Search results for PLCG2

Showing 24 results out of 37

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Species

Types

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Protein (7 results from a total of 10)

Identifier: R-HSA-2023875
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: PLCG2: P16885
Identifier: R-HSA-1604645
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PLCG2: P16885
Identifier: R-HSA-984806
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P16885
Identifier: R-HSA-114601
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: P16885
Identifier: R-HSA-114602
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: PLCG2: P16885
Identifier: R-HSA-9029105
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PLCG2: P16885
Identifier: R-HSA-2685601
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: PLCG2: P16885

Reaction (7 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.

Complex (7 results from a total of 8)

Identifier: R-HSA-2023881
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-9606170
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-9606886
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-9606152
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-9606149
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-9606167
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-5621158
Species: Homo sapiens
Compartment: plasma membrane

Pathway (3 results from a total of 3)

Identifier: R-HSA-9027277
Species: Homo sapiens
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). PLCG1 and PLCG2 produce inositol 1,4,5-trisphosphate which then activates calcium signaling, and diacylglycerol (DAG) which then activates protein kinase C (PKC).
Identifier: R-HSA-5607763
Species: Homo sapiens
Compartment: plasma membrane, cytosol
CLEC7A (Dectin-1) signals through the classic calcineurin/NFAT pathway through Syk activation phospholipase C-gamma 2 (PLCG2) leading to increased soluble IP3 (inositol trisphosphate). IP3 is able to bind endoplasmic Ca2+ channels, resulting in an influx of Ca2+ into the cytoplasm. This increase in calcium concentration induces calcineurin activation and consequently, dephosphorylation of NFAT and its translocation into the nucleus, triggering gene transcription and extracellular release of Interleukin-2 (Plato et al. 2013, Goodridge et al. 2007, Mourao-Sa et al. 2011).
Identifier: R-HSA-9006335
Species: Homo sapiens
Erythropoietin (EPO) is a cytokine that serves as the primary regulator of erythropoiesis, the differentiation of erythrocytes from stem cells in the liver of the fetus and the bone marrow of adult mammals (reviewed in Ingley 2012, Zhang et al. 2014, Kuhrt and Wojchowski 2015). EPO is produced in the kidneys in response to low oxygen tension and binds a receptor, EPOR, located on progenitor cells: burst forming unit-erythroid (BFU-e) cells and colony forming unit-erythroid (CFU-e) cells.
The erythropoietin receptor (EPOR) exists in lipid rafts (reviewed in McGraw and List 2017) as a dimer pre-associated with proteins involved in downstream signaling: the tyrosine kinase JAK2, the tyrosine kinase LYN, and the scaffold protein IRS2. Binding of EPO to the EPOR dimer causes a change in conformation (reviewed in Watowich et al. 2011, Corbett et al. 2016) that activates JAK2, which then transphosphorylates JAK2 and phosphorylates the cytoplasmic domain of EPOR. The phosphorylated EPOR serves directly or indirectly as a docking site for signaling molecules such as STAT5, phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K), phospholipase C gamma (PLCG1, PLCG2), and activators of RAS (SHC1, GRB2:SOS1, GRB2:VAV1).
EPO activates 4 major signaling pathways: STAT5-activated transcription, PI3K-AKT, RAS-RAF-ERK, and PLC-PKC. JAK2-STAT5 activates expression of BCL2L1 (Bcl-xL) and therefore appears to be important for anti-apoptosis. PI3K-AKT appears to be important for both anti-apoptosis and proliferation. The roles of other signaling pathways are controversial but both RAS-RAF-MEK-ERK and PLCgamma-PKC have mitogenic effects. Phosphatases such as SHP1 are also recruited and downregulate the EPO signal.
EPO also has effects outside of erythropoiesis. The EPOR is expressed in various tissues such as endothelium where it can act to stimulate growth and promote cell survival (Debeljak et al. 2014, Kimáková et al. 2017). EPO and EPOR in the neurovascular system act via Akt, Wnt1, mTOR, SIRT1, and FOXO proteins to prevent apoptotic cell injury (reviewed in Ostrowski and Heinrich 2018, Maiese 2016) and EPO may have therapeutic value in the nervous system (Ma et al. 2016).
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