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Protein PLCG2 PDB 2K2J.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases PLCG2, APLAID, FCAS3, PLC-IV, PLC-gamma-2, phospholipase C gamma 2
External IDs MGI: 97616 HomoloGene: 55671 GeneCards: 5336
Genetically Related Diseases
breast cancer[1]
RNA expression pattern
PBB GE PLCG2 204613 at tn.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 16: 81.74 – 81.96 Mb Chr 8: 117.5 – 117.64 Mb
PubMed search [2] [3]
View/Edit Human View/Edit Mouse

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


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][5]


PLCG2 has been shown to interact with:


  1. ^ "Diseases that are genetically associated with PLCG2 view/edit references on wikidata". 
  2. ^ "Human PubMed Reference:". 
  3. ^ "Mouse PubMed Reference:". 
  4. ^ Hernandez D, Egan SE, Yulug IG, Fisher EM (February 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. 
  5. ^ a b "Entrez Gene: PLCG2 phospholipase C, gamma 2 (phosphatidylinositol-specific)". 
  6. ^ a b Guo B, Kato RM, Garcia-Lloret M, Wahl MI, Rawlings DJ (August 2000). "Engagement of the human pre-B cell receptor generates a lipid raft-dependent calcium signaling complex". Immunity. 13 (2): 243–53. doi:10.1016/s1074-7613(00)00024-8. PMID 10981967. 
  7. ^ Yasuda T, Tezuka T, Maeda A, Inazu T, Yamanashi Y, Gu H, Kurosaki T, Yamamoto T (July 2002). "Cbl-b positively regulates Btk-mediated activation of phospholipase C-gamma2 in B cells". J. Exp. Med. 196 (1): 51–63. doi:10.1084/jem.20020068. PMC 2194016free to read. PMID 12093870. 
  8. ^ a b c Boudot C, Kadri Z, Petitfrère E, Lambert E, Chrétien S, Mayeux P, Haye B, Billat C (October 2002). "Phosphatidylinositol 3-kinase regulates glycosylphosphatidylinositol hydrolysis through PLC-gamma(2) activation in erythropoietin-stimulated cells". Cell. Signal. 14 (10): 869–78. doi:10.1016/s0898-6568(02)00036-0. PMID 12135708. 
  9. ^ Pleiman CM, Clark MR, Gauen LK, Winitz S, Coggeshall KM, Johnson GL, Shaw AS, Cambier JC (September 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. 13 (9): 5877–87. PMC 360336free to read. PMID 8395016. 
  10. ^ Perskvist N, Zheng L, Stendahl O (January 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. 164 (2): 959–65. doi:10.4049/jimmunol.164.2.959. PMID 10623845. 

Further reading[edit]