p23 (PTGES3) binds HSP90:ATP:FKBP4:nascent protein

Stable Identifier
Reaction [transition]
Homo sapiens
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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).

Literature References
PubMed ID Title Journal Year
21183720 N-terminal domain of human Hsp90 triggers binding to the cochaperone p23

Karagöz, GE, Duarte, AM, Ippel, H, Uetrecht, C, Sinnige, T, van Rosmalen, M, Hausmann, J, Heck, AJ, Boelens, R, Rüdiger, SG

Proc. Natl. Acad. Sci. U.S.A. 2011
16403413 The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins

McLaughlin, SH, Sobott, F, Yao, ZP, Zhang, W, Nielsen, PR, Grossmann, JG, Laue, ED, Robinson, CV, Jackson, SE

J. Mol. Biol. 2006
Participant Of
Orthologous Events
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