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Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
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Abstract
Holding kinases at the ready: About 60% of kinases only reach their active state in the presence of the molecular chaperone Hsp90 and its co-chaperone Cdc37. It is unclear how the chaperones facilitate kinase function or why only some kinases are chaperone-dependent. Verba et al. determined a 3.9 Å cryo–electron microscopy structure of Hsp90:Cdc37 in complex with the kinase Cdk4. Together, Hsp90 and Cdc37 trap the kinase in an open, partially unfolded state. Taking on this state probably has direct functional benefits. Science , this issue p. 1542
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“have been identified to contact the unfolded Cdk4 client in the Hsp90:Cdc37:Cdk4 closed state structure”
From The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state (2021) · cites this paper as Verba et al., 2016
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“Cryo-EM structures of the client-bound Hsp90 reveal the client undergoes substantial unfolding, likely upon formation of the Hsp90 closed state”
From The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state (2021) · cites this paper as Verba et al., 2016
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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“in existing closed state structures (Huck et al., 2017; Verba et al., 2016) the CTD adopts this widened conformation in the absence of a bound H7e moiety, indicating this may result from NTD dimerization alone”
From The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state (2021) · cites this paper as Verba et al., 2016
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Both clients are threaded through the closed Hsp90 lumen, suggesting a universal binding mode for Hsp90 clients11,35”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [11]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“we found that two hydrophobic residues may represent the common binding pattern of the Hsp90 client, which are I271 and I274 in AhR, L525 and L528 in GR,33 and V89 and V92 in Cdk428”
From Cryo-EM structure of the cytosolic AhR complex. (2023) · cites this paper as [28]
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In the citing paper
“The N-lobe of Cdk4 is unfolded and threaded though the MD dimer cleft in the Hsp90:Cdc37:Cdk4 structure exposing a strand of residues that would be inaccessible in the folded state”
From The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state (2021) · cites this paper as Verba et al., 2016
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“sharply contrasting with the unfolded kinase:Hsp90 structure11.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [11]
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“The kinase:Hsp90 structure11 first revealed how Hsp90 can stabilize an inactive client, but provided no insights to explain how Hsp90 can reactivate a client, such as GR.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [11]
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“The active, native GR in our complex starkly contrasts with the only other structure of a closed Hsp90:client complex, which stabilizes an unfolded kinase client11.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [11]
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“These findings support an emerging paradigm in which Hsp90 cochaperones make specific, direct contact with Hsp90 clients to aid in client recognition and function11,12.”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [11]
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“20 mM sodium molybdate (used to stabilize the closed conformation of Hsp9011,42,43, likely by acting as a γ-phosphate analog to stabilize the post-ATP hydrolysis transition state of Hsp90 (Extended Data Fig. 2c))”
From Structure of Hsp90–p23–GR reveals the Hsp90 client-remodelling mechanism (2022) · cites this paper as [11]
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“In the Hsp90:FKBP51:p23 structure FKBP51 extends from the CTD-TPR interaction along the Hsp90 MD, enabling the N-terminal FK1 domain to be positioned adjacent Hsp90 client interaction sites”
From The structure of an Hsp90-immunophilin complex reveals cochaperone recognition of the client maturation state (2021) · cites this paper as Verba et al., 2016
Experimental — accuracy not yet measuredIn the citing paper
“and by mediating client interaction [e.g., the kinase-specific Cdc37 (5, 6)].”
