PLCB2

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 is an enzyme that in humans is encoded by the PLCB2 gene.[5][6][7]

PLCB2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2FJU, 2ZKM
Identifiers
Aliases	PLCB2, PLC-beta-2, phospholipase C beta 2
External IDs	OMIM: 604114 MGI: 107465 HomoloGene: 20957 GeneCards: PLCB2
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q15.1 Start 40,278,176 bp[1] End 40,307,935 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2 E5|2 59.43 cM Start 118,707,517 bp[2] End 118,728,438 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • phosphoric diester hydrolase activity • phospholipase C activity • calcium ion binding • hydrolase activity • signal transducer activity • metal ion binding • phosphatidylinositol phospholipase C activity Cellular component • cytoplasm • cytosol Biological process • lipid catabolic process • sensory perception of bitter taste • phospholipid metabolic process • GO:0007243 intracellular signal transduction • inositol phosphate metabolic process • activation of phospholipase C activity • signal transduction • lipid metabolism • Wnt signaling pathway, calcium modulating pathway • G-protein coupled receptor signaling pathway • inositol trisphosphate biosynthetic process • phosphatidylinositol-mediated signaling • release of sequestered calcium ion into cytosol Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5330	18796
Ensembl	ENSG00000137841	ENSMUSG00000040061
UniProt	Q00722	A3KGF7
RefSeq (mRNA)	NM_001284297 NM_001284298 NM_001284299 NM_004573	NM_001290790 NM_177568
RefSeq (protein)	NP_001271226 NP_001271227 NP_001271228 NP_004564	NP_001277719 NP_808236
Location (UCSC)	Chr 15: 40.28 – 40.31 Mb	Chr 2: 118.71 – 118.73 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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[8] and TRPM7.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000137841 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040061 - 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. Park D, Jhon DY, Kriz R, Knopf J, Rhee SG (Sep 1992). "Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2". J. Biol. Chem. 267 (23): 16048–55. PMID 1644792.
6. Park SH, Ryu SH, Suh PG, Kim H (Mar 1999). "Assignment1 of human PLCB2 encoding PLC beta2 to human chromosome 15q15 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 83 (1–2): 48–9. doi:10.1159/000015166. PMID 9925923.
7. "Entrez Gene: PLCB2 phospholipase C, beta 2".
8. Barr AJ, Marjoram R, Xu J, Snyderman R (Apr 2002). "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. 293 (1): 647–52. doi:10.1016/S0006-291X(02)00259-0. PMID 12054652.
9. 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.

Further reading

• 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.
• Buhl AM, Osawa S, Johnson GL (1995). "Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor". J. Biol. Chem. 270 (34): 19828–32. doi:10.1074/jbc.270.34.19828. PMID 7649993.
• 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.
• Darè E, Kifor O, Brown EM, Weber G (1998). "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. doi:10.1677/jme.0.0210007. PMID 9723859.
• 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.
• Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC (2000). "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.
• 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.
• Runnels LW, Yue L, Clapham DE (2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371.
• Scarlata S (2002). "Regulation of the lateral association of phospholipase Cbeta2 and G protein subunits by lipid rafts". Biochemistry. 41 (22): 7092–9. doi:10.1021/bi025625j. PMID 12033943.
• Bertagnolo V, Marchisio M, Pierpaoli S, Colamussi ML, Brugnoli F, Visani G, Zauli G, Capitani S (2002). "Selective up-regulation of phospholipase C-beta2 during granulocytic differentiation of normal and leukemic hematopoietic progenitors". J. Leukoc. Biol. 71 (6): 957–65. PMID 12050180.
• Barr AJ, Marjoram R, Xu J, Snyderman R (2002). "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. 293 (1): 647–52. doi:10.1016/S0006-291X(02)00259-0. PMID 12054652.
• Buck E, Schatz P, Scarlata S, Iyengar R (2002). "Role of dynamic interactions in effective signal transfer for Gbeta stimulation of phospholipase C-beta 2". J. Biol. Chem. 277 (51): 49707–15. doi:10.1074/jbc.M205553200. PMID 12388553.
• Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2002). "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha". Virology. 303 (1): 174–80. doi:10.1006/viro.2002.1676. PMID 12482669.