Biology:PLCB2
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 is an enzyme that in humans is encoded by the PLCB2 gene.[1][2][3]
Function
The gene codes for the enzyme phospholipase C β2. The enzyme catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11, as well as G-beta gamma subunits.
Interactions
PLCB2 has been shown to interact with MAP2K3[4] and TRPM7.[5]
References
- ↑ "Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2". J. Biol. Chem. 267 (23): 16048–55. Sep 1992. doi:10.1016/S0021-9258(18)41963-1. PMID 1644792.
- ↑ "Assignment1 of human PLCB2 encoding PLC beta2 to human chromosome 15q15 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 83 (1–2): 48–9. Mar 1999. doi:10.1159/000015166. PMID 9925923.
- ↑ "Entrez Gene: PLCB2 phospholipase C, beta 2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5330.
- ↑ "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. 293 (1): 647–52. Apr 2002. doi:10.1016/S0006-291X(02)00259-0. PMID 12054652.
- ↑ "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. May 2002. doi:10.1038/ncb781. PMID 11941371.
Further reading
- "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.
- "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.
- "Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor". J. Biol. Chem. 270 (34): 19828–32. 1995. doi:10.1074/jbc.270.34.19828. PMID 7649993.
- "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.
- "Characterization of the phosphatidylinositol-specific phospholipase C isozymes present in the bovine parathyroid and in human kidney HEK293 cells stably transfected with the human parathyroid Ca2+-sensing receptor". J. Mol. Endocrinol. 21 (1): 7–17. 1998. doi:10.1677/jme.0.0210007. PMID 9723859.
- "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.
- "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.
- "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". J. Immunol. 164 (12): 6538–42. 2000. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
- "Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF". J. Biol. Chem. 275 (48): 37559–64. 2000. doi:10.1074/jbc.M006635200. PMID 10980202.
- "Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)". Biochim. Biophys. Acta 1517 (1): 63–72. 2000. doi:10.1016/S0167-4781(00)00260-8. PMID 11118617.
- "A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q". Nat. Struct. Biol. 9 (1): 32–6. 2002. doi:10.1038/nsb731. PMID 11753430.
- "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. 2002. doi:10.1038/ncb781. PMID 11941371.
- "Regulation of the lateral association of phospholipase Cbeta2 and G protein subunits by lipid rafts". Biochemistry 41 (22): 7092–9. 2002. doi:10.1021/bi025625j. PMID 12033943.
- "Selective up-regulation of phospholipase C-beta2 during granulocytic differentiation of normal and leukemic hematopoietic progenitors". J. Leukoc. Biol. 71 (6): 957–65. 2002. doi:10.1189/jlb.71.6.957. PMID 12050180.
- "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. 293 (1): 647–52. 2002. doi:10.1016/S0006-291X(02)00259-0. PMID 12054652.
- "Role of dynamic interactions in effective signal transfer for Gbeta stimulation of phospholipase C-beta 2". J. Biol. Chem. 277 (51): 49707–15. 2002. doi:10.1074/jbc.M205553200. PMID 12388553.
- "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha". Virology 303 (1): 174–80. 2002. doi:10.1006/viro.2002.1676. PMID 12482669.
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