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- W3206039069 endingPage "109867" @default.
- W3206039069 startingPage "109867" @default.
- W3206039069 abstract "Phosphatidylinositol 3-kinase-related kinases (PIKKs) are a family of kinases that control fundamental processes, including cell growth, DNA damage repair, and gene expression. Although their regulation and activities are well characterized, little is known about how PIKKs fold and assemble into active complexes. Previous work has identified a heat shock protein 90 (Hsp90) cochaperone, the TTT complex, that specifically stabilizes PIKKs. Here, we describe a mechanism by which TTT promotes their de novo maturation in fission yeast. We show that TTT recognizes newly synthesized PIKKs during translation. Although PIKKs form multimeric complexes, we find that they do not engage in cotranslational assembly with their partners. Rather, our findings suggest a model by which TTT protects nascent PIKK polypeptides from misfolding and degradation because PIKKs acquire their native state after translation is terminated. Thus, PIKK maturation and assembly are temporally segregated, suggesting that the biogenesis of large complexes requires both dedicated chaperones and cotranslational interactions between subunits." @default.
- W3206039069 created "2021-10-25" @default.
- W3206039069 creator A5005339086 @default.
- W3206039069 creator A5016120084 @default.
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- W3206039069 creator A5030872396 @default.
- W3206039069 creator A5040437721 @default.
- W3206039069 creator A5045130861 @default.
- W3206039069 creator A5057207678 @default.
- W3206039069 date "2021-10-01" @default.
- W3206039069 modified "2023-10-17" @default.
- W3206039069 title "The Hsp90 cochaperone TTT promotes cotranslational maturation of PIKKs prior to complex assembly" @default.
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