DGKG: Difference between revisions
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'''Diacylglycerol kinase gamma''' is an [[enzyme]] that in humans is encoded by the ''DGKG'' [[gene]].<ref name="pmid8034597">{{cite journal | vauthors = Kai M, Sakane F, Imai S, Wada I, Kanoh H | title = Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in [[human retina]] with a truncated and inactive enzyme expression in most other human cells | journal = J Biol Chem | volume = 269 | issue = 28 | pages = 18492–8 |date=Aug 1994 | pmid = 8034597 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DGKG diacylglycerol kinase, gamma 90kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1608| accessdate = }}</ref> | |||
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| summary_text = This gene encodes an enzyme that is a member of the type I subfamily of diacylglycerol kinases, which are involved in lipid metabolism. These enzymes generate phosphatidic acid by catalyzing the phosphorylation of diacylglycerol, a fundamental lipid second messenger that activates numerous proteins, including protein kinase C isoforms, Ras guanyl nucleotide-releasing proteins and some transient receptor potential channels. Diacylglycerol kinase gamma has been implicated in cell cycle regulation and in the negative regulation of macrophage differentiation in leukemia cells. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez" | | summary_text = This gene encodes an enzyme that is a member of the type I subfamily of diacylglycerol kinases, which are involved in lipid metabolism. These enzymes generate phosphatidic acid by catalyzing the phosphorylation of diacylglycerol, a fundamental lipid second messenger that activates numerous proteins, including protein kinase C isoforms, Ras guanyl nucleotide-releasing proteins and some transient receptor potential channels. Diacylglycerol kinase gamma has been implicated in cell cycle regulation and in the negative regulation of macrophage differentiation in leukemia cells. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez" /> | ||
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==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
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| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Brose N, Betz A, Wegmeyer H |title=Divergent and convergent signaling by the diacylglycerol second messenger pathway in mammals. |journal=Curr. Opin. Neurobiol. |volume=14 |issue= 3 |pages= 328–40 |year= 2004 |pmid= 15194113 |doi= 10.1016/j.conb.2004.05.006 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Luo B, Regier DS, Prescott SM, Topham MK |title=Diacylglycerol kinases. |journal=Cell. Signal. |volume=16 |issue= 9 |pages= 983–9 |year= 2005 |pmid= 15212759 |doi= 10.1016/j.cellsig.2004.03.016 }} | ||
*{{cite journal | author=Topham MK |title=Signaling roles of diacylglycerol kinases. |journal=J. Cell. Biochem. |volume=97 |issue= 3 |pages= | *{{cite journal | author=Topham MK |title=Signaling roles of diacylglycerol kinases. |journal=J. Cell. Biochem. |volume=97 |issue= 3 |pages= 474–84 |year= 2006 |pmid= 16288460 |doi= 10.1002/jcb.20704 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=10.1101/gr.6.9.791 }} | ||
*{{cite journal | vauthors=Yamada K, Sakane F, Matsushima N, Kanoh H |title=EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes. | series=321 |journal=Biochem. J. |volume=( Pt 1) |issue= |pages= 59–64 |year= 1997 |pmid= 9003401 |doi= | pmc=1218036 }} | |||
*{{cite journal | | *{{cite journal | vauthors=Stöhr H, Klein J, Gehrig A |title=Mapping and genomic characterization of the gene encoding diacylglycerol kinase gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1). |journal=Hum. Genet. |volume=104 |issue= 1 |pages= 99–105 |year= 1999 |pmid= 10071200 |doi=10.1007/s004390050917 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Yamada K, Sakane F, Imai S |title=Regulatory role of diacylglycerol kinase gamma in macrophage differentiation of leukemia cells. |journal=Biochem. Biophys. Res. Commun. |volume=305 |issue= 1 |pages= 101–7 |year= 2003 |pmid= 12732202 |doi=10.1016/S0006-291X(03)00713-7 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Oyaizu K, Kantarci A, Maeda H |title=Identification of mRNAs for the various diacylglycerol kinase isoforms in neutrophils from patients with localized aggressive periodontitis. |journal=J. Periodont. Res. |volume=38 |issue= 5 |pages= 488–95 |year= 2003 |pmid= 12941073 |doi=10.1034/j.1600-0765.2003.00680.x |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Tsushima S, Kai M, Yamada K |title=Diacylglycerol kinase gamma serves as an upstream suppressor of Rac1 and lamellipodium formation. |journal=J. Biol. Chem. |volume=279 |issue= 27 |pages= 28603–13 |year= 2004 |pmid= 15102830 |doi= 10.1074/jbc.M314031200 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Filosto M, Mancuso M, Tomelleri G |title=Hepato-cerebral syndrome: genetic and pathological studies in an infant with a dGK mutation. |journal=Acta Neuropathol. |volume=108 |issue= 2 |pages= 168–71 |year= 2004 |pmid= 15150663 |doi= 10.1007/s00401-004-0872-9 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Batista EL, Warbington M, Badwey JA, Van Dyke TE |title=Differentiation of HL-60 cells to granulocytes involves