |author3=Ahn J K |author4=Meadows G G |author5=Joe C O |date=May 2001 |title=Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation |journal=Biochem. Biophys. Res. Commun. |volume=283 |issue=2 |pages=273–7 |publisher= |location = United States| issn = 0006-291X| pmid = 11327693 |doi = 10.1006/bbrc.2001.4773 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> and with [[NMT2]].<ref>{{Cite journal | last1 = Selvakumar | first1 = P. | last2 = Lakshmikuttyamma | first2 = A. | last3 = Sharma | first3 = RK. | title = Biochemical characterization of bovine brain myristoyl-CoA:protein N-myristoyltransferase type 2. | journal = J Biomed Biotechnol | volume = 2009 | issue = | pages = 907614 | year = 2009 | doi = 10.1155/2009/907614 | PMID = 19746168 | pmc=2737134}}</ref> | |||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | author= | *{{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 | | *{{cite journal |vauthors=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=10.1111/j.1432-1033.1992.tb17255.x }} | ||
*{{cite journal | author=Sakai K |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=10.1016/S0888-7543(05)80301-5 |name-list-format=vanc| author2=Hirai M | author3=Kudoh J | display-authors=3 | last4=Minoshima | first4=Shinsei | last5=Shimizu | first5=Nobuyoshi }} | |||
*{{cite journal | author=Harlan DM |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= |name-list-format=vanc| author2=Graff JM | author3=Stumpo DJ | display-authors=3 | last4=Eddy Jr | first4=RL | last5=Shows | first5=TB | last6=Boyle | first6=JM | last7=Blackshear | first7=PJ }} | |||
*{{cite journal | author= | *{{cite journal |vauthors=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 |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=10.1111/j.1432-1033.1995.448_2.x |name-list-format=vanc| author2=Oehrlein SA | author3=Pappin DJ | display-authors=3 | last4=Rozengurt | first4=Enrique | last5=Parker | first5=Peter J. }} | |||
*{{cite journal | | *{{cite journal |vauthors=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=Herget T | *{{cite journal | author=Rao PH |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=10.1159/000133710 |name-list-format=vanc| author2=Murty VV | author3=Gaidano G | display-authors=3 | last4=Hauptschein | first4=R. | last5=Dalla-Favera | first5=R. | last6=Chaganti | first6=R.S.K. }} | ||
*{{cite journal |vauthors=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=Rao PH | *{{cite journal | author=Palmer RH |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=10.1016/0014-5793(95)01454-3 |name-list-format=vanc| author2=Schönwasser DC | author3=Rahman D | display-authors=3 | last4=Pappin | first4=DJ | last5=Herget | first5=T | last6=Parker | first6=PJ }} | ||
*{{cite journal |vauthors=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=10.1074/jbc.271.38.23424 }} | |||
*{{cite journal | | *{{cite journal |vauthors=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=10.1074/jbc.272.38.23833 }} | ||
*{{cite journal | author= | *{{cite journal | author=Qi Q |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=10.1074/jbc.275.13.9673 |name-list-format=vanc| author2=Rajala RV | author3=Anderson W | display-authors=3 | last4=Jiang | first4=C | last5=Rozwadowski | first5=K | last6=Selvaraj | first6=G | last7=Sharma | first7=R | last8=Datla | first8=R }} | ||
*{{cite journal | author=Jin Cho S |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 |name-list-format=vanc| author2=La M | author3=Ahn JK | display-authors=3 | last4=Meadows | first4=Gary G. | last5=Joe | first5=Cheol O. }} | |||
*{{cite journal | | *{{cite journal |vauthors=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 | | *{{cite journal |vauthors=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.M109572200 }} | ||
*{{cite journal | author= | *{{cite journal |author1=Sergio Alonso |author2=Undine Dietrich |author3=Chris Händel |author4=Josef A. Käs |author5=Markus Bär |title=Oscillations in the Lateral Pressure of Lipid Monolayers Induced by Nonlinear Chemical Dynamics of the Second Messengers MARCKS and Protein Kinase C |journal=Biophysical Journal |volume=100 |issue= 4 |pages= 939–947 |year= 2011 |pmid=21320438 |doi= 10.1016/j.bpj.2010.12.3702 |pmc=3037601}} | ||
*{{cite journal |author1=Jürgen Lippoldt |author2=Chris Händel |author3=Undine Dietrich |author4=Josef A. Käs |title=Dynamic membrane structure induces temporal pattern formation |journal=Biochimica et Biophysica Acta (BBA) - Biomembranes |volume=1838 |issue= 10 |pages= 2380–90 |year= 2014 |pmid=24866013 |doi= 10.1016/j.bbamem.2014.05.018}} | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
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Revision as of 01:49, 27 October 2017
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| External IDs | GeneCards: [1] | ||||||
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Myristoylated alanine-rich C-kinase substrate is a protein that in humans is encoded by the MARCKS gene.[1][2][3] It plays important roles in cell shape, cell motility, secretion, transmembrane transport, regulation of the cell cycle, and neural development.[4] Recently, MARCKS has been implicated in the exocytosis of a number of vesicles and granules such as mucin and chromaffin. It is also the name of a protein family, of which MARCKS is the most studied member. They are intrinsically disordered proteins, with an acidic pH, 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.[3]
Interactions
MARCKS has been shown to interact with TOB1[5] and with NMT2.[6]
References
- ↑ 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.
- ↑ Blackshear PJ (Feb 1993). "The MARCKS family of cellular protein kinase C substrates". J Biol Chem. 268 (3): 1501–4. PMID 8420923.
- ↑ 3.0 3.1 "Entrez Gene: MARCKS myristoylated alanine-rich protein kinase C substrate".
- ↑ 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. 328: 119–138. doi:10.1002/jez.b.22691.
- ↑ 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.
- ↑ 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. PMC 2737134. 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 3037601. 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.