Biology:PLCB1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
1-Phosphatidylinositol-4,5-bisphosphate phospholipase beta-1 is an enzyme that in humans is encoded by the PLCB1 gene.[1][2][3]
Function
The protein encoded by this gene 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. Two transcript variants encoding different isoforms have been found for this gene.[3]
Interactions
PLCB1 has been shown to interact with TRPM7.[4]
Pathology
Homozygous PLCB1 deletion is associated with malignant migrating partial seizures in infancy.[5]
References
- ↑ "Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1)". Biochim. Biophys. Acta 1484 (2–3): 175–82. Jun 2000. doi:10.1016/s1388-1981(00)00012-3. PMID 10760467.
- ↑ "Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)". Biochim. Biophys. Acta 1517 (1): 63–72. Jan 2001. doi:10.1016/S0167-4781(00)00260-8. PMID 11118617.
- ↑ 3.0 3.1 "Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23236.
- ↑ "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. May 2002. doi:10.1038/ncb781. PMID 11941371.
- ↑ "Homozygous PLCB1 deletion associated with malignant migrating partial seizures in infancy". Epilepsia 53 (8): e146–50. 2012. doi:10.1111/j.1528-1167.2012.03538.x. PMID 22690784.
Further reading
- "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. 2002. doi:10.1093/dnares/9.3.99. PMID 12168954.
- "Nuclear phosphoinositide specific phospholipase C (PI-PLC)-beta 1: a central intermediary in nuclear lipid-dependent signal transduction". Histol. Histopathol. 20 (4): 1251–60. 2005. PMID 16136505.
- "Nuclear inositide signaling: an appraisal of phospholipase C beta 1 behavior in myelodysplastic and leukemia cells". Adv. Enzyme Regul. 47: 2–9. 2007. doi:10.1016/j.advenzreg.2006.12.003. PMID 17335878.
- "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.
- "Distribution of phospholipase C isozymes in normal human lung tissue and their immunohistochemical localization". J. Korean Med. Sci. 11 (4): 305–13. 1996. doi:10.3346/jkms.1996.11.4.305. PMID 8878798.
- "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.
- "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 5 (1): 31–9. 1998. doi:10.1093/dnares/5.1.31. PMID 9628581.
- "GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain". J. Biol. Chem. 273 (28): 17749–55. 1998. doi:10.1074/jbc.273.28.17749. PMID 9651375.
- "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.
- "Determination of the contact energies between a regulator of G protein signaling and G protein subunits and phospholipase C beta 1". Biochemistry 40 (2): 414–21. 2001. doi:10.1021/bi001923+. PMID 11148035.
- "Protein kinase C alpha -mediated negative feedback regulation is responsible for the termination of insulin-like growth factor I-induced activation of nuclear phospholipase C beta1 in Swiss 3T3 cells". J. Biol. Chem. 276 (18): 14980–6. 2001. doi:10.1074/jbc.M009144200. PMID 11278470.
- "Phosphorylation of nuclear phospholipase C beta1 by extracellular signal-regulated kinase mediates the mitogenic action of insulin-like growth factor I". Mol. Cell. Biol. 21 (9): 2981–90. 2001. doi:10.1128/MCB.21.9.2981-2990.2001. PMID 11287604.
- "Interleukin 2 activates nuclear phospholipase Cbeta by mitogen-activated protein kinase-dependent phosphorylation in human natural killer cells". FASEB J. 15 (10): 1789–91. 2001. doi:10.1096/fj.01-0008fje. PMID 11481231.
- "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.
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