Biology:PTGES3

Generic protein structure example

Prostaglandin E synthase 3 (cytosolic) is an enzyme that in humans is encoded by the PTGES3 gene.

The protein encoded by this gene is also known as p23 which functions as a chaperone which is required for proper functioning of the glucocorticoid and other steroid receptors.

Further reading

• "Characterization of a novel 23-kilodalton protein of inactive progesterone receptor complexes". Mol. Cell. Biol. 14 (3): 1956–63. 1994. doi:10.1128/MCB.14.3.1956. PMID 8114727. 
• "Expression and cellular localization of cyclooxygenases and prostaglandin E synthases in the hemorrhagic brain.". J Neuroinflammation 8: 22. 2011. doi:10.1186/1742-2094-8-22. PMID 21385433. 
• "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. 1997. doi:10.1101/gr.6.9.791. PMID 8889548. 
• "Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90.p60.hsp70-dependent step is sufficient for creating the steroid binding conformation". J. Biol. Chem. 272 (20): 13047–13054. 1997. doi:10.1074/jbc.272.20.13047. PMID 9148915. 
• Dittmar KD; Demady DR; Stancato LF et al. (1997). "Folding of the glucocorticoid receptor by the heat shock protein (hsp) 90-based chaperone machinery. The role of p23 is to stabilize receptor.hsp90 heterocomplexes formed by hsp90.p60.hsp70". J. Biol. Chem. 272 (34): 21213–21220. doi:10.1074/jbc.272.34.21213. PMID 9261129. 
• Zou J; Guo Y; Guettouche T et al. (1998). "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1". Cell 94 (4): 471–480. doi:10.1016/S0092-8674(00)81588-3. PMID 9727490. 
• "Interaction of the p23/p198 protein with ErbB-3". Gene 229 (1–2): 215–221. 1999. doi:10.1016/S0378-1119(98)00604-0. PMID 10095121. 
• "Role for Hsp90-associated cochaperone p23 in estrogen receptor signal transduction". Mol. Cell. Biol. 19 (5): 3748–59. 1999. doi:10.1128/MCB.19.5.3748. PMID 10207098. 
• "The identification of Wos2, a p23 homologue that interacts with Wee1 and Cdc2 in the mitotic control of fission yeasts". Genetics 153 (4): 1561–72. 2000. doi:10.1093/genetics/153.4.1561. PMID 10581266. 
• "The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies". Genes Dev. 14 (4): 422–34. 2000. doi:10.1101/gad.14.4.422. PMID 10691735. 
• Weaver AJ; Sullivan WP; Felts SJ et al. (2000). "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone". J. Biol. Chem. 275 (30): 23045–23052. doi:10.1074/jbc.M003410200. PMID 10811660. 
• Tanioka T; Nakatani Y; Semmyo N et al. (2000). "Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis". J. Biol. Chem. 275 (42): 32775–32782. doi:10.1074/jbc.M003504200. PMID 10922363. 
• "The immunophilin-like protein XAP2 regulates ubiquitination and subcellular localization of the dioxin receptor". J. Biol. Chem. 275 (52): 41317–41324. 2001. doi:10.1074/jbc.M007765200. PMID 11013261. 
• Futatsumori M; Kasai K; Takatsu H et al. (2001). "Identification and characterization of novel isoforms of COP I subunits". J. Biochem. 128 (5): 793–801. doi:10.1093/oxfordjournals.jbchem.a022817. PMID 11056392. 
• "The hsp90 chaperone complex regulates intracellular localization of the dioxin receptor". Mol. Cell. Biol. 21 (7): 2594–2607. 2001. doi:10.1128/MCB.21.7.2594-2607.2001. PMID 11259606. 
• Forsythe HL; Jarvis JL; Turner JW et al. (2001). "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase". J. Biol. Chem. 276 (19): 15571–15574. doi:10.1074/jbc.C100055200. PMID 11274138. 
• "The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKR". EMBO J. 20 (14): 3771–3780. 2001. doi:10.1093/emboj/20.14.3771. PMID 11447118. 
• Elder RT; Yu M; Chen M et al. (2001). "HIV-1 Vpr induces cell cycle G2 arrest in fission yeast (Schizosaccharomyces pombe) through a pathway involving regulatory and catalytic subunits of PP2A and acting on both Wee1 and Cdc25". Virology 287 (2): 359–370. doi:10.1006/viro.2001.1007. PMID 11531413. 
• "HSP40 binding is the first step in the HSP90 chaperoning pathway for the progesterone receptor". J. Biol. Chem. 277 (14): 11873–11881. 2002. doi:10.1074/jbc.M111445200. PMID 11809754. 
• "Stimulation of the weak ATPase activity of human hsp90 by a client protein". J. Mol. Biol. 315 (4): 787–798. 2002. doi:10.1006/jmbi.2001.5245. PMID 11812147. 
• "The p23 co-chaperone facilitates dioxin receptor signaling in a yeast model system". Toxicol. Lett. 129 (1–2): 13–21. 2002. doi:10.1016/S0378-4274(01)00465-9. PMID 11879970.