regulation of select diacylglycerol kinases (DGKs). |journal=J. Cell. Biochem. |volume=94 |issue= 4 |pages= 774–93 |year= 2005 |pmid= 15578578 |doi= 10.1002/jcb.20356 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Matsubara T, Shirai Y, Miyasaka K |title=Nuclear transportation of diacylglycerol kinase gamma and its possible function in the nucleus. |journal=J. Biol. Chem. |volume=281 |issue= 10 |pages= 6152–64 |year= 2006 |pmid= 16407189 |doi= 10.1074/jbc.M509873200 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Yamaguchi Y, Shirai Y, Matsubara T |title=Phosphorylation and up-regulation of diacylglycerol kinase gamma via its interaction with protein kinase C gamma. |journal=J. Biol. Chem. |volume=281 |issue= 42 |pages= 31627–37 |year= 2006 |pmid= 16905533 |doi= 10.1074/jbc.M606992200 |display-authors=etal}} | ||
*{{cite journal | | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
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[[Category:EF-hand-containing proteins]] |
Latest revision as of 17:08, 27 November 2017
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External IDs | GeneCards: [1] | ||||||
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Species | Human | Mouse | |||||
Entrez |
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Location (UCSC) | n/a | n/a | |||||
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Diacylglycerol kinase gamma is an enzyme that in humans is encoded by the DGKG gene.[1][2]
This gene encodes an enzyme that is a member of the type I subfamily of diacylglycerol kinases, which are involved in lipid metabolism. These enzymes generate phosphatidic acid by catalyzing the phosphorylation of diacylglycerol, a fundamental lipid second messenger that activates numerous proteins, including protein kinase C isoforms, Ras guanyl nucleotide-releasing proteins and some transient receptor potential channels. Diacylglycerol kinase gamma has been implicated in cell cycle regulation and in the negative regulation of macrophage differentiation in leukemia cells. Multiple transcript variants encoding different isoforms have been found for this gene.[2]
References
- ↑ Kai M, Sakane F, Imai S, Wada I, Kanoh H (Aug 1994). "Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells". J Biol Chem. 269 (28): 18492–8. PMID 8034597.
- ↑ 2.0 2.1 "Entrez Gene: DGKG diacylglycerol kinase, gamma 90kDa".
Further reading
- Brose N, Betz A, Wegmeyer H (2004). "Divergent and convergent signaling by the diacylglycerol second messenger pathway in mammals". Curr. Opin. Neurobiol. 14 (3): 328–40. doi:10.1016/j.conb.2004.05.006. PMID 15194113.
- Luo B, Regier DS, Prescott SM, Topham MK (2005). "Diacylglycerol kinases". Cell. Signal. 16 (9): 983–9. doi:10.1016/j.cellsig.2004.03.016. PMID 15212759.
- Topham MK (2006). "Signaling roles of diacylglycerol kinases". J. Cell. Biochem. 97 (3): 474–84. doi:10.1002/jcb.20704. PMID 16288460.
- Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
- Yamada K, Sakane F, Matsushima N, Kanoh H (1997). "EF-hand motifs of alpha, beta and gamma isoforms of diacylglycerol kinase bind calcium with different affinities and conformational changes". Biochem. J. 321. ( Pt 1): 59–64. PMC 1218036. PMID 9003401.
- Stöhr H, Klein J, Gehrig A, et al. (1999). "Mapping and genomic characterization of the gene encoding diacylglycerol kinase gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1)". Hum. Genet. 104 (1): 99–105. doi:10.1007/s004390050917. PMID 10071200.
- 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. PMC 139241. PMID 12477932.
- Yamada K, Sakane F, Imai S, et al. (2003). "Regulatory role of diacylglycerol kinase gamma in macrophage differentiation of leukemia cells". Biochem. Biophys. Res. Commun. 305 (1): 101–7. doi:10.1016/S0006-291X(03)00713-7. PMID 12732202.
- Oyaizu K, Kantarci A, Maeda H, et al. (2003). "Identification of mRNAs for the various diacylglycerol kinase isoforms in neutrophils from patients with localized aggressive periodontitis". J. Periodont. Res. 38 (5): 488–95. doi:10.1034/j.1600-0765.2003.00680.x. PMID 12941073.
- Tsushima S, Kai M, Yamada K, et al. (2004). "Diacylglycerol kinase gamma serves as an upstream suppressor of Rac1 and lamellipodium formation". J. Biol. Chem. 279 (27): 28603–13. doi:10.1074/jbc.M314031200. PMID 15102830.
- Filosto M, Mancuso M, Tomelleri G, et al. (2004). "Hepato-cerebral syndrome: genetic and pathological studies in an infant with a dGK mutation". Acta Neuropathol. 108 (2): 168–71. doi:10.1007/s00401-004-0872-9. PMID 15150663.
- Batista EL, Warbington M, Badwey JA, Van Dyke TE (2005). "Differentiation of HL-60 cells to granulocytes involves regulation of select diacylglycerol kinases (DGKs)". J. Cell. Biochem. 94 (4): 774–93. doi:10.1002/jcb.20356. PMID 15578578.
- Matsubara T, Shirai Y, Miyasaka K, et al. (2006). "Nuclear transportation of diacylglycerol kinase gamma and its possible function in the nucleus". J. Biol. Chem. 281 (10): 6152–64. doi:10.1074/jbc.M509873200. PMID 16407189.
- Yamaguchi Y, Shirai Y, Matsubara T, et al. (2006). "Phosphorylation and up-regulation of diacylglycerol kinase gamma via its interaction with protein kinase C gamma". J. Biol. Chem. 281 (42): 31627–37. doi:10.1074/jbc.M606992200. PMID 16905533.
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