ArticleMolecular and cellular biology2006
Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 45 citations in OpenAlex.
- Article
- Oncogenic non-V600 mutations evade the regulatory machinery of RAF including the Cdc37/Hsp90 chaperone and the 14-3-3 scaffold.Theranostics · 2025Article
- Epithelial-derived gasdermin D mediates nonlytic IL-1β release during experimental colitis.The Journal of clinical investigation · 2020Article
- A Synergistic Anticancer FAK and HDAC Inhibitor Combination Discovered by a Novel Chemical-Genetic High-Content Phenotypic Screen.Molecular cancer therapeutics · 2020Article
- Understanding the role of genetic variability in LRRK2 in Indian population.Movement disorders : official journal of the Movement Disorder Society · 2019Article
- Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery.Journal of hematology & oncology · 2018Review
- Phospho-proteomic analyses of B-Raf protein complexes reveal new regulatory principles.Oncotarget · 2016Article
- Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.The Journal of biological chemistry · 2015Article
- Arabidopsis TRIGALACTOSYLDIACYLGLYCEROL5 Interacts with TGD1, TGD2, and TGD4 to Facilitate Lipid Transfer from the Endoplasmic Reticulum to Plastids.The Plant cell · 2015Article
- Identification of a DYRK1A Inhibitor that Induces Degradation of the Target Kinase using Co-chaperone CDC37 fused with Luciferase nanoKAZ.Scientific reports · 2015Article
- Article
- Regulation of Greatwall kinase by protein stabilization and nuclear localization.Cell cycle (Georgetown, Tex.) · 2014Article
- Functions of the Hsp90 chaperone system: lifting client proteins to new heights.International journal of biochemistry and molecular biology · 2013Review
- 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
- Oral administration of an HSP90 inhibitor, 17-DMAG, intervenes tumor-cell infiltration into multiple organs and improves survival period for ATL model mice.Blood cancer journal · 2013Article
- ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system.Nature chemical biology · 2013Article
- Cdc37-Hsp90 complexes are responsive to nucleotide-induced conformational changes and binding of further cofactors.The Journal of biological chemistry · 2010Article
- HSP90 at the hub of protein homeostasis: emerging mechanistic insights.Nature reviews. Molecular cell biology · 2010Review
- Specific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.Circulation research · 2010Article
- The Hsp90 inhibitor geldanamycin abrogates colocalization of eIF4E and eIF4E-transporter into stress granules and association of eIF4E with eIF4G.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently, we identified a client-binding site of Cdc37 that is required for its association with protein kinases. Phage display technology and liquid chromatography-tandem mass spectrometry (which identifies a total of 33 proteins) consistently identify a unique sequence, GXFG, as a Cdc37-interacting motif that occurs in the canonical glycine-rich loop (GXGXXG) of protein kinases, regardless of their dependence on Hsp90 or Cdc37. The glycine-rich motif of Raf-1 (GSGSFG) is necessary for its association with Cdc37; nevertheless, the N lobe of Raf-1 (which includes the GSGSFG motif) on its own cannot interact with Cdc37. Chimeric mutants of Cdk2 and Cdk4, which differ sharply in their affinities toward Cdc37, show that their C-terminal portions may determine this difference. In addition, a nonclient kinase, the catalytic subunit of cyclic AMP-dependent protein kinase, interacts with Cdc37 but only when a threonine residue in the activation segment of its C lobe is unphosphorylated. Thus, although a region in the C termini of protein kinases may be crucial for accomplishing and maintaining their interaction with Cdc37, we conclude that the N-terminal glycine-rich loop of protein kinases is essential for physically associating with Cdc37.
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