DGKZ

From Wikipedia, the free encyclopedia

Diacylglycerol kinase, zeta 104kDa

Identifiers

DGKZ; DAGK5; DAGK6; DGK-ZETA; hDGKzeta

External IDs

OMIM: 601441 MGI: 1278339 HomoloGene: 37831

Gene ontology
Molecular Function:	• diacylglycerol kinase activity • protein binding • ATP binding • zinc ion binding • transferase activity • diacylglycerol binding • metal ion binding
Cellular Component:	• nucleus
Biological Process:	• protein kinase C activation • intracellular signaling cascade

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003646 (mRNA)
NP_003637 (protein)

NM_138306 (mRNA)
NP_612179 (protein)

Location

Chr 11: 46.31 - 46.36 Mb

Chr 2: 91.73 - 91.76 Mb

Pubmed search

[1]

[2]

Diacylglycerol kinase, zeta 104kDa, also known as DGKZ, is a human gene.^[1]

The protein encoded by this gene belongs to the eukaryotic diacylglycerol kinase family. It may attenuate protein kinase C activity by regulating diacylglycerol levels in intracellular signaling cascade and signal transduction. Alternative splicing occurs at this locus and three transcript variants encoding three distinct isoforms have been identified.^[1]

[edit] References

^ ^a ^b Entrez Gene: DGKZ diacylglycerol kinase, zeta 104kDa.

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Bunting M, Tang W, Zimmerman GA, et al. (1996). "Molecular cloning and characterization of a novel human diacylglycerol kinase zeta.". J. Biol. Chem. 271 (17): 10230–6. PMID 8626588.
Ding L, Bunting M, Topham MK, et al. (1997). "Alternative splicing of the human diacylglycerol kinase zeta gene in muscle.". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5519–24. PMID 9159104.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Topham MK, Bunting M, Zimmerman GA, et al. (1998). "Protein kinase C regulates the nuclear localization of diacylglycerol kinase-zeta.". Nature 394 (6694): 697–700. doi:10.1038/29337. PMID 9716136.
Liu Z, Chang GQ, Leibowitz SF (2001). "Diacylglycerol kinase zeta in hypothalamus interacts with long form leptin receptor. Relation to dietary fat and body weight regulation.". J. Biol. Chem. 276 (8): 5900–7. doi:10.1074/jbc.M007311200. PMID 11078732.
Topham MK, Prescott SM (2001). "Diacylglycerol kinase zeta regulates Ras activation by a novel mechanism.". J. Cell Biol. 152 (6): 1135–43. PMID 11257115.
Hogan A, Shepherd L, Chabot J, et al. (2001). "Interaction of gamma 1-syntrophin with diacylglycerol kinase-zeta. Regulation of nuclear localization by PDZ interactions.". J. Biol. Chem. 276 (28): 26526–33. doi:10.1074/jbc.M104156200. PMID 11352924.
Santos T, Carrasco S, Jones DR, et al. (2002). "Dynamics of diacylglycerol kinase zeta translocation in living T-cells. Study of the structural domain requirements for translocation and activity.". J. Biol. Chem. 277 (33): 30300–9. doi:10.1074/jbc.M200999200. PMID 12015310.
Zhong XP, Hainey EA, Olenchock BA, et al. (2002). "Regulation of T cell receptor-induced activation of the Ras-ERK pathway by diacylglycerol kinase zeta.". J. Biol. Chem. 277 (34): 31089–98. doi:10.1074/jbc.M203818200. PMID 12070163.
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.
Zhong XP, Hainey EA, Olenchock BA, et al. (2003). "Enhanced T cell responses due to diacylglycerol kinase zeta deficiency.". Nat. Immunol. 4 (9): 882–90. doi:10.1038/ni958. PMID 12883552.
Luo B, Prescott SM, Topham MK (2003). "Protein kinase C alpha phosphorylates and negatively regulates diacylglycerol kinase zeta.". J. Biol. Chem. 278 (41): 39542–7. doi:10.1074/jbc.M307153200. PMID 12890670.
Abramovici H, Hogan AB, Obagi C, et al. (2004). "Diacylglycerol kinase-zeta localization in skeletal muscle is regulated by phosphorylation and interaction with syntrophins.". Mol. Biol. Cell 14 (11): 4499–511. doi:10.1091/mbc.E03-03-0190. PMID 14551255.
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.
Davidson L, Pawson AJ, López de Maturana R, et al. (2004). "Gonadotropin-releasing hormone-induced activation of diacylglycerol kinase-zeta and its association with active c-src.". J. Biol. Chem. 279 (12): 11906–16. doi:10.1074/jbc.M310784200. PMID 14707140.
Luo B, Prescott SM, Topham MK (2005). "Diacylglycerol kinase zeta regulates phosphatidylinositol 4-phosphate 5-kinase Ialpha by a novel mechanism.". Cell. Signal. 16 (8): 891–7. doi:10.1016/j.cellsig.2004.01.010. PMID 15157668.
Avila-Flores A, Santos T, Rincón E, Mérida I (2005). "Modulation of the mammalian target of rapamycin pathway by diacylglycerol kinase-produced phosphatidic acid.". J. Biol. Chem. 280 (11): 10091–9. doi:10.1074/jbc.M412296200. PMID 15632115.
Los AP, Vinke FP, de Widt J, et al. (2006). "The retinoblastoma family proteins bind to and activate diacylglycerol kinase zeta.". J. Biol. Chem. 281 (2): 858–66. doi:10.1074/jbc.M502693200. PMID 16286473.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.