The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural insight into guanylyl cyclase receptor hijacking of the kinase–Hsp90 regulatory mechanism
Open accessPreprint — published as 10.7554/elife.86784.3 · Paper page
Abstract
Abstract Membrane receptor guanylyl cyclases play a role in many important facets of human physiology, from regulating blood pressure to intestinal fluid secretion. The structural mechanisms which influence these important physiological processes have yet to be explored. We present the 3.9 Å resolution cryo-EM structure of the human membrane receptor guanylyl cyclase GC-C in complex with Hsp90 and its co-chaperone Cdc37, providing insight into the mechanism of Cdc37 mediated binding of GC-C to the Hsp90 regulatory complex. As a membrane protein and non-kinase client of Hsp90–Cdc37, this work shows the remarkable plasticity of Cdc37 to interact with a broad array of clients with significant sequence variation. Further, this work shows how membrane receptor guanylyl cyclases hijack the regulatory mechanisms used for active kinases to facilitate their regulation. Given the known druggability of Hsp90, these insights can guide the further development of membrane receptor guanylyl cyclase-targeted therapeutics and lead to new avenues to treat hypertension, inflammatory bowel disease, and other membrane receptor guanylyl cyclase-related conditions.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
Verba, K. A., Wang, R. Y.-R., Arakawa, A., Liu, Y., Shirouzu, M., Yokoyama, S., & Agard, D. A. (2016) · Science · doi:10.1126/science.aaf5023 · Cited by 424
Flagged first, then by citations
Research works printed but not linked: 32
- 2010, PHENIX: A comprehensive Python-based system for macromolecular structure solution, Acta Crystallographica Section D: Biological Crystallography, 66, 213, 10.1107/S0907444909052925 · DOI · Paper page
- 2021, Evaluating Local and Directional Resolution of Cryo-EM Density Maps, Methods in Molecular Biology, 2215, 161, 10.1007/978-1-0716-0966-8_8/COVER · DOI
- 2019, Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs, Nature Methods, 16, 1153, 10.1038/s41592-019-0575-8 · DOI
- 2010, MolProbity: All-atom structure validation for macromolecular crystallography, Acta Crystallographica Section D: Biological Crystallography, 66, 12, 10.1107/S0907444909042073 · DOI · Paper page
- 1994, Targeting of a distinctive protein-serine phosphatase to the protein kinase-like domain of the atrial natriuretic peptide receptor, Proceedings of the National Academy of Sciences, 91, 11075, 10.1073/PNAS.91.23.11075 · DOI
- 2004, Coot: Model-building tools for molecular graphics, Acta Crystallographica Section D: Biological Crystallography, 60, 2126, 10.1107/S0907444904019158 · DOI · Paper page
- 2022, Structure of the RAF1-HSP90-CDC37 complex reveals the basis of RAF1 regulation, Molecular Cell, 82, 3438, 10.1016/J.MOLCEL.2022.08.012 · DOI
- 2022, Structure of a Janus kinase cytokine receptor complex reveals the basis for dimeric activation, Science, 376, 163, 10.1126/science.abn8933 · DOI
- 2001a, Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone, Science, 293, 1657, 10.1126/SCIENCE.1062246/SUPPL_FILE/1062246S2_THUMB.GIF · DOI
- 2001b, Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone, Science, 293, 1657, 10.1126/SCIENCE.1062246/SUPPL_FILE/1062246S2_THUMB.GIF · DOI
- 2006, Structural Determinants of Natriuretic Peptide Receptor Specificity and Degeneracy, Journal of Molecular Biology, 361, 698, 10.1016/J.JMB.2006.06.060 · DOI
- 2019, Namdinator - Automatic molecular dynamics flexible fitting of structural models into cryo-EM and crystallography experimental maps, IUCrJ, 6, 526, 10.1107/S2052252519007619/EH5002SUP3.PDF · DOI
- 2012, Human Atrial Natriuretic Peptide Treatment for Acute Heart Failure: A Systematic Review of Efficacy and Mortality, Canadian Journal of Cardiology, 28, 102, