PLCB1

Phospholipase C, beta 1 (phosphoinositide-specific)

Identifiers

PLCB1 ; EIEE12; PI-PLC; PLC-154; PLC-I; PLC154; PLCB1A; PLCB1B

External IDs

OMIM: 607120 MGI: 97613 HomoloGene: 22876 ChEMBL: 4034 GeneCards: PLCB1 Gene

3.1.4.11

Gene ontology
Molecular function	• phosphatidylinositol phospholipase C activity • signal transducer activity • GTPase activator activity • calcium ion binding • protein binding • calmodulin binding • lamin binding • phosphatidylinositol-4,5-bisphosphate binding • enzyme binding • protein homodimerization activity
Cellular component	• nuclear chromatin • nucleus • cytoplasm • cytosol • nuclear speck • nuclear membrane • myelin sheath • extracellular exosome
Biological process	• G2/M transition of mitotic cell cycle • signal transduction • G-protein coupled acetylcholine receptor signaling pathway • glutamate receptor signaling pathway • synaptic transmission • memory • regulation of G-protein coupled receptor protein signaling pathway • lipid catabolic process • cerebral cortex development • positive regulation of interleukin-12 production • intracellular signal transduction • interleukin-12-mediated signaling pathway • interleukin-15-mediated signaling pathway • positive regulation of embryonic development • positive regulation of GTPase activity • inositol phosphate metabolic process • small molecule metabolic process • fat cell differentiation • positive regulation of myoblast differentiation • negative regulation of transcription, DNA-templated • positive regulation of transcription, DNA-templated • positive regulation of JNK cascade • phosphatidylinositol metabolic process • insulin-like growth factor receptor signaling pathway • positive regulation of developmental growth • activation of meiosis involved in egg activation • interleukin-1-mediated signaling pathway • regulation of fertilization • positive regulation of G1/S transition of mitotic cell cycle • positive regulation of acrosome reaction • negative regulation of monocyte extravasation • positive regulation of CD24 biosynthetic process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 20:
8.11 – 8.97 Mb

Chr 2:
134.79 – 135.48 Mb

PubMed search

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase 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

↑ 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.
↑ 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.
1 2 "Entrez Gene: PLCB1 phospholipase C, beta 1 (phosphoinositide-specific)".
↑ 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.
↑ 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.

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.
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.
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.
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.
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.

Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases

Lipase

Phospholipase
- A1
- A2
- B

3.1.2: Thioesterase

3.1.3: Phosphatase

3.1.4: Phosphodiesterase

3.1.6: Sulfatase

Nuclease (includes
deoxyribonuclease and
ribonuclease)

3.1.11-16: Exonuclease

Exodeoxyribonuclease	RecBCD

Exoribonuclease	Oligonucleotidase

3.1.21-31: Endonuclease

Endodeoxyribonuclease	Deoxyribonuclease I Deoxyribonuclease II Deoxyribonuclease IV Restriction enzyme UvrABC endonuclease

Endoribonuclease	RNase III RNase H 1 2A 2B 2C RNase P RNase A 1 2 3 4/5 RNase T1 RNA-induced silencing complex

either deoxy- or ribo-	Aspergillus nuclease S1 Micrococcal nuclease

Proteins: enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases(list) EC2 Transferases(list) EC3 Hydrolases(list) EC4 Lyases(list) EC5 Isomerases(list) EC6 Ligases(list)

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PLCB1

Function

Interactions

Pathology

References

Further reading