ArticleThe Journal of biological chemistry2015
Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90.Nature communications · 2024Article
- Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones.Biomolecules · 2022Article
- Assembly mechanism of early Hsp90-Cdc37-kinase complexes.Science advances · 2022Article
- Nematode CDC-37 and DNJ-13 form complexes and can interact with HSP-90.Scientific reports · 2021Article
- HSP-90/kinase complexes are stabilized by the large PPIase FKB-6.Scientific reports · 2021Article
- Hsp90 modulates human sperm capacitation via the Erk1/2 and p38 MAPK signaling pathways.Reproductive biology and endocrinology : RB&E · 2021Article
- Epithelial-derived gasdermin D mediates nonlytic IL-1β release during experimental colitis.The Journal of clinical investigation · 2020Article
- Coordinated targeting of CK2 and KIT in gastrointestinal stromal tumours.British journal of cancer · 2020Article
- Structure, Function, and Regulation of the Hsp90 Machinery.Cold Spring Harbor perspectives in biology · 2019Review
- CDC37 as a novel target for the treatment of NPM1-ALK expressing anaplastic large cell lymphomas.Blood cancer journal · 2019Article
- Therapeutic Potential of the Hsp90/Cdc37 Interaction in Neurodegenerative Diseases.Frontiers in neuroscience · 2019Review
- Nonsteroidal Anti-inflammatory Drugs Potently Inhibit the Replication of Zika Viruses by Inducing the Degradation of AXL.Journal of virology · 2018Article
- Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery.Journal of hematology & oncology · 2018Review
- Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System.Structure (London, England : 1993) · 2018Article
- Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation.Nature communications · 2018Article
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- The HSP90 chaperone machinery.Nature reviews. Molecular cell biology · 2017Review
- Myocyte-Derived Hsp90 Modulates Collagen Upregulation via Biphasic Activation of STAT-3 in Fibroblasts during Cardiac Hypertrophy.Molecular and cellular biology · 2017Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein kinases are the most prominent group of heat shock protein 90 (Hsp90) clients and are recruited to the molecular chaperone by the kinase-specific cochaperone cell division cycle 37 (Cdc37). The interaction between Hsp90 and nematode Cdc37 is mediated by binding of the Hsp90 middle domain to an N-terminal region of Caenorhabditis elegans Cdc37 (CeCdc37). Here we map the binding site by NMR spectroscopy and define amino acids relevant for the interaction between CeCdc37 and the middle domain of Hsp90. Apart from these distinct Cdc37/Hsp90 interfaces, binding of the B-Raf protein kinase to the cochaperone is conserved between mammals and nematodes. In both cases, the C-terminal part of Cdc37 is relevant for kinase binding, whereas the N-terminal domain displaces the nucleotide from the kinase. This interaction leads to a cooperative formation of the ternary complex of Cdc37 and kinase with Hsp90. For the mitogen-activated protein kinase extracellular signal-regulated kinase 2 (Erk2), we observe that certain features of the interaction with Cdc37·Hsp90 are conserved, but the contribution of Cdc37 domains varies slightly, implying that different kinases may utilize distinct variations of this binding mode to interact with the Hsp90 chaperone machinery.
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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.