Search results for PTGES

Showing 20 results out of 27

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Species

Types

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Protein (6 results from a total of 6)

Identifier: R-HSA-2142717
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Primary external reference: UniProt: PTGES: O14684
Identifier: R-HSA-5082403
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: PTGES3: Q15185
Identifier: R-HSA-6799232
Species: Homo sapiens
Compartment: azurophil granule lumen
Primary external reference: UniProt: PTGES2: Q9H7Z7
Identifier: R-HSA-6806185
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: Q9H7Z7
Identifier: R-HSA-265269
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTGES3: Q15185
Identifier: R-HSA-5423596
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: PTGES2: Q9H7Z7

Complex (7 results from a total of 14)

Identifier: R-HSA-2142686
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane
Identifier: R-HSA-5324622
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-5324619
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-4793919
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-5082410
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-8948980
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-8948970
Species: Homo sapiens
Compartment: cytosol

Reaction (6 results from a total of 6)

Identifier: R-HSA-2161660
Species: Homo sapiens
Compartment: endoplasmic reticulum membrane, cytosol
Prostaglandin E synthase (PTGES) requires glutathione (GSH) as an essential cofactor for its enzymatic activity, and together they isomerise prostaglandin H2 (PGH2) to prostaglandin E2 (PGE2) (Jegerschold et al. 2008). After PGH2 has been produced by the prostaglandin G/H synthases (PTGS1 and 2) on the lumenal side of the endoplasmic reticulum, it diffuses through the membrane to the active site of PTGES located on the cytoplasmic side.
Identifier: R-HSA-5324617
Species: Homo sapiens
Compartment: nucleoplasm
Under non-stress conditions monomeric HSF1 is sequestered in a HSP90-containing heterocomplex. FKBP4 (immunophilin) is one of the components of HSP90-chaperone machinery which was found to associate with trimeric, but not monomeric form of HSF1 (Guo Y et al. 2001). Multichaperone complex of HSP90:FKBP4:PKGES3 has been shown to associate with HSF1 trimer through its regulatory domain, and this is thought to repress HSF1 transcriptional activity (Guo Y et al. 2001).

Identifier: R-HSA-5618098
Species: Homo sapiens
Compartment: cytosol
Immunophilin p23 (also known as PTGES3) binds selectively to the ATP-bound state of HSP90. p23 stabilizes the closed state of HSP90, which weakens the binding of STIP1(HOP) and promotes its exit from the complex (McLaughlin H et al. 2006; Karagöz GE et al. 2011). When FKBP51 (FKBP5) is present, a stable intermediate FKBP51:GR:HSP90:p23 is formed by expulsion of HSP70 and STIP1(HOP) (Ebong I et al. 2016).
Identifier: R-HSA-5618110
Species: Homo sapiens
Compartment: cytosol
Immunophilin p23 (also known as PTGES3) binds selectively to the ATP-bound state of HSP90. p23 stabilizes the closed state of HSP90, which weakens the binding of STIP1(HOP) and promotes its exit from the complex (McLaughlin H et al. 2006; Karagöz GE et al. 2011). When p23 is added to the client-transfer complex in the absence of the immunophilin or with FKBP51 (FKBP5), two copies of p23 are incorporated with concomitant loss of HSP70 and HOP (Ebong I et al. 2016). By contrast no stable complex with two p23 subunits is observed in the presence of FKBP52 (FKBP4); expulsion of HSP70, HOP and p23 occur with a low population of a complex incorporating only one p23 subunit (Ebong I et al. 2016).
Identifier: R-HSA-9690534
Species: Homo sapiens
Compartment: cytosol
Steroid hormones receptors (SHRs) are intracellular transcription factors that can be activated by binding specific ligands (i.e., steroid hormones (SH)) to the ligand-binding domain (LBD) (Ray DW et AL. 1999; Pike AC et al. 1999; Bledsoe RK et al. 2002; Li Y et al. 2005; Kumar R and McEwan IJ 2012; Kumar R et al. 2011; Williams SP & Sigler PB 1998; Tanenbaum DM et al. 1998; Lusher SJ et al. 2012). LBD (E-region) resides in the C-terminal half of the receptor and in addition to ligand binding function contains a transcriptional activation function (AF2), sequences for dimerization, heat shock protein association, intermolecular silencing and intramolecular repression (Kumar R and McEwan IJ 2012). The binding of hormone acts as an allosteric switch to regulate SHR-DNA and SHR-protein interactions, including interdomain interactions and/or dimerization (Kumar R and McEwan IJ 2012).

SHs are synthesized from cholesterol in the adrenal cortex (glucocorticoids, mineralocorticoids, and adrenal androgens), the testes (testicular androgens, estrogen), and the ovary and placenta (estrogen and progestogen or progestins) (Payne AH & Hales DB 2004; Hu J et al. 2010;). SHs reach their target cells via the blood, where they are bound to specific carrier proteins (Grishkovskaya I et al. 2000; Hammond GL 2016). SHs detach from the carrier proteins and because of their lipophilic nature readily diffuse through the plasma membrane of cells (Oren I et al. 2004). Within the target cells SHs bind to steroid hormone receptors (SHRs) which are present in a heterocomplex with heat shock protein HSP90 and co-chaperones (e.g., immunophilins p23) (Echeverria PC & Picard D 2010). The ATP-bound form of HSP90 and chaperone-mediated conformational changes are required to keep SHRs in a ligand binding-competent state (McLaughlin SH et al. 2002; Pratt WB et al. 2008; Krukenberg KA et al. 2011).

Identifier: R-HSA-5324632
Species: Homo sapiens
Compartment: cytosol
Proteotoxic stress results in an accumulation of misfolded proteins which tend to form insoluble protein aggregates. Histone deacetylase 6 (HDAC6) binds to ubiquitinated protein aggregates to regulate their degradation (Boyault C et al. 2006). HDAC6 was also found to interact with HSP90 and to regulate HSP90 chaperone complex activity via deacetylation of HSP90 (Kovacs JJ et al. 2005; Boyault C et al. 2007). Binding of HDAC6 to polyubiquitinted proteins triggers the dissociation of the HDAC6:HSP90:HSF1 complex resulting in the activation of HSF1 (Boyault C et al. 2007).

In the absence of stress HSF1 is predominantly monomeric and is thought to be repressed in its inactive monomeric state by the following mechanisms:

  • interaction with chaperone proteins such as HSP90 (Zou J et al.1998; Guo Y et al. 2001)
  • intramolecular coiled-coil interactions between a hydrophobic leucine zipper domain in the carboxyl-terminus of the protein and three amino-terminal leucine zippers, which are required for homotrimerization and transcriptional activation (Rabindran SK et al. 1993; Zuo J et al. 1995)
  • post-translation modifications that include protein acetylation, sumoylation and phosphorylation may also contribute to HSF1 repression (Knauf U et al. 1996; Hietakangas V et al. 2003; Batista-Nascimento L et al. 2011)

Set (1 results from a total of 1)

Identifier: R-HSA-8864254
Species: Homo sapiens
Compartment: cytosol
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