Distantly related cousins of MAP kinase: biochemical properties and possible physiological functions
- PMID: 10600495
- DOI: 10.1006/bbrc.1999.1705
Distantly related cousins of MAP kinase: biochemical properties and possible physiological functions
Abstract
MAP kinases have been established to be key regulators of cellular signal transduction systems and are conserved from baker's yeast to human beings. Until now, three major types of mammalian MAP kinases (ERK, p38, and JNK/SAPK) have been reported and extensively studied. Advancement of genomic research as well as homology cloning techniques has revealed that there are several other protein kinase families that are structurally modestly related to those conventional MAP kinases. Indeed, most of them possess the TXY motif characteristic to MAP kinases in their activation loop, and can be regarded as members of the MAP kinase superfamily, yet some of them show closest overall similarity to Cdks. These kinases, all of mammalian origin, include MAK, MRK, MOK, p42KKIALRE, p56KKIAMRE, NLK, DYRK/Mnb, and Prp4. Although most of their physiological roles remain unknown, recent progress starts shedding some light on their functions.
Copyright 1999 Academic Press.
Similar articles
-
Cloning of DPK, a novel dendritic cell-derived protein kinase activating the ERK1/ERK2 and JNK/SAPK pathways.Biochem Biophys Res Commun. 2000 Aug 11;274(3):872-9. doi: 10.1006/bbrc.2000.3244. Biochem Biophys Res Commun. 2000. PMID: 10924369
-
Molecular cloning and characterization of a novel member of the MAP kinase superfamily.Genes Cells. 1999 May;4(5):299-309. doi: 10.1046/j.1365-2443.1999.00261.x. Genes Cells. 1999. PMID: 10421840
-
Characterisation of EmMPK1, an ERK-like MAP kinase from Echinococcus multilocularis which is activated in response to human epidermal growth factor.Int J Parasitol. 2006 Sep;36(10-11):1097-112. doi: 10.1016/j.ijpara.2006.05.008. Epub 2006 Jun 12. Int J Parasitol. 2006. PMID: 16793045
-
Mitogen-activated protein kinase signaling.Int Rev Neurobiol. 2004;59:201-20. doi: 10.1016/S0074-7742(04)59008-6. Int Rev Neurobiol. 2004. PMID: 15006489 Review.
-
Physiological roles of SAPK/JNK signaling pathway.J Biochem. 2004 Aug;136(2):123-6. doi: 10.1093/jb/mvh117. J Biochem. 2004. PMID: 15496581 Review.
Cited by
-
Identification of the autophosphorylation sites and characterization of their effects in the protein kinase DYRK1A.Biochem J. 2001 Nov 1;359(Pt 3):497-505. doi: 10.1042/0264-6021:3590497. Biochem J. 2001. PMID: 11672423 Free PMC article.
-
dDYRK2: a novel dual-specificity tyrosine-phosphorylation-regulated kinase in Drosophila.Biochem J. 2003 Sep 1;374(Pt 2):381-91. doi: 10.1042/BJ20030500. Biochem J. 2003. PMID: 12786602 Free PMC article.
-
The promoter for intestinal cell kinase is head-to-head with F-Box 9 and contains functional sites for TCF7L2 and FOXA factors.Mol Cancer. 2010 May 11;9:104. doi: 10.1186/1476-4598-9-104. Mol Cancer. 2010. PMID: 20459822 Free PMC article.
-
Parasite mitogen-activated protein kinases as drug discovery targets to treat human protozoan pathogens.J Signal Transduct. 2011;2011:971968. doi: 10.1155/2011/971968. Epub 2011 Feb 27. J Signal Transduct. 2011. PMID: 21637385 Free PMC article.
-
How ERK1/2 activation controls cell proliferation and cell death: Is subcellular localization the answer?Cell Cycle. 2009 Apr 15;8(8):1168-75. doi: 10.4161/cc.8.8.8147. Epub 2009 Apr 11. Cell Cycle. 2009. PMID: 19282669 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Research Materials
Miscellaneous