PLCG2

Phospholipase C, gamma 2 (phosphatidylinositol-specific)

Rendering based on PDB 2K2J.
Identifiers
Symbols PLCG2;
External IDs OMIM: 600220 MGI: 97616 HomoloGene: 55671 GeneCards: PLCG2 Gene
EC number 3.1.4.11
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 5336 234779
Ensembl ENSG00000197943 ENSMUSG00000034330
UniProt P16885 Q8CIH5
RefSeq (mRNA) NM_002661 NM_172285.1
RefSeq (protein) NP_002652 NP_758489.1
Location (UCSC) Chr 16:
81.81 – 81.99 Mb		 Chr 8:
120.02 – 120.16 Mb
PubMed search [1] [2]

1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 is an enzyme that in humans is encoded by the PLCG2 gene.[1][2]

Contents

Function

Enzymes of the phospholipase C family catalyze the hydrolysis of phospholipids to yield diacylglycerols and water-soluble phosphorylated derivatives of the lipid head groups. A number of these enzymes have specificity for phosphoinositides. Of the phosphoinositide-specific phospholipase C enzymes, C-beta is regulated by heterotrimeric G protein-coupled receptors, while the closely related C-gamma-1 (PLCG1; MIM 172420) and C-gamma-2 enzymes are controlled by receptor tyrosine kinases. The C-gamma-1 and C-gamma-2 enzymes are composed of phospholipase domains that flank regions of homology to noncatalytic domains of the SRC oncogene product, SH2 and SH3.[supplied by OMIM][2]

Interactions

PLCG2 has been shown to interact with PTPN11,[3] LYN,[4][5] Bruton's tyrosine kinase,[6][5] SHC1[7][3] and GAB2.[3]

References

  1. ^ Hernandez D, Egan SE, Yulug IG, Fisher EM (Feb 1995). "Mapping the gene that encodes phosphatidylinositol-specific phospholipase C-gamma 2 in the human and the mouse". Genomics 23 (2): 504–7. doi:10.1006/geno.1994.1533. PMID 7835906. 
  2. ^ a b "Entrez Gene: PLCG2 phospholipase C, gamma 2 (phosphatidylinositol-specific)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5336. 
  3. ^ a b c Boudot, Cédric; Kadri Zahra, Petitfrère Emmanuelle, Lambert Elise, Chrétien Stany, Mayeux Patrick, Haye Bernard, Billat Claudine (Oct. 2002). "Phosphatidylinositol 3-kinase regulates glycosylphosphatidylinositol hydrolysis through PLC-gamma(2) activation in erythropoietin-stimulated cells". Cell. Signal. (England) 14 (10): 869–78. doi:10.1016/S0898-6568(02)00036-0. ISSN 0898-6568. PMID 12135708. 
  4. ^ Pleiman, C M; Clark M R, Gauen L K, Winitz S, Coggeshall K M, Johnson G L, Shaw A S, Cambier J C (Sep. 1993). "Mapping of sites on the Src family protein tyrosine kinases p55blk, p59fyn, and p56lyn which interact with the effector molecules phospholipase C-gamma 2, microtubule-associated protein kinase, GTPase-activating protein, and phosphatidylinositol 3-kinase". Mol. Cell. Biol. (UNITED STATES) 13 (9): 5877–87. ISSN 0270-7306. PMC 360336. PMID 8395016. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=360336. 
  5. ^ a b Guo, B; Kato R M, Garcia-Lloret M, Wahl M I, Rawlings D J (Aug. 2000). "Engagement of the human pre-B cell receptor generates a lipid raft-dependent calcium signaling complex". Immunity (UNITED STATES) 13 (2): 243–53. doi:10.1016/S1074-7613(00)00024-8. ISSN 1074-7613. PMID 10981967. 
  6. ^ Yasuda, Tomoharu; Tezuka Tohru, Maeda Akito, Inazu Tetsuya, Yamanashi Yuji, Gu Hua, Kurosaki Tomohiro, Yamamoto Tadashi (Jul. 2002). "Cbl-b positively regulates Btk-mediated activation of phospholipase C-gamma2 in B cells". J. Exp. Med. (United States) 196 (1): 51–63. doi:10.1084/jem.20020068. ISSN 0022-1007. PMC 2194016. PMID 12093870. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2194016. 
  7. ^ Perskvist, N; Zheng L, Stendahl O (Jan. 2000). "Activation of human neutrophils by Mycobacterium tuberculosis H37Ra involves phospholipase C gamma 2, Shc adapter protein, and p38 mitogen-activated protein kinase". J. Immunol. (UNITED STATES) 164 (2): 959–65. ISSN 0022-1767. PMID 10623845. 


Further reading