Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Regulation of the phospholipase C-gamma2 pathway in B cells.
Real time fluorescence imaging of PLC gamma translocation and its interaction with the epidermal growth factor receptor.
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Human PLCγ2 constructs redistribute to intracellular vesicles after EGF stimulation in the expression system.
"As shown in Fig. 2, in the absence of EGF, PLCγ1 and PLCγ2 were distributed throughout the cytoplasm and excluded from the nucleus and plasma membrane."
Tyrosine residues in phospholipase Cgamma 2 essential for the enzyme function in B-cell signaling.
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Human PLCγ2 rescues chicken DT40 signaling; purified BTK efficiently phosphorylates PLCγ2 whereas SYK efficiently phosphorylates BLNK.
"Of the two kinases that previously have been proposed to phosphorylate PLCgamma2, Btk, and Syk, purified Btk had much greater ability to phosphorylate recombinant PLCgamma2 in vitro, whereas Syk efficiently phosphorylated adapter protein BLNK."
Activation of phospholipase Cgamma2 by tyrosine phosphorylation.
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Recombinant full-length human PLCγ2 is calcium dependent and activated by tyrosine phosphorylation; platelet activation supports the regulatory sites.
"In vitro phosphorylation experiments with recombinant PLCgamma2 and recombinant Lck, Fyn, and Lyn tyrosine kinases showed that phosphorylation of PLCgamma2 led to activation of the recombinant enzyme."
Glycoproteins VI and Ib-IX-V stimulate tyrosine phosphorylation of tyrosine kinase Syk and phospholipase Cgamma2 at distinct sites.
Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2.
A systematic scan of interactions with tyrosine motifs in the erythropoietin receptor using a mammalian 2-hybrid approach.
A quantitative protein interaction network for the ErbB receptors using protein microarrays.
Molecular profiling of isolated histological components of wilms tumor implicates a common role for the Wnt signaling pathway in kidney and tumor development.
MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis.
Tarp regulates early Chlamydia-induced host cell survival through interactions with the human adaptor protein SHC1.
A hypermorphic missense mutation in PLCG2, encoding phospholipase Cγ2, causes a dominantly inherited autoinflammatory disease with immunodeficiency.
BANK1 and BLK act through phospholipase C gamma 2 in B-cell signaling.
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BANK1–PLCG2 proximity changes its perinuclear distribution after BCR stimulation in human Daudi cells.
"In non-stimulated cells, the few BANK1-PLCG2 interactions are close to the nuclei, they lose the perinuclear localization at one minute of stimulation and at 20 minutes return to a position close to the nuclei."
Fine specificity and molecular competition in SLAM family receptor signalling.
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Recombinant human PLCγ2 SH2 domains bind EAT-2/LAT phosphotyrosine motifs; NK92 experiments separately establish a cytotoxic signaling role.
"Recombinant PLCγ2 SH2 domains also bound immobilized EAT-2 Y127 and LAT Y132 peptides with comparable affinity"
The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells.
Enhanced prediction of Src homology 2 (SH2) domain binding potentials using a fluorescence polarization-derived c-Met, c-Kit, ErbB, and androgen receptor interactome.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
Phospho-tyrosine dependent protein-protein interaction network.
CD21 and FCRL5 form a receptor complex with robust B-cell activating capacity.
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
Alzheimer's-associated PLCγ2 is a signaling node required for both TREM2 function and the inflammatory response in human microglia.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Systematic discovery of mutation-directed neo-protein-protein interactions in cancer.
BLNK (SLP-65) Signalosome hydrolyzes phosphatidyinositol bisphosphate forming diacylglycerol and inositol-1,4,5-trisphosphate
PLC gamma 2-mediated PIP2 hydrolysis
PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by tethered PLC[1] at the plasma membrane
PLC-gamma1 hydrolyses PIP2
Phosphorylation and activation of PLCG
Recruitment of PLCgamma to membrane
Release of PLCG from FCGR
Phosphorylation of SLP-76 by p-SYK
Recruitment of PLC-gamma to SLP-76 and p-5Y-LAT
Activation of RAC1 by VAV2/3
Recruitment of VAV and BTK to p-SLP-76
Phosphorylation of BTK by p-SYK
Phosphorylation and activation of VAV2/VAV3 by SYK
Phosphorylation of PLC-gamma by p-BTK/p-SYK
Fc epsilon receptor (FCERI) signaling
Phosphorylation of TEC kinases by p-SYK
Activation of RAC1 by VAV
Phosphorylation and activation of VAV
Hydrolysis of PIP2 by PLCG
Phosphorylation of SLP-76 by p-SYK
Autophosphorylation of PAK
Autophosphorylation of BTK/ITK
Recruitment of PAK to the membrane by binding active RAC1
Recruitment of VAV to p-SLP-76
SLP-76 stimulates PLC gamma 2
p-Y753,Y759-PLCG2 hydrolyses PIP2
p-Y753,Y759-PLCG2 translocates from cytosol to plasma membrane
PLCG2 translocates from cytosol to plasma membrane
SYK phosphorylates PLCG2 in p-6Y-SYK:p-Y65,Y76-FCER1G:PLCG2
C-type lectin receptors (CLRs)
Platelet activation, signaling and aggregation
Phosphorylated BLNK (SLP65, in Antigen:p-BCR:p-SYK:p-BLNK:CIN85:GRB2:SOS1) binds BTK, PLCG2, VAV1, NCK1
p-DAPP1 (p-BAM32) binds PLCG2
Recruitment of PLCgamma to membrane due to FCGR3A effect
Release of PLCG from FCGR3A
Phosphorylation and activation of PLCG due to FCGR3A effect
Structural insights into formation of an active signaling complex between Rac and phospholipase C gamma 2.
Cold urticaria, immunodeficiency, and autoimmunity related to PLCG2 deletions.
TULA-2 Protein Phosphatase Suppresses Activation of Syk through the GPVI Platelet Receptor for Collagen by Dephosphorylating Tyr(P)346, a Regulatory Site of Syk.
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Platelet pull-down experiments support binding of SYK to PLCγ2 tandem SH2 domains, weaker than binding to PLCγ1.
"Notably, binding of human platelet Syk, but not that of SLP-76, to the SH2(NC) of PLCγ2, the major functional form of PLCγ in platelets ( 43 , 44 ), was much weaker than its binding to the SH2(NC) of PLCγ1 ( Fig. 4 A )."