MARK1 explained

Serine/threonine-protein kinase MARK1 is an enzyme that in humans is encoded by the MARK1 gene.^{[1] [2]}

Further reading

• Drewes G, Trinczek B, Illenberger S, etal . Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. . J. Biol. Chem. . 270 . 13 . 7679–88 . 1995 . 7706316 . 10.1074/jbc.270.13.7679. free .
• Yang SD, Yu JS, Shiah SG, Huang JJ . Protein kinase FA/glycogen synthase kinase-3 alpha after heparin potentiation phosphorylates tau on sites abnormally phosphorylated in Alzheimer's disease brain. . J. Neurochem. . 63 . 4 . 1416–25 . 1994 . 7931292 . 10.1046/j.1471-4159.1994.63041416.x . 85176778 .
• Illenberger S, Drewes G, Trinczek B, etal . Phosphorylation of microtubule-associated proteins MAP2 and MAP4 by the protein kinase p110mark. Phosphorylation sites and regulation of microtubule dynamics. . J. Biol. Chem. . 271 . 18 . 10834–43 . 1996 . 8631898 . 10.1074/jbc.271.18.10834. free .
• Paudel HK . The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase. . J. Biol. Chem. . 272 . 3 . 1777–85 . 1997 . 8999860 . 10.1016/S0021-9258(19)67481-8 . free .
• Sengupta A, Kabat J, Novak M, etal . Phosphorylation of tau at both Thr 231 and Ser 262 is required for maximal inhibition of its binding to microtubules. . Arch. Biochem. Biophys. . 357 . 2 . 299–309 . 1998 . 9735171 . 10.1006/abbi.1998.0813 .
• Wang JZ, Wu Q, Smith A, etal . Tau is phosphorylated by GSK-3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A-kinase. . FEBS Lett. . 436 . 1 . 28–34 . 1998 . 9771888 . 10.1016/S0014-5793(98)01090-4 . free .
• Hanger DP, Betts JC, Loviny TL, etal . New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry. . J. Neurochem. . 71 . 6 . 2465–76 . 1998 . 9832145 . 10.1046/j.1471-4159.1998.71062465.x . free .
• Schneider A, Biernat J, von Bergen M, etal . Phosphorylation that detaches tau protein from microtubules (Ser262, Ser214) also protects it against aggregation into Alzheimer paired helical filaments. . Biochemistry . 38 . 12 . 3549–58 . 1999 . 10090741 . 10.1021/bi981874p .
• Reynolds CH, Betts JC, Blackstock WP, etal . Phosphorylation sites on tau identified by nanoelectrospray mass spectrometry: differences in vitro between the mitogen-activated protein kinases ERK2, c-Jun N-terminal kinase and P38, and glycogen synthase kinase-3beta. . J. Neurochem. . 74 . 4 . 1587–95 . 2000 . 10737616 . 10.1046/j.1471-4159.2000.0741587.x . free .
• Nagase T, Kikuno R, Ishikawa K, etal . Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. . DNA Res. . 7 . 2 . 143–50 . 2000 . 10819331 . 10.1093/dnares/7.2.143 . free .
• Liu F, Iqbal K, Grundke-Iqbal I, Gong CX . Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK-3beta. . FEBS Lett. . 530 . 1–3 . 209–14 . 2002 . 12387894 . 10.1016/S0014-5793(02)03487-7 . free .
• Liu F, Zaidi T, Iqbal K, etal . Aberrant glycosylation modulates phosphorylation of tau by protein kinase A and dephosphorylation of tau by protein phosphatase 2A and 5 . Neuroscience . 115 . 3 . 829–37 . 2003 . 12435421 . 10.1016/S0306-4522(02)00510-9 . 26118803 .
• Strausberg RL, Feingold EA, Grouse LH, etal . Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences . Proc. Natl. Acad. Sci. U.S.A. . 99 . 26 . 16899–903 . 2003 . 12477932 . 10.1073/pnas.242603899 . 139241 . 2002PNAS...9916899M . free .
• Timm T, Li XY, Biernat J, etal . MARKK, a Ste20-like kinase, activates the polarity-inducing kinase MARK/PAR-1 . EMBO J. . 22 . 19 . 5090–101 . 2003 . 14517247 . 10.1093/emboj/cdg447 . 204455 .
• Trinczek B, Brajenovic M, Ebneth A, Drewes G . MARK4 is a novel microtubule-associated proteins/microtubule affinity-regulating kinase that binds to the cellular microtubule network and to centrosomes . J. Biol. Chem. . 279 . 7 . 5915–23 . 2004 . 14594945 . 10.1074/jbc.M304528200 . free .
• Ota T, Suzuki Y, Nishikawa T, etal . Complete sequencing and characterization of 21,243 full-length human cDNAs . Nat. Genet. . 36 . 1 . 40–5 . 2004 . 14702039 . 10.1038/ng1285 . free .
• Lizcano JM, Göransson O, Toth R, etal . LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1 . EMBO J. . 23 . 4 . 833–43 . 2005 . 14976552 . 10.1038/sj.emboj.7600110 . 381014 .
• Gerhard DS, Wagner L, Feingold EA, etal . The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC) . Genome Res. . 14 . 10B . 2121–7 . 2004 . 15489334 . 10.1101/gr.2596504 . 528928 .
• Benzinger A, Muster N, Koch HB, etal . Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer . Mol. Cell. Proteomics . 4 . 6 . 785–95 . 2005 . 15778465 . 10.1074/mcp.M500021-MCP200 . free .

Notes and References

1. Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E . MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption . Cell . 89 . 2 . 297–308 . May 1997 . 9108484 . 10.1016/S0092-8674(00)80208-1 . 15647848 . free .
2. Web site: Entrez Gene: MARK1 MAP/microtubule affinity-regulating kinase 1.