STK4

From Wikipedia, the free encyclopedia

Serine/threonine kinase 4

PDB rendering based on 2jo8.

Available structures: 2jo8

Identifiers

Symbol(s)

STK4; MST1; DKFZp686A2068; KRS2; YSK3

External IDs

OMIM: 604965 MGI: 1929004 HomoloGene: 55965

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • protein serine/threonine kinase activity • protein-tyrosine kinase activity • ATP binding • transcription factor binding • transferase activity • protein homodimerization activity
Cellular Component:	• nucleus • cytoplasm • integral to membrane
Biological Process:	• cell morphogenesis • protein amino acid phosphorylation • apoptosis • signal transduction • cell surface receptor linked signal transduction • protein kinase cascade • peptidyl-serine phosphorylation • positive regulation of apoptosis • protein amino acid autophosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006282 (mRNA)
NP_006273 (protein)

NM_021420 (mRNA)
NP_067395 (protein)

Location

Chr 20: 43.03 - 43.14 Mb

Chr 2: 163.77 - 163.85 Mb

Pubmed search

[1]

[2]

Serine/threonine kinase 4, also known as STK4, is a human gene.

The protein encoded by this gene is a cytoplasmic kinase that is structurally similar to the yeast Ste20p kinase, which acts upstream of the stress-induced mitogen-activated protein kinase cascade. The encoded protein can phosphorylate myelin basic protein and undergoes autophosphorylation. A caspase-cleaved fragment of the encoded protein has been shown to be capable of phosphorylating histone H2B. The particular phosphorylation catalyzed by this protein has been correlated with apoptosis, and it's possible that this protein induces the chromatin condensation observed in this process.^[1]

[edit] References

^ Entrez Gene: STK4 serine/threonine kinase 4.

[edit] Further reading

de Souza PM, Lindsay MA (2005). "Mammalian Sterile20-like kinase 1 and the regulation of apoptosis.". Biochem. Soc. Trans. 32 (Pt3): 485–8. doi:10.1042/BST0320485. PMID 15157167.
Han S, Stuart LA, Degen SJ (1991). "Characterization of the DNF15S2 locus on human chromosome 3: identification of a gene coding for four kringle domains with homology to hepatocyte growth factor.". Biochemistry 30 (40): 9768–80. PMID 1655021.
Gerber MJ, Drabkin HA, Firnhaber C, et al. (1988). "Regional localization of chromosome 3-specific DNA fragments by using a hybrid cell deletion mapping panel.". Am. J. Hum. Genet. 43 (4): 442–51. PMID 2902784.
Creasy CL, Chernoff J (1995). "Cloning and characterization of a human protein kinase with homology to Ste20.". J. Biol. Chem. 270 (37): 21695–700. PMID 7665586.
Schultz SJ, Nigg EA (1994). "Identification of 21 novel human protein kinases, including 3 members of a family related to the cell cycle regulator nimA of Aspergillus nidulans.". Cell Growth Differ. 4 (10): 821–30. PMID 8274451.
Creasy CL, Chernoff J (1996). "Cloning and characterization of a member of the MST subfamily of Ste20-like kinases.". Gene 167 (1-2): 303–6. PMID 8566796.
Creasy CL, Ambrose DM, Chernoff J (1996). "The Ste20-like protein kinase, Mst1, dimerizes and contains an inhibitory domain.". J. Biol. Chem. 271 (35): 21049–53. PMID 8702870.
Taylor LK, Wang HC, Erikson RL (1996). "Newly identified stress-responsive protein kinases, Krs-1 and Krs-2.". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10099–104. PMID 8816758.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Graves JD, Gotoh Y, Draves KE, et al. (1998). "Caspase-mediated activation and induction of apoptosis by the mammalian Ste20-like kinase Mst1.". EMBO J. 17 (8): 2224–34. doi:10.1093/emboj/17.8.2224. PMID 9545236.
Lee KK, Ohyama T, Yajima N, et al. (2001). "MST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activation.". J. Biol. Chem. 276 (22): 19276–85. doi:10.1074/jbc.M005109200. PMID 11278283.
Graves JD, Draves KE, Gotoh Y, et al. (2001). "Both phosphorylation and caspase-mediated cleavage contribute to regulation of the Ste20-like protein kinase Mst1 during CD95/Fas-induced apoptosis.". J. Biol. Chem. 276 (18): 14909–15. doi:10.1074/jbc.M010905200. PMID 11278782.
Ura S, Masuyama N, Graves JD, Gotoh Y (2001). "Caspase cleavage of MST1 promotes nuclear translocation and chromatin condensation.". Proc. Natl. Acad. Sci. U.S.A. 98 (18): 10148–53. doi:10.1073/pnas.181161698. PMID 11517310.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Lee KK, Yonehara S (2002). "Phosphorylation and dimerization regulate nucleocytoplasmic shuttling of mammalian STE20-like kinase (MST).". J. Biol. Chem. 277 (14): 12351–8. doi:10.1074/jbc.M108138200. PMID 11805089.
Khokhlatchev A, Rabizadeh S, Xavier R, et al. (2002). "Identification of a novel Ras-regulated proapoptotic pathway.". Curr. Biol. 12 (4): 253–65. PMID 11864565.
De Souza PM, Kankaanranta H, Michael A, et al. (2002). "Caspase-catalyzed cleavage and activation of Mst1 correlates with eosinophil but not neutrophil apoptosis.". Blood 99 (9): 3432–8. PMID 11964314.
Glantschnig H, Rodan GA, Reszka AA (2003). "Mapping of MST1 kinase sites of phosphorylation. Activation and autophosphorylation.". J. Biol. Chem. 277 (45): 42987–96. doi:10.1074/jbc.M208538200. PMID 12223493.
Lin Y, Khokhlatchev A, Figeys D, Avruch J (2003). "Death-associated protein 4 binds MST1 and augments MST1-induced apoptosis.". J. Biol. Chem. 277 (50): 47991–8001. doi:10.1074/jbc.M202630200. PMID 12384512.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. doi:10.1073/pnas.242603899. PMID 12477932.