ZAK
Sterile alpha motif and leucine zipper containing kinase AZK, also known as ZAK, is a human gene.[1]
This gene is a member of the MAPKKK family of signal transduction molecules and encodes a protein with an N-terminal kinase catalytic domain, followed by a leucine zipper motif and a sterile-alpha motif (SAM). This magnesium-binding protein forms homodimers and is located in the cytoplasm. The protein mediates gamma radiation signaling leading to cell cycle arrest and activity of this protein plays a role in cell cycle checkpoint regulation in cells. The protein also has pro-apoptotic activity. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[1]
Interactions
ZAK has been shown to interact with ZNF33A.[2]
References
- ↑ 1.0 1.1 “Entrez Gene: ZAK sterile alpha motif and leucine zipper containing kinase AZK”.
- ↑ Yang, Jaw-Ji (Jan 2003). “A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the ZAK-expressing cells re-entering the cell cycle”. Biochem. Biophys. Res. Commun. United States. 301 (1): 71–7. doi:10.1016/S0006-291X(02)02980-7. ISSN 0006-291X. PMID 12535642.
Further reading
- Liu TC, Huang CJ, Chu YC, et al. (2000). “Cloning and expression of ZAK, a mixed lineage kinase-like protein containing a leucine-zipper and a sterile-alpha motif”. Biochem. Biophys. Res. Commun. 274 (3): 811–6. doi:10.1006/bbrc.2000.3236. PMID 10924358.
- Gotoh I, Adachi M, Nishida E (2001). “Identification and characterization of a novel MAP kinase kinase kinase, MLTK”. J. Biol. Chem. 276 (6): 4276–86. doi:10.1074/jbc.M008595200. PMID 11042189.
- Bloem LJ, Pickard TR, Acton S, et al. (2002). “Tissue distribution and functional expression of a cDNA encoding a novel mixed lineage kinase”. J. Mol. Cell. Cardiol. 33 (9): 1739–50. doi:10.1006/jmcc.2001.1437. PMID 11549352.
- Gross EA, Callow MG, Waldbaum L, et al. (2002). “MRK, a mixed lineage kinase-related molecule that plays a role in gamma-radiation-induced cell cycle arrest”. J. Biol. Chem. 277 (16): 13873–82. doi:10.1074/jbc.M111994200. PMID 11836244.
- Yang JJ (2002). “Mixed lineage kinase ZAK utilizing MKK7 and not MKK4 to activate the c-Jun N-terminal kinase and playing a role in the cell arrest”. Biochem. Biophys. Res. Commun. 297 (1): 105–10. doi:10.1016/S0006-291X(02)02123-X. PMID 12220515.
- 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. Bibcode:2002PNAS…9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Yang JJ (2003). “A novel zinc finger protein, ZZaPK, interacts with ZAK and stimulates the ZAK-expressing cells re-entering the cell cycle”. Biochem. Biophys. Res. Commun. 301 (1): 71–7. doi:10.1016/S0006-291X(02)02980-7. PMID 12535642.
- Takahashi M, Gotoh Y, Isagawa T, et al. (2004). “Regulation of a mitogen-activated protein kinase kinase kinase, MLTK by PKN”. J. Biochem. 133 (2): 181–7. doi:10.1093/jb/mvg022. PMID 12761180.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). “Complete sequencing and characterization of 21,243 full-length human cDNAs”. Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
- Cho YY, Bode AM, Mizuno H, et al. (2004). “A novel role for mixed-lineage kinase-like mitogen-activated protein triple kinase alpha in neoplastic cell transformation and tumor development”. Cancer Res. 64 (11): 3855–64. doi:10.1158/0008-5472.CAN-04-0201. PMID 15172994.
- Jin J, Smith FD, Stark C, et al. (2004). “Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization”. Curr. Biol. 14 (16): 1436–50. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- Tosti E, Waldbaum L, Warshaw G, et al. (2005). “The stress kinase MRK contributes to regulation of DNA damage checkpoints through a p38gamma-independent pathway”. J. Biol. Chem. 279 (46): 47652–60. doi:10.1074/jbc.M409961200. PMID 15342622.
- Huang CY, Kuo WW, Chueh PJ, et al. (2004). “Transforming growth factor-beta induces the expression of ANF and hypertrophic growth in cultured cardiomyoblast cells through ZAK”. Biochem. Biophys. Res. Commun. 324 (1): 424–31. doi:10.1016/j.bbrc.2004.09.067. PMID 15465036.
- Huang CY, Chueh PJ, Tseng CT, et al. (2004). “ZAK re-programs atrial natriuretic factor expression and induces hypertrophic growth in H9c2 cardiomyoblast cells”. Biochem. Biophys. Res. Commun. 324 (3): 973–80. doi:10.1016/j.bbrc.2004.09.156. PMID 15485649.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Choi HS, Choi BY, Cho YY, et al. (2005). “Phosphorylation of Ser28 in histone H3 mediated by mixed lineage kinase-like mitogen-activated protein triple kinase alpha”. J. Biol. Chem. 280 (14): 13545–53. doi:10.1074/jbc.M410521200. PMID 15684425.
- Wang X, Mader MM, Toth JE, et al. (2005). “Complete inhibition of anisomycin and UV radiation but not cytokine induced JNK and p38 activation by an aryl-substituted dihydropyrrolopyrazole quinoline and mixed lineage kinase 7 small interfering RNA”. J. Biol. Chem. 280 (19): 19298–305. doi:10.1074/jbc.M413059200. PMID 15737997.
- Benzinger A, Muster N, Koch HB, et al. (2005). “Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer”. Mol. Cell. Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
- Hillier LW, Graves TA, Fulton RS, et al. (2005). “Generation and annotation of the DNA sequences of human chromosomes 2 and 4”. Nature. 434 (7034): 724–31. Bibcode:2005Natur.434..724H. doi:10.1038/nature03466. PMID 15815621.
- Rual JF, Venkatesan K, Hao T, et al. (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514.
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