Search results for PLCG2

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Reaction (16 results from a total of 16)

Identifier: R-HSA-9606894
Species: Homo sapiens
Compartment: plasma membrane
Phosphorylated DAPP1 (BAM32) bound to phosphoinositol 3,4,5-trisphosphate (PIP3) at the plasma membrane binds phospholipase gamma-2 (PLCG2) (Marshall et al. 2000).
Identifier: R-HSA-9606162
Species: Homo sapiens
Compartment: plasma membrane
Activated BTK (BTK phosphorylated on tyrosine-551 and tyrosine-223) bound to phosphorylated BLNK phosphorylates phospholipase gamma-2 (PKCG2) on tyrosines 753, 759, and 1217 (Rodriguez et al. 2001 and inferred from the rat homolog) thereby activating PLCG2 to hydrolyze phosphatidylinositol 4,5-bisphosphate, yielding the second messengers diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) (Carter et al. 1991, Roifman and Wang 1992, Kim et al. 2004, Sekiya et al. 2004). PLCG2 also binds phosphoinositol 3,4,5-trisphosphate (PIP3) produced by PI3K at the plasma membrane.
Identifier: R-HSA-5621363
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Activation of SYK triggers multiple cascades, which induces NF-kB activation through a CARD9-dependent pathway. Phospholipase C-gamma 2 (PLCG2) is one of the key signaling components of the CLEC4E (Mincle)/CLEC6A (Dectin-2) pathway that connects SYK activation to CARD9 recruitment. PLCG2 is activated upon CLEC4E (Mincle)/CLEC6A (Dectin-2) engagement and triggers an intracellular Ca2+ flux. SYK and Src family kinases are upstream of PLCG2. SYK phosphorylates PLCG2 on Y753 and Y759, enhancing the activity of PLCG2 (Gorjestani et al. 2011, Suzuki-Inoue et al. 2004).
Identifier: R-HSA-5621347
Species: Homo sapiens
Compartment: plasma membrane
Tyrosine-phosphorylated Phospholipase C-gamma 2 (PLCG2) translocates from the cytosol to the plasma membrane. At the membrane PLCG2 is in close proximity to phosphatidylinositol 4,5-bisphosphate (PIP2) and its other substrates generating the second messengers IP3 and DAG (Rhee 2001). This leads to the activation of CARD9-BCL10-MALT1/NF-kB signaling.
Identifier: R-HSA-5607735
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Following tyrosine phosphorylation, phospholipase C-gamma 2 (PLCG2) catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2 or PIP2] to inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG).
Identifier: R-HSA-5607755
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Tyrosine-phosphorylated Phospholipase C-gamma 2 (PLCG2) translocates from the cytosol to the plasma membrane. At the membrane PLCG2 is in close proximity to phosphatidylinositol 4,5-bisphosphate (PIP2) and its other substrates generating the second messengers IP3 and DAG (Rhee 2001). This leads to the activation of CARD9-BCL10-MALT1/NF-kB signaling and stimulates calcineurin/NFAT signaling.
Identifier: R-HSA-9606151
Species: Homo sapiens
Compartment: plasma membrane
Phosphorylated BLNK (also called BASH or SLP-65) at the plasma membrane recruits BTK, PLC gamma, VAV, GRB2, and NCK (Fu and Chan 1997, Fu et al. 1998, Wienands et al. 1998, Su et al. 1999, Baba et al. 2001, Chiu et al. 2002). The SH2 domain of BTK binds phosphorylated BLNK (Hashimoto et al. 1999, Su et al. 1999, Baba et al. 2001). BLNK is constitutively bound to CIN85 and phosphorylated BLNK is bound to a large complex containing CIN85, SOS1, GRB2, phosphorylated SYK, and the B cell receptor.
Identifier: R-HSA-5607745
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Activation of SYK triggers multiple cascades, which induces NF-kB activation through a CARD9-dependent pathway. Phospholipase C-gamma 2 (PLCG2) is one of the key signaling components of the CLEC7A (Dectin-1) pathway that connects SYK activation to CARD9 recruitment. PLCG2 is activated upon CLEC7A engagement and triggers an intracellular Ca2+ flux. SYK and Src family kinases are upstream of PLCG2 (Xu et al. 2009, Tassi et al. 2009, Gorjestani et al. 2011). SYK phosphorylates PLCG2 on Y753 and Y759, enhancing the activity of PLCG2 (Suzuki-Inoue et al. 2004).
Identifier: R-HSA-9027373
Species: Homo sapiens
Compartment: plasma membrane
PLCG2 (PLCgamma2) binds phosphotyrosine-432 and phosphotyrosine-480 of EPOR (Montoye et al. 2005, and inferred from moue homologs). PLCG1 can also bind the phosphorylated EPOR (inferred from mouse homologs). After binding, PLCG2 is phosphorylated (Ren et al. 1994)
Identifier: R-HSA-9027425
