[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/plcb2-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/plcb2-wikipedia\/","headline":"PLCB2 &#8211; Wikipedia","name":"PLCB2 &#8211; Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens 1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 is an enzyme","datePublished":"2016-02-25","dateModified":"2016-02-25","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/f\/fc\/PDB_2fju_EBI.jpg\/180px-PDB_2fju_EBI.jpg","url":"https:\/\/upload.wikimedia.org\/wikipedia\/commons\/thumb\/f\/fc\/PDB_2fju_EBI.jpg\/180px-PDB_2fju_EBI.jpg","height":"135","width":"180"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/plcb2-wikipedia\/","about":["Wiki"],"wordCount":5479,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiens1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 is an enzyme that in humans is encoded by the PLCB2 gene.[5][6][7]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsFunction[edit]Interactions[edit]References[edit]Further reading[edit]Function[edit]The gene codes for the enzyme phospholipase C \u03b22. 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[edit]PLCB2 has been shown to interact with MAP2K3[8] and TRPM7.[9]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000137841 &#8211; Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040061 &#8211; Ensembl, May 2017^ &#8220;Human PubMed Reference:&#8221;. National Center for Biotechnology Information, U.S. National Library of Medicine.^ &#8220;Mouse PubMed Reference:&#8221;. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Park D, Jhon DY, Kriz R, Knopf J, Rhee SG (Sep 1992). &#8220;Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2&#8221;. J. Biol. Chem. 267 (23): 16048\u201355. doi:10.1016\/S0021-9258(18)41963-1. PMID\u00a01644792.^ Park SH, Ryu SH, Suh PG, Kim H (Mar 1999). &#8220;Assignment1 of human PLCB2 encoding PLC beta2 to human chromosome 15q15 by fluorescence in situ hybridization&#8221;. Cytogenet. Cell Genet. 83 (1\u20132): 48\u20139. doi:10.1159\/000015166. PMID\u00a09925923. S2CID\u00a045169136.^ &#8220;Entrez Gene: PLCB2 phospholipase C, beta 2&#8221;.^ Barr AJ, Marjoram R, Xu J, Snyderman R (Apr 2002). &#8220;Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3&#8221;. Biochem. Biophys. Res. Commun. 293 (1): 647\u201352. doi:10.1016\/S0006-291X(02)00259-0. PMID\u00a012054652.^ Runnels LW, Yue L, Clapham DE (May 2002). &#8220;The TRPM7 channel is inactivated by PIP(2) hydrolysis&#8221;. Nat. Cell Biol. 4 (5): 329\u201336. doi:10.1038\/ncb781. PMID\u00a011941371. S2CID\u00a021592843.Further reading[edit]Cefai D, Debre P, Kaczorek M, Idziorek T, Autran B, Bismuth G (1990). &#8220;Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3\/T cell-antigen receptor phosphoinositide transduction pathway&#8221;. J. Clin. Invest. 86 (6): 2117\u201324. doi:10.1172\/JCI114950. PMC\u00a0329852. PMID\u00a01979339.Zauli G, Previati M, Caramelli E, Bassini A, Falcieri E, Gibellini D, Bertolaso L, Bosco D, Robuffo I, Capitani S (1995). &#8220;Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line&#8221;. Eur. J. Immunol. 25 (9): 2695\u2013700. doi:10.1002\/eji.1830250944. PMID\u00a07589147. S2CID\u00a020562627.Buhl AM, Osawa S, Johnson GL (1995). &#8220;Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor&#8221;. J. Biol. Chem. 270 (34): 19828\u201332. doi:10.1074\/jbc.270.34.19828. PMID\u00a07649993.Chen P, Mayne M, Power C, Nath A (1997). &#8220;The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases&#8221;. J. Biol. Chem. 272 (36): 22385\u20138. doi:10.1074\/jbc.272.36.22385. PMID\u00a09278385.Dar\u00e8 E, Kifor O, Brown EM, Weber G (1998). &#8220;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&#8221;. J. Mol. Endocrinol. 21 (1): 7\u201317. doi:10.1677\/jme.0.0210007. PMID\u00a09723859.Mayne M, Bratanich AC, Chen P, Rana F, Nath A, Power C (1998). &#8220;HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease&#8221;. Neuroimmunomodulation. 5 (3\u20134): 184\u201392. doi:10.1159\/000026336. PMID\u00a09730685. S2CID\u00a019529677.Haughey NJ, Holden CP, Nath A, Geiger JD (1999). &#8220;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&#8221;. J. Neurochem. 73 (4): 1363\u201374. doi:10.1046\/j.1471-4159.1999.0731363.x. PMID\u00a010501179.Mayne M, Holden CP, Nath A, Geiger JD (2000). &#8220;Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages&#8221;. J. Immunol. 164 (12): 6538\u201342. doi:10.4049\/jimmunol.164.12.6538. PMID\u00a010843712.Tang Y, Tang J, Chen Z, Trost C, Flockerzi V, Li M, Ramesh V, Zhu MX (2000). &#8220;Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF&#8221;. J. Biol. Chem. 275 (48): 37559\u201364. doi:10.1074\/jbc.M006635200. PMID\u00a010980202.Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC (2000). &#8220;Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)&#8221;. Biochim. Biophys. Acta. 1517 (1): 63\u201372. doi:10.1016\/S0167-4781(00)00260-8. PMID\u00a011118617.Singer AU, Waldo GL, Harden TK, Sondek J (2002). &#8220;A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q&#8221;. Nat. Struct. Biol. 9 (1): 32\u20136. doi:10.1038\/nsb731. PMID\u00a011753430. S2CID\u00a013301839.Runnels LW, Yue L, Clapham DE (2002). &#8220;The TRPM7 channel is inactivated by PIP(2) hydrolysis&#8221;. Nat. Cell Biol. 4 (5): 329\u201336. doi:10.1038\/ncb781. PMID\u00a011941371. S2CID\u00a021592843.Scarlata S (2002). &#8220;Regulation of the lateral association of phospholipase Cbeta2 and G protein subunits by lipid rafts&#8221;. Biochemistry. 41 (22): 7092\u20139. doi:10.1021\/bi025625j. PMID\u00a012033943.Bertagnolo V, Marchisio M, Pierpaoli S, Colamussi ML, Brugnoli F, Visani G, Zauli G, Capitani S (2002). &#8220;Selective up-regulation of phospholipase C-beta2 during granulocytic differentiation of normal and leukemic hematopoietic progenitors&#8221;. J. Leukoc. Biol. 71 (6): 957\u201365. doi:10.1189\/jlb.71.6.957. PMID\u00a012050180. S2CID\u00a037477730.Barr AJ, Marjoram R, Xu J, Snyderman R (2002). &#8220;Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3&#8221;. Biochem. Biophys. Res. Commun. 293 (1): 647\u201352. doi:10.1016\/S0006-291X(02)00259-0. PMID\u00a012054652.Buck E, Schatz P, Scarlata S, Iyengar R (2002). &#8220;Role of dynamic interactions in effective signal transfer for Gbeta stimulation of phospholipase C-beta 2&#8221;. J. Biol. Chem. 277 (51): 49707\u201315. doi:10.1074\/jbc.M205553200. PMID\u00a012388553.Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2002). &#8220;Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha&#8221;. Virology. 303 (1): 174\u201380. doi:10.1006\/viro.2002.1676. PMID\u00a012482669.PDB gallery2fju: Activated Rac1 bound to its effector phospholipase C beta 2       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/plcb2-wikipedia\/#breadcrumbitem","name":"PLCB2 &#8211; Wikipedia"}}]}]