ArticleCell stress & chaperones2007
Functioning of the Hsp90 machine in chaperoning checkpoint kinase I (Chk1) and the progesterone receptor (PR).
Article in Cell stress & chaperones, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- C1206, a novel curcumin derivative, potently inhibits Hsp90 and human chronic myeloid leukemia cells in vitro.Acta pharmacologica Sinica · 2018Article
- Nox5 stability and superoxide production is regulated by C-terminal binding of Hsp90 and CO-chaperones.Free radical biology & medicine · 2015Article
- Hsp70 clears misfolded kinases that partitioned into distinct quality-control compartments.Molecular biology of the cell · 2015Article
- Article
- Gedunin inactivates the co-chaperone p23 protein causing cancer cell death by apoptosis.The Journal of biological chemistry · 2013Article
- The therapeutic target Hsp90 and cancer hallmarks.Current pharmaceutical design · 2013Review
- Biochemical reconstitution of steroid receptor•Hsp90 protein complexes and reactivation of ligand binding.Journal of visualized experiments : JoVE · 2011Article
- Conformational dynamics of the molecular chaperone Hsp90.Quarterly reviews of biophysics · 2011Review
- Article
- Hsp90 and co-chaperones twist the functions of diverse client proteins.Biopolymers · 2010Review
- Celastrol inhibits Hsp90 chaperoning of steroid receptors by inducing fibrillization of the Co-chaperone p23.The Journal of biological chemistry · 2010Article
- Plasticity of the Hsp90 chaperone machine in divergent eukaryotic organisms.Cell stress & chaperones · 2009Article
- Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.Molecular and cellular biology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Hsp90 is an abundant and highly conserved chaperone that functions at later stages of protein folding to maintain and regulate the activity of client proteins. Using a recently described in vitro system to fold a functional model kinase Chk1, we performed a side-by-side comparison of the Hsp90-dependent chaperoning of Chk1 to that of the progesterone receptor (PR) and show that these distinct types of clients have different chaperoning requirements. The less stable PR required more total chaperone protein(s) and p23, whereas Chk1 folding was critically dependent on Cdc37. When the 2 clients were reconstituted under identical conditions, each client folding was dose dependent for Hsp90 protein levels and was inhibited by geldanamycin. Using this tractable system, we found that Chk1 kinase folding was more effective if we used a type II Hsp40 cochaperone, whereas PR is chaperoned equally well with a type I or type II Hsp40. Additional dissection of Chk1-chaperone complexes and the resulting kinase activity suggests that kinase folding, like that previously shown for PR, is a dynamic, multistep process. Importantly, the cochaperones Hop and Cdc37 cooperate as the kinase transitions from immature Hsp70- to mature Hsp90-predominant complexes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.