ArticleThe Journal of cell biology2002
The Cdc37 protein kinase-binding domain is sufficient for protein kinase activity and cell viability.
Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
35 citing papers in PubMed, 69 citations in OpenAlex.
- A fluorescence-based sensor for calibrated measurement of protein kinase stability in live cells.Protein science : a publication of the Protein Society · 2024Article
- A Fluorescence-Based Sensor for Calibrated Measurement of Protein Kinase Stability in Live Cells.bioRxiv : the preprint server for biology · 2023Article
- HSPA8 acts as an amyloidase to suppress necroptosis by inhibiting and reversing functional amyloid formation.Cell research · 2023Article
- Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery.Acta pharmaceutica Sinica. B · 2020Review
- Yeast can accommodate phosphotyrosine: v-Src toxicity in yeast arises from a single disrupted pathway.FEMS yeast research · 2018Article
- An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.Nature communications · 2017Article
- Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.Molecular cell · 2016Article
- Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.Biochemistry · 2015Article
- Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins.Oncogene · 2015Article
- Structural bioinformatics and protein docking analysis of the molecular chaperone-kinase interactions: towards allosteric inhibition of protein kinases by targeting the hsp90-cdc37 chaperone machinery.Pharmaceuticals (Basel, Switzerland) · 2013Article
- Novel interaction between the co-chaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth.The Journal of biological chemistry · 2013Article
- Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Review
- Quality control and fate determination of Hsp90 client proteins.Biochimica et biophysica acta · 2012Review
- Conformational dynamics of the molecular chaperone Hsp90.Quarterly reviews of biophysics · 2011Review
- Specific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.Circulation research · 2010Article
- Silencing the cochaperone CDC37 destabilizes kinase clients and sensitizes cancer cells to HSP90 inhibitors.Oncogene · 2009Article
- Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.Molecular cell · 2008Article
- Ydj1 protects nascent protein kinases from degradation and controls the rate of their maturation.Molecular and cellular biology · 2008Article
- Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Cdc37 is a molecular chaperone required for folding of protein kinases. It functions in association with Hsp90, although little is known of its mechanism of action or where it fits into a folding pathway involving other Hsp90 cochaperones. Using a genetic approach with Saccharomyces cerevisiae, we show that CDC37 overexpression suppressed a defect in v-Src folding in yeast deleted for STI1, which recruits Hsp90 to misfolded clients. Expression of CDC37 truncation mutants that were deleted for the Hsp90-binding site stabilized v-Src and led to some folding in both sti1Delta and hsc82Delta strains. The protein kinase-binding domain of Cdc37 was sufficient for yeast cell viability and permitted efficient signaling through the yeast MAP kinase-signaling pathway. We propose a model in which Cdc37 can function independently of Hsp90, although its ability to do so is restricted by its normally low expression levels. This may be a form of regulation by which cells restrict access to Cdc37 until it has passed through a triage involving other chaperones such as Hsp70 and Hsp90.
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What OpenQuestion holds
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.