PLCB1

PLCB1
Identifiers
Aliases	PLCB1 , EIEE12, PI-PLC, PLC-154, PLC-I, PLC154, PLCB1A, PLCB1B, PLC-beta-1, phospholipase C beta 1, DEE12
External IDs	OMIM: 607120 MGI: 97613 HomoloGene: 22876 GeneCards: PLCB1
Gene location (Human) Chr. Chromosome 20 (human) [1] Band 20p12.3 Start 8,077,251 bp [1] End 8,968,360 bp [1]
Gene location (Mouse) Chr. Chromosome 2 (mouse) [2] Band 2 F3|2 65.66 cM Start 134,627,987 bp [2] End 135,317,178 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell Brodmann area 23 superior frontal gyrus middle temporal gyrus postcentral gyrus Brodmann area 10 Brodmann area 46 frontal pole entorhinal cortex parotid gland Top expressed in olfactory tubercle subiculum Region I of hippocampus proper globus pallidus facial motor nucleus piriform cortex primary motor cortex anterior horn of spinal cord superior frontal gyrus superior colliculus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding protein homodimerization activity GTPase activator activity signal transducer activity protein binding phosphoric diester hydrolase activity enzyme binding phosphatidylinositol-4,5-bisphosphate binding hydrolase activity lamin binding phosphatidylinositol phospholipase C activity phospholipase C activity calmodulin binding Cellular component cytoplasm cytosol nuclear speck nuclear membrane membrane myelin sheath extracellular exosome nucleus postsynapse glutamatergic synapse GABA-ergic synapse protein-containing complex Biological process G protein-coupled acetylcholine receptor signaling pathway glutamate receptor signaling pathway insulin-like growth factor receptor signaling pathway interleukin-15-mediated signaling pathway intracellular signal transduction positive regulation of developmental growth phosphatidylinositol metabolic process negative regulation of monocyte extravasation positive regulation of interleukin-12 production regulation of G protein-coupled receptor signaling pathway lipid metabolism inositol phosphate metabolic process positive regulation of JNK cascade memory regulation of cell cycle positive regulation of transcription, DNA-templated lipid catabolic process positive regulation of G1/S transition of mitotic cell cycle interleukin-1-mediated signaling pathway positive regulation of acrosome reaction brain development G2/M transition of mitotic cell cycle interleukin-12-mediated signaling pathway positive regulation of myoblast differentiation positive regulation of CD24 production cerebral cortex development activation of meiosis involved in egg activation regulation of fertilization positive regulation of embryonic development negative regulation of transcription, DNA-templated fat cell differentiation signal transduction Wnt signaling pathway, calcium modulating pathway positive regulation of GTPase activity G protein-coupled receptor signaling pathway postsynaptic modulation of chemical synaptic transmission regulation of retrograde trans-synaptic signaling by endocanabinoid inositol trisphosphate biosynthetic process phosphatidylinositol-mediated signaling release of sequestered calcium ion into cytosol Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23236 18795 Ensembl ENSG00000182621 ENSMUSG00000051177 UniProt Q9NQ66 Q9Z1B3 RefSeq (mRNA) NM_015192 NM_182734 NM_001145830 NM_019677 RefSeq (protein) NP_056007 NP_877398 NP_001139302 NP_062651 Location (UCSC) Chr 20: 8.08 – 8.97 Mb Chr 2: 134.63 – 135.32 Mb PubMed search [3] [4]
Wikidata
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1-Phosphatidylinositol-4,5-bisphosphate phospholipase beta-1 is an enzyme that in humans is encoded by the PLCB1 gene. ^{[5] [6] [7]}

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. ^[7]

Interactions

PLCB1 has been shown to interact with TRPM7. ^[8]

Pathology

Homozygous PLCB1 deletion is associated with malignant migrating partial seizures in infancy. ^[9]

References

1. GRCh38: Ensembl release 89: ENSG00000182621 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000051177 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L (Jun 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. doi:10.1016/s1388-1981(00)00012-3. PMID   10760467.
6. Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC (Jan 2001). "Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)". Biochim. Biophys. Acta. 1517 (1): 63–72. doi:10.1016/S0167-4781(00)00260-8. PMID   11118617.
7. "Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific)".
8. Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID   11941371. S2CID   21592843.
9. Poduri A, Chopra SS, Neilan EG, Elhosary PC, Kurian MA, Meyer E, Barry BJ, Khwaja OS, Salih MA, Stödberg T, Scheffer IE, Maher ER, Sahin M, Wu BL, Berry GT, Walsh CA, Picker J, Kothare SV (2012). "Homozygous PLCB1 deletion associated with malignant migrating partial seizures in infancy". Epilepsia. 53 (8): e146–50. doi:10.1111/j.1528-1167.2012.03538.x. PMC   3851296 . PMID   22690784.

Further reading

• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (2002). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi: 10.1093/dnares/9.3.99 . PMID   12168954.
• Martelli AM, Fiume R, Faenza I, Tabellini G, Evangelista C, Bortul R, Follo MY, Falà F, Cocco L (2005). "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, Bavelloni A, Billi AM, Martelli AM, Manzoli L (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, Idziorek T, Autran B, Bismuth G (1990). "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. doi:10.1172/JCI114950. PMC   329852 . PMID   1979339.
• Zauli G, Previati M, Caramelli E, Bassini A, Falcieri E, Gibellini D, Bertolaso L, Bosco D, Robuffo I, Capitani S (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. doi:10.1002/eji.1830250944. PMID   7589147. S2CID   20562627.
• Hwang SC, Park KH, Ha MJ, Noh IS, Park TB, Lee YH (1996). "Distribution of phospholipase C isozymes in normal human lung tissue and their immunohistochemical localization". J. Korean Med. Sci. 11 (4): 305–13. doi:10.3346/jkms.1996.11.4.305. PMC   3054083 . 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. doi: 10.1074/jbc.272.36.22385 . PMID   9278385.
• Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (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. doi: 10.1093/dnares/5.1.31 . PMID   9628581.
• Snow BE, Hall RA, Krumins AM, Brothers GM, Bouchard D, Brothers CA, Chung S, Mangion J, Gilman AG, Lefkowitz RJ, Siderovski DP (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. doi: 10.1074/jbc.273.28.17749 . PMID   9651375.
• Mayne M, Bratanich AC, Chen P, Rana F, Nath A, Power C (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation. 5 (3–4): 184–92. doi:10.1159/000026336. PMID   9730685. S2CID   19529677.
• 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. doi:10.1046/j.1471-4159.1999.0731363.x. PMID   10501179. S2CID   25410140.
• 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. doi: 10.4049/jimmunol.164.12.6538 . PMID   10843712.
• Tang Y, Tang J, Chen Z, Trost C, Flockerzi V, Li M, Ramesh V, Zhu MX (2000). "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.
• Dowal L, Elliott J, Popov S, Wilkie TM, Scarlata S (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. doi:10.1021/bi001923+. 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, Pearson RB, Seok OY, Cocco L, Gilmour RS (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. PMC   86927 . PMID   11287604.
• Vitale M, Matteucci A, Manzoli L, Rodella L, Mariani AR, Zauli G, Falconi M, Billi AM, Martelli AM, Gilmour RS, Cocco L (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. doi: 10.1096/fj.01-0008fje . PMID   11481231. S2CID   13373496.
• 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. S2CID   13301839.