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Details on Person HSP90 and FKBP8 interact through the TPR domain of FKBP8 and...

Class:IdSummation:9969053
_displayNameHSP90 and FKBP8 interact through the TPR domain of FKBP8 and...
_timestamp2026-02-06 20:28:46
created[InstanceEdit:9969048] Rothfels, Karen, 2025-10-20
modified[InstanceEdit:9976669] Rothfels, Karen, 2025-12-12
[InstanceEdit:9981288] Rothfels, Karen, 2026-02-06
textHSP90 and FKBP8 interact through the TPR domain of FKBP8 and the MEEVD motif of HSP90 (Okamoto et al, 2006; reviewed in Biebl and Buchner 2019) to promote the maturation of protein folding substrates, also known as clients. HSP90 additionally interacts with a p23 protein, which regulates the ATP hydrolysis cycle. p23 binds and stabilizes the closed conformation of HSP90, preventing ATP hydrolysis and client release (Li et al, 2017; reviewed in Li and Buchner, 2013; Biebl and Buchner, 2019).
In the context of motile axoneme assembly, HSP90 and FKBP8 associate with an array of cytosolic dynein arm assembly factors (DNAAFs) and the R2TP family of complexes and contribute to the assembly of inner and outer dynein arms (IDA and ODA respectively) prior to their translocation to the forming motile cilia (Mali et al, 2018; reviewed in Lynham and Houry, 2022; King, 2021; King, 2023; Desai et al, 2018). The exact roles of the DNAAFs and chaperone complexes and which axonemal dynein arm components they interact with remains to be fully elucidated.
(summation)[Reaction:9969493] HSP90 dimer binds FKBP8 [Homo sapiens]
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