PLCB1

From Wikipedia, the free encyclopedia

Phospholipase C, beta 1 (phosphoinositide-specific)

Identifiers

PLCB1; PI-PLC; FLJ45792; PLC-154; PLC-I

External IDs

OMIM: 607120 MGI: 97613 HomoloGene: 22876

Gene ontology
Molecular Function:	• phosphoinositide phospholipase C activity • signal transducer activity • calcium ion binding • hydrolase activity
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• regulation of progression through cell cycle • lipid metabolic process • intracellular signaling cascade • lipid catabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_015192 (mRNA)
NP_056007 (protein)

NM_019677 (mRNA)
NP_062651 (protein)

Location

Chr 20: 8.06 - 8.81 Mb

Chr 2: 134.48 - 135.16 Mb

Pubmed search

[1]

[2]

Phospholipase C, beta 1 (phosphoinositide-specific), also known as PLCB1, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific).

[edit] Further reading

Nakajima D, Okazaki N, Yamakawa H, et al. (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones.". DNA Res. 9 (3): 99–106. PMID 12168954.
Martelli AM, Fiume R, Faenza I, et al. (2006). "Nuclear phosphoinositide specific phospholipase C (PI-PLC)-beta 1: a central intermediary in nuclear lipid-dependent signal transduction.". Histol. Histopathol. 20 (4): 1251–60. PMID 16136505.
Cocco L, Follo MY, Faenza I, et al. (2007). "Nuclear inositide signaling: an appraisal of phospholipase C beta 1 behavior in myelodysplastic and leukemia cells.". Adv. Enzyme Regul. 47: 2–9. doi:10.1016/j.advenzreg.2006.12.003. PMID 17335878.
Cefai D, Debre P, Kaczorek M, et al. (1991). "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. PMID 1979339.
Zauli G, Previati M, Caramelli E, et al. (1995). "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. PMID 7589147.
Hwang SC, Park KH, Ha MJ, et al. (1997). "Distribution of phospholipase C isozymes in normal human lung tissue and their immunohistochemical localization.". J. Korean Med. Sci. 11 (4): 305–13. PMID 8878798.
Chen P, Mayne M, Power C, Nath A (1997). "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. PMID 9278385.
Nagase T, Ishikawa K, Miyajima N, et al. (1998). "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. PMID 9628581.
Snow BE, Hall RA, Krumins AM, et al. (1998). "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. PMID 9651375.
Mayne M, Bratanich AC, Chen P, et al. (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease.". Neuroimmunomodulation 5 (3-4): 184–92. PMID 9730685.
Haughey NJ, Holden CP, Nath A, Geiger JD (1999). "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. PMID 10501179.
Peruzzi D, Calabrese G, Faenza I, et al. (2000). "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. PMID 10760467.
Mayne M, Holden CP, Nath A, Geiger JD (2000). "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. PMID 10843712.
Tang Y, Tang J, Chen Z, et al. (2001). "Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF.". J. Biol. Chem. 275 (48): 37559–64. doi:10.1074/jbc.M006635200. PMID 10980202.
Caricasole A, Sala C, Roncarati R, et al. (2001). "Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1).". Biochim. Biophys. Acta 1517 (1): 63–72. PMID 11118617.
Dowal L, Elliott J, Popov S, et al. (2001). "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. PMID 11148035.
Xu A, Wang Y, Xu LY, Gilmour RS (2001). "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. doi:10.1074/jbc.M009144200. PMID 11278470.
Xu A, Suh PG, Marmy-Conus N, et al. (2001). "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. doi:10.1128/MCB.21.9.2981-2990.2001. PMID 11287604.
Vitale M, Matteucci A, Manzoli L, et al. (2001). "Interleukin 2 activates nuclear phospholipase Cbeta by mitogen-activated protein kinase-dependent phosphorylation in human natural killer cells.". FASEB J. 15 (10): 1789–91. PMID 11481231.
Singer AU, Waldo GL, Harden TK, Sondek J (2002). "A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q.". Nat. Struct. Biol. 9 (1): 32–6. doi:10.1038/nsb731. PMID 11753430.