ArticleMolecular and cellular biochemistry2005
CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone.
Article in Molecular and cellular biochemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
28 citing papers in PubMed, 51 citations in OpenAlex.
- The oncolytic avian reovirus p17 protein triggers chaperone-mediated autophagy by modulating Hsp90 and the T-complex protein-1 ring complex chaperones and co-chaperones to activate the IKK/NF-κB signaling.Journal of virology · 2025Article
- Protective effect of CK2 against endoplasmic reticulum stress in pancreatic β cells.Diabetology international · 2025Article
- Inhibition of casein kinase 2 induces cell death in tyrosine kinase inhibitor resistant chronic myelogenous leukemia cells.PloS one · 2023Article
- Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity.Sub-cellular biochemistry · 2023Article
- Therapeutic potential of CDK4/6 inhibitors in renal cell carcinoma.Nature reviews. Urology · 2022Review
- p17-Modulated Hsp90/Cdc37 Complex Governs Oncolytic Avian Reovirus Replication by Chaperoning p17, Which Promotes Viral Protein Synthesis and Accumulation of Viral Proteins σC and σA in Viral Factories.Journal of virology · 2022Article
- Targeting extracellular Hsp90: A unique frontier against cancer.Frontiers in molecular biosciences · 2022Review
- The structure-function relationship of oncogenic LMTK3.Science advances · 2020Article
- Post-translational modifications of Hsp90 and translating the chaperone code.The Journal of biological chemistry · 2020Review
- Coordinated targeting of CK2 and KIT in gastrointestinal stromal tumours.British journal of cancer · 2020Article
- Design of Disruptors of the Hsp90-Cdc37 Interface.Molecules (Basel, Switzerland) · 2020Article
- Cyclin-dependent kinase 7 (CDK7)-mediated phosphorylation of the CDK9 activation loop promotes P-TEFb assembly with Tat and proviral HIV reactivation.The Journal of biological chemistry · 2018Article
- The small-molecule kinase inhibitor D11 counteracts 17-AAG-mediated up-regulation of HSP70 in brain cancer cells.PloS one · 2017Article
- Structural and functional basis of protein phosphatase 5 substrate specificity.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.Scientific reports · 2016Article
- Protein kinase CK2 in breast cancer: the CK2β regulatory subunit takes center stage in epithelial plasticity.Cellular and molecular life sciences : CMLS · 2015Review
- Cdc37 as a co-chaperone to Hsp90.Sub-cellular biochemistry · 2015Review
- The molecular chaperone TRiC/CCT binds to the Trp-Asp 40 (WD40) repeat protein WDR68 and promotes its folding, protein kinase DYRK1A binding, and nuclear accumulation.The Journal of biological chemistry · 2014Article
- Transcriptome analysis of the Bombyx mori fat body after constant high temperature treatment shows differences between the sexes.Molecular biology reports · 2014Article
- The casein kinase 2-nrf1 axis controls the clearance of ubiquitinated proteins by regulating proteasome gene expression.Molecular and cellular biology · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein kinase CK2 phosphorylates and regulates a large number of substrates but roles of CK2 in protein kinase-mediated signal transduction systems remain largely uncertain. Cdc37 is a protein kinase-targeting molecular chaperone and its function in cooperation with Hsp90 is required for various signaling kinases. In this article, interaction between CK2 and Cdc37 is described. We present evidence indicating that phosphorylation of Cdc37 by CK2 in conserved Ser13 in the N-terminal extremity was prerequisite for the efficient binding activity of Cdc37 to protein kinases including Akt, Cdk4, MOK, and Raf1. In addition, the phosphorylation of Cdc37 by CK2 was crucial for the recruitment of Hsp90 to the protein kinase-Cdc37 complexes. We observed that a subset of CK2 was associated with Hsp90 and Cdc37 in cells. Whereas Hsp90 and Cdc37 were exclusively distributed in the cytoplasm, CK2alpha and CK2beta were localized mainly in the nucleus but also in the cytoplasm with different patterns. Moreover, direct association of Cdc37 with CK2alpha was observed in an E. coli system. Collectively, these findings indicated that a subpopulation of CK2 forms complexes with Hsp90 and Cdc37 in the cytoplasm and phosphorylates Cdc37, thus regulates the molecular chaperone activity of Cdc37. Since CK2 activity depends on Cdc37, CK2 and Cdc37 constitute a positive feedback machinery to control multiple Cdc37-dependent signaling protein kinases. The structure of Cdc37 and physiological importance of the CK2-Cdc37 interaction are discussed.
Indexed as
Identifiers
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.