Species: Homo sapiens
Compartment: plasma membrane
PLCG1 (Phospholipase C gamma1) or PLCG2 bound to the activated EPOR is phosphorylated on tyrosine residues by the kinase LYN (Ren et al. 1994, and inferred from mouse homologs).
Identifier: R-HSA-5621356
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Phospholipase C-gamma (PLCG) binds to phosphorylated Tyr-348 (Tyr-342 in mouse) and Tyr-352 (Tyr-346 in mouse) in SYK with its C-terminal SH2 domain (Law et al. 1996). PLCG2 functions downstream of CLEC6A/Dectin-2 and triggers cytokine production in response to the infection by Candida albicans. PLCG2 deficiency results in the defective production of NF-kB and significantly reduced production of reactive oxygen species (ROS) following infection (Gorjestani et al. 2011).
Identifier: R-HSA-2730888
Species: Homo sapiens
Compartment: plasma membrane, cytosol
Tyrosine phosphorylation of PLC-gamma enhances its catalytic activity. BTK and SYK are involved in the phosphorylation of PLC-gamma (PLCG). Phosphorylation of tyrosine residues 753, 759, 1197, and 1217 in PLCG2 and 771, 783, and 1254 in PLCG1 have been identified as BTK/SYK-dependent phosphorylation sites.
Identifier: R-HSA-9606887
Species: Homo sapiens
Compartment: plasma membrane
Phosphorylated CD19 binds PI3K (Roifman and Ke 1993, Chalupny et al. 1993, Uckun et al. 1993, Weng et al. 1994, Brooks et al. 2000, Brooks et al. 2004) and can bind PLC-gamma2 (PLCG2), which competes with VAV1 for the binding to phosphotyrosine-391 on CD19 (Brooks et al. 2000, Brooks et al. 2004). GRB2 appears to bind phosphotyrosine-330 on CD19 (Brooks et al. 2004).
Identifier: R-HSA-9032478
Species: Homo sapiens
Compartment: plasma membrane
Phospholipase C gamma (PLCG1 or PLCG2) bound to the phosphorylated cytoplasmic domain of the EPO receptor (EPOR) hydrolyzes 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to yield the second messengers diacylglycerol and 1D-myo-inositol 1,4,5-trisphosphate (Ren et al. 1994, and inferred from mouse). Erythropoietin may also activate the hydrolysis of phosphatidylcholine and phosphatidylethanolamine (inferred from mouse homologs),
Identifier: R-HSA-6787820
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
The receptor for Interleukin-34 (IL34) is colony stimulating factor 1 receptor (CSF1R), also called macrophage colony stimulating factor receptor (M-CSF-R). Dimeric IL34 and CSF1 bind the same general region of CSF1R, interacting with overlapping but distinct epitopes. Ligand binding leads to receptor dimerisation (Ma et al. 2012, Liu et al. 2012). Like CSF1, IL34 stimulation of CSF1R leads to phosphorylation of extracellular signal-regulated kinase (ERK) 1 and 2 in human monocytes (Lin et al. 2008). CSF1R activates several signaling pathways including JAK-STAT3, 5A/B, phosphorylation of PIK3R1, PLCG2, GRB2, SLA2 and CBL. PLCG2 phosphorylation leads to increassed production of the cellular signaling molecules diacylglycerol (DAG) and inositol 1,4,5 trisphosphate (IP3), which activate protein kinase C family members, especially PRKCD. Phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3 kinase, leads to activation of the AKT1 signaling pathway. Activated CSF1R also mediates activation of MAPK1 (ERK2) or MAPK3 (ERK1) and the SRC family kinases SRC, FYN and YES1. Activated CSF1R binds GRB2 and promotes tyrosine phosphorylation of SHC1 and INPP5D (SHIP1). Signaling is down regulated by protein phosphatases such as INPP5D that can dephosphorylate the receptor and its downstream effectors.
Identifier: R-HSA-1855221
Species: Homo sapiens
Compartment: plasma membrane, cytosol
A group of phospholipase C proteins (“PLC(degh)”) bind to the plasma membrane via their PH domains. These phospholipases hydrolyse phosphatidylinositol 4,5 bisphosphate (PI(4,5)P2) to inositol 1,4,5 trisphosphate (I(1,4,5)P3) and diacylglycerol (DAG). The C2 domains of the enzymes bind to PI(4,5)P2 at the membrane.

The phospholipase C isoforms involved and their corresponding literature references are: phosphoinositide phospholipase C delta-1(PLCD1) (Cheng et al. 1995); epsilon-1 (PLCE1) (Song et al. 2001, Lopez et al. 2001); delta-3 (PLCD3) (Pawelczyk & Matecki 1997); gamma-1 (PLCG1) (Harita et al. 2009, Baldassare et al. 1989); gamma-2 (PLCG2) (Banno et al. 1988); eta-1 (PLCH1) (Hwang et al. 2005); and eta-2 (PLCH2) (Zhou et al 2005).
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