From Client binding shifts the populations of dynamic Hsp90 conformations through an allosteric network (2021) · cites this paper as [6]
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Cites
UCSF Chimera—A visualization system for exploratory research and analysis
Pettersen, E. F., Goddard, T. D., Huang, C. C., Couch, G. S., Greenblatt, D. M., Meng, E. C., & Ferrin, T. E. (2004) · Journal of Computational Chemistry · doi:10.1002/jcc.20084 · Cited by 45,882
Features and development of Coot
Emsley, P., Lohkamp, B., Scott, W. G., & Cowtan, K. (2010) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444910007493 · Cited by 29,915
Scalable molecular dynamics with NAMD
Phillips, J. C., Braun, R., Wang, W., Gumbart, J., Tajkhorshid, E., Villa, E., Chipot, C., Skeel, R. D., Kalé, L., & Schulten, K. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20289 · Cited by 16,914
RELION: Implementation of a Bayesian approach to cryo-EM structure determination
Scheres, S. H. W. (2012) · Journal of Structural Biology · doi:10.1016/j.jsb.2012.09.006 · Cited by 5,446
CTFFIND4: Fast and accurate defocus estimation from electron micrographs
Rohou, A. L., & Grigorieff, N. (2015) · Journal of Structural Biology · doi:10.1016/j.jsb.2015.08.008 · Cited by 4,759
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
Davis, I., Leaver‐Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B., Snoeyink, J. S., Richardson, J. S., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm216 · Cited by 3,918
EMAN2: An extensible image processing suite for electron microscopy
Tang, G., Peng, L., Baldwin, P. R., Mann, D. S., Jiang, W., Rees, I., & Ludtke, S. J. (2006) · Journal of Structural Biology · doi:10.1016/j.jsb.2006.05.009 · Cited by 2,914
Targeting cancer with small molecule kinase inhibitors
Zhang, J., Yang, P. L., & Gray, N. S. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2559 · Cited by 2,648
Rosenthal, P. B., & Henderson, R. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.07.013 · Cited by 2,416
Li, X.-M., Mooney, P., Zheng, S., Booth, C., Braunfeld, M. B., Gubbens, S., Agard, D., & Cheng, Y.-F. (2013) · Nature Methods · doi:10.1038/nmeth.2472 · Cited by 1,866
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Jin, Y., Kotler, J. L. M., Wang, S., Huang, B., Halpin, J. C., & Street, T. O. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.166963 · Cited by 15
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Verkhivker, G. M. (2022) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167506 · Cited by 15
Peng, S., Woodruff, J., Pathak, P. K., Matts, R. L., & Deng, J. (2022) · Acta Crystallographica Section D Structural Biology · doi:10.1107/s2059798322002261 · Cited by 15
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Hardman, G. E., Perkins, S. R., Ruan, Z., Kannan, N., Brownridge, P., Byrne, D. P., Eyers, P. A., Jones, A. R., & Eyers, C. E. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/202820 · Cited by 15
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Natarajan, N., Shaik, A., & Thiruvenkatam, V. (2020) · ACS Omega · doi:10.1021/acsomega.0c02480 · Cited by 7
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Tassone, G., Mangani, S., Botta, M., & Pozzi, C. (2018) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2018.09.005 · Cited by 7
Godoy-Castillo, C., Bravo-Acuña, N., Arriagada, G., Faunes, F., León, R., & Soto‐Delgado, J. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1803134 · Cited by 7
Kanugovi, A., & Subbarao, S. A. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118943 · Cited by 7
Kirschke, E., Roe-Zurz, Z., Noddings, C., & Agard, D. (2020) · doi:10.1101/2020.05.03.075523 · Cited by 6
Self-citationWang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2020) · doi:10.1101/2020.11.05.370247 · Cited by 10
Self-citationIizumi, Y., Sowa, Y., Goi, W., Aono, Y., Watanabe, M., Kurumida, Y., Kameda, T., Akaji, K., Kitagawa, M., & Sakai, T. (2022) · Communications Biology · doi:10.1038/s42003-022-03522-6 · Cited by 9
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Self-citationTych, K. M., & Rief, M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2229-2_15 · Cited by 6
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Ihama, F., Yamamoto, M., Kojima, C., Fujiwara, T., Matsuzaki, K., Miyata, Y., & Hoshino, M. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.06.007 · Cited by 5
Metadata
- Authors
- Verba, K. A., Wang, R. Y.-R., Arakawa, A., Liu, Y., Shirouzu, M., Yokoyama, S., & Agard, D. A.
- Affiliations
- Howard Hughes Medical Institute (US)
- RIKEN (JP)
- Corresponding author
- Agard, David A.
- ORCID
- Venue
- Science
- Published
- 2016-06-24
- Volume
- 352
- Issue
- 6293
- Pages
- 1542-1547
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- PMC
- PMC5373496
- OpenAlex
- W2467034934
- Semantic Scholar
- be9d874235bbeead8cd0fdf0f8296dc124cc3bd3
- Cited by
- 424
- References
- 58
- Citations by year
- 2026: 25 · 2025: 23 · 2024: 35 · 2023: 44 · 2022: 53 · 2021: 52 · 2020: 52 · 2019: 52 · 2018: 40 · 2017: 39 · 2016: 7
- FWCI
- 23.90
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Licence
- cc-by-nc-nd
- Locations
- Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Protein Structure Initiative-Biology (U01 GM098254)
- American Association for Cancer Research-Breast Cancer Research Foundation (218084)
- HHMI Helen Hay Whitney Foundation Fellowship
- HHMI International Student Research Fellowship
- HHMI
- NIH National Institute of General Medical Sciences (P41 GM103310)
- NSF (ACI-1053575)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- HSP90, Cdc37, CDK4, kinase activation, molecular chaperones, protein complex structure
- MeSH terms
- Animals, Enzyme Stability, Humans, Models, Molecular, Protein Structure, Secondary, Cell Cycle Proteins, Chaperonins, HSP90 Heat-Shock Proteins, Multiprotein Complexes, Cyclin-Dependent Kinase 4, Protein Unfolding, Sf9 Cells
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