Biology:STK4
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Serine/threonine-protein kinase 4 is an enzyme that in humans is encoded by the STK4 gene.[1][2][3]
Function
The protein encoded by this gene is a cytoplasmic kinase that is structurally similar to the yeast Ste20p (sterile 20 protein) kinase, which acts upstream of the stress-induced mitogen-activated protein kinase (MAPK) 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.[4]
Interactions
STK4 has been shown to interact with PRKRIR.[5]
STK4 has also been shown to prevent, through Yap1 coactivator modulation, haematological tumor cell apoptosis.[6]
References
- ↑ "Newly identified stress-responsive protein kinases, Krs-1 and Krs-2". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10099–104. November 1996. doi:10.1073/pnas.93.19.10099. PMID 8816758. Bibcode: 1996PNAS...9310099T.
- ↑ "Caspase-mediated activation and induction of apoptosis by the mammalian Ste20-like kinase Mst1". EMBO J. 17 (8): 2224–34. June 1998. doi:10.1093/emboj/17.8.2224. PMID 9545236.
- ↑ "Caspase cleavage of MST1 promotes nuclear translocation and chromatin condensation". Proc. Natl. Acad. Sci. U.S.A. 98 (18): 10148–53. August 2001. doi:10.1073/pnas.181161698. PMID 11517310. Bibcode: 2001PNAS...9810148U.
- ↑ "Entrez Gene: STK4 serine/threonine kinase 4". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6789.
- ↑ "Death-associated protein 4 binds MST1 and augments MST1-induced apoptosis". J. Biol. Chem. 277 (50): 47991–8001. December 2002. doi:10.1074/jbc.M202630200. PMID 12384512.
- ↑ "Rescue of Hippo coactivator YAP1 triggers DNA damage-induced apoptosis in hematological cancers". Nat. Med. 20 (6): 599–606. 2014. doi:10.1038/nm.3562. PMID 24813251. PMC 4057660. https://dash.harvard.edu/bitstream/handle/1/13581189/4057660.pdf?sequence=1.
Further reading
- Kaeberlein, Matt, ed (2009). "Mst1-FoxO signaling protects Naïve T lymphocytes from cellular oxidative stress in mice". PLOS ONE 4 (11): e8011. doi:10.1371/journal.pone.0008011. PMID 19956688. Bibcode: 2009PLoSO...4.8011C.
- "Mammalian Sterile20-like kinase 1 and the regulation of apoptosis". Biochem. Soc. Trans. 32 (Pt3): 485–8. 2004. doi:10.1042/BST0320485. PMID 15157167.
- "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. 1991. doi:10.1021/bi00104a029. PMID 1655021.
- "Regional localization of chromosome 3-specific DNA fragments by using a hybrid cell deletion mapping panel". Am. J. Hum. Genet. 43 (4): 442–51. 1988. PMID 2902784.
- "Cloning and characterization of a human protein kinase with homology to Ste20". J. Biol. Chem. 270 (37): 21695–700. 1995. doi:10.1074/jbc.270.37.21695. PMID 7665586.
- "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. 1993. PMID 8274451.
- "Cloning and characterization of a member of the MST subfamily of Ste20-like kinases". Gene 167 (1–2): 303–6. 1995. doi:10.1016/0378-1119(95)00653-2. PMID 8566796.
- "The Ste20-like protein kinase, Mst1, dimerizes and contains an inhibitory domain". J. Biol. Chem. 271 (35): 21049–53. 1996. doi:10.1074/jbc.271.35.21049. PMID 8702870.
- "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. 1996. doi:10.1101/gr.6.9.791. PMID 8889548.
- "MST, a physiological caspase substrate, highly sensitizes apoptosis both upstream and downstream of caspase activation". J. Biol. Chem. 276 (22): 19276–85. 2001. doi:10.1074/jbc.M005109200. PMID 11278283.
- "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. 2001. doi:10.1074/jbc.M010905200. PMID 11278782.
- "Phosphorylation and dimerization regulate nucleocytoplasmic shuttling of mammalian STE20-like kinase (MST)". J. Biol. Chem. 277 (14): 12351–8. 2002. doi:10.1074/jbc.M108138200. PMID 11805089.
- "Identification of a novel Ras-regulated proapoptotic pathway". Curr. Biol. 12 (4): 253–65. 2002. doi:10.1016/S0960-9822(02)00683-8. PMID 11864565.
- "Caspase-catalyzed cleavage and activation of Mst1 correlates with eosinophil but not neutrophil apoptosis". Blood 99 (9): 3432–8. 2002. doi:10.1182/blood.V99.9.3432. PMID 11964314.
- "Mapping of MST1 kinase sites of phosphorylation. Activation and autophosphorylation". J. Biol. Chem. 277 (45): 42987–96. 2002. doi:10.1074/jbc.M208538200. PMID 12223493.
- "Death-associated protein 4 binds MST1 and augments MST1-induced apoptosis". J. Biol. Chem. 277 (50): 47991–8001. 2002. doi:10.1074/jbc.M202630200. PMID 12384512.
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