Biology:PLCG2
Generic protein structure example |
1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 is an enzyme that in humans is encoded by the PLCG2 gene.[1][2]
Function
From OMIM as of March 24, 2020:[3]
Enzymes of the phospholipase C family catalyze the hydrolysis of phospholipids to yield diacylglycerols and water-soluble phosphorylated derivatives of the lipid head groups. A number of these enzymes have specificity for phosphoinositides. Of the phosphoinositide-specific phospholipase C enzymes, C-beta is regulated by heterotrimeric G protein-coupled receptors, while the closely related C-gamma-1 (PLCG1; MIM 172420) and C-gamma-2 enzymes are controlled by receptor tyrosine kinases. The C-gamma-1 and C-gamma-2 enzymes are composed of phospholipase domains that flank regions of homology to noncatalytic domains of the SRC oncogene product, SH2 and SH3.
Interactions
PLCG2 has been shown to interact with:
References
- ↑ "Mapping the gene that encodes phosphatidylinositol-specific phospholipase C-gamma 2 in the human and the mouse". Genomics 23 (2): 504–7. February 1995. doi:10.1006/geno.1994.1533. PMID 7835906.
- ↑ "Entrez Gene: PLCG2 phospholipase C, gamma 2 (phosphatidylinositol-specific)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5336.
- ↑ Bocchini, Carol A. (2020-03-24). "600220: PHOSPHOLIPASE C, GAMMA-2; PLCG2" (in en). Johns Hopkins University. https://www.omim.org/entry/600220.
- ↑ 4.0 4.1 "Engagement of the human pre-B cell receptor generates a lipid raft-dependent calcium signaling complex". Immunity 13 (2): 243–53. August 2000. doi:10.1016/s1074-7613(00)00024-8. PMID 10981967.
- ↑ "Cbl-b positively regulates Btk-mediated activation of phospholipase C-gamma2 in B cells". J. Exp. Med. 196 (1): 51–63. July 2002. doi:10.1084/jem.20020068. PMID 12093870.
- ↑ 6.0 6.1 6.2 "Phosphatidylinositol 3-kinase regulates glycosylphosphatidylinositol hydrolysis through PLC-gamma(2) activation in erythropoietin-stimulated cells". Cell. Signal. 14 (10): 869–78. October 2002. doi:10.1016/s0898-6568(02)00036-0. PMID 12135708.
- ↑ "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase". Mol. Cell. Biol. 13 (9): 5877–87. September 1993. doi:10.1128/MCB.13.9.5877. PMID 8395016.
- ↑ "Activation of human neutrophils by Mycobacterium tuberculosis H37Ra involves phospholipase C gamma 2, Shc adapter protein, and p38 mitogen-activated protein kinase". J. Immunol. 164 (2): 959–65. January 2000. doi:10.4049/jimmunol.164.2.959. PMID 10623845.
Further reading
- "Xid-like phenotypes: a B cell signalosome takes shape". Immunity 13 (1): 1–3. 2000. doi:10.1016/S1074-7613(00)00002-9. PMID 10933389.
- "Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway". J. Clin. Invest. 86 (6): 2117–24. 1990. doi:10.1172/JCI114950. PMID 1979339.
- "Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes". FEBS Lett. 242 (1): 31–5. 1988. doi:10.1016/0014-5793(88)80979-7. PMID 2849563.
- "Preferred sites of glycosylphosphatidylinositol modification in folate receptors and constraints in the primary structure of the hydrophobic portion of the signal". Biochemistry 34 (44): 14594–600. 1995. doi:10.1021/bi00044a039. PMID 7578066.
- "Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line". Eur. J. Immunol. 25 (9): 2695–700. 1995. doi:10.1002/eji.1830250944. PMID 7589147.
- "In vitro tyrosine phosphorylation of PLC-gamma 1 & PLC-gamma 2 by src-family protein tyrosine kinases". Biochem. Biophys. Res. Commun. 191 (3): 1028–1033. 1993. doi:10.1006/bbrc.1993.1320. PMID 7682059.
- "Evidence for a role for tyrosine phosphorylation of phospholipase C gamma 2 in collagen-induced platelet cytosolic calcium mobilization". Biochem. J. 302 (2): 617–22. 1994. doi:10.1042/bj3020617. PMID 8093016.
- "Identification of Trk binding sites for SHC and phosphatidylinositol 3'-kinase and formation of a multimeric signaling complex". J. Biol. Chem. 268 (31): 22963–6. 1993. doi:10.1016/S0021-9258(19)49410-6. PMID 8226808.
- "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase". Mol. Cell. Biol. 13 (9): 5877–87. 1993. doi:10.1128/MCB.13.9.5877. PMID 8395016.
- "Protein kinase C mu (PKC mu) associates with the B cell antigen receptor complex and regulates lymphocyte signaling". Immunity 5 (4): 353–63. 1996. doi:10.1016/S1074-7613(00)80261-7. PMID 8885868.
- "Cloning and functional analysis of the hematopoietic cell-specific phospholipase C(gamma)2 promoter". FEBS Lett. 399 (1–2): 14–20. 1996. doi:10.1016/S0014-5793(96)01276-8. PMID 8980110.
- "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". J. Biol. Chem. 272 (36): 22385–8. 1997. doi:10.1074/jbc.272.36.22385. PMID 9278385.
- "Interactions of FLT-1 and KDR with phospholipase C gamma: identification of the phosphotyrosine binding sites". Biochem. Biophys. Res. Commun. 240 (3): 635–9. 1997. doi:10.1006/bbrc.1997.7719. PMID 9398617.
- "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation 5 (3–4): 184–92. 1998. doi:10.1159/000026336. PMID 9730685.
- "Nucleophosmin-anaplastic lymphoma kinase of large-cell anaplastic lymphoma is a constitutively active tyrosine kinase that utilizes phospholipase C-gamma to mediate its mitogenicity". Mol. Cell. Biol. 18 (12): 6951–61. 1998. doi:10.1128/mcb.18.12.6951. PMID 9819383.
- "Molecular requirements for attachment of the glycosylphosphatidylinositol anchor to the human alpha folate receptor". J. Cell. Biochem. 72 (1): 111–8. 1999. doi:10.1002/(SICI)1097-4644(19990101)72:1<111::AID-JCB12>3.0.CO;2-1. PMID 10025672.
- "Evidence for SH3 domain directed binding and phosphorylation of Sam68 by Src". Oncogene 18 (33): 4647–53. 1999. doi:10.1038/sj.onc.1203079. PMID 10467411.
- "Evidence that phospholipase C-gamma2 interacts with SLP-76, Syk, Lyn, LAT and the Fc receptor gamma-chain after stimulation of the collagen receptor glycoprotein VI in human platelets". Eur. J. Biochem. 263 (3): 612–23. 1999. doi:10.1046/j.1432-1327.1999.00560.x. PMID 10469124.
- "Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat". J. Neurochem. 73 (4): 1363–74. 1999. doi:10.1046/j.1471-4159.1999.0731363.x. PMID 10501179.
Original source: https://en.wikipedia.org/wiki/PLCG2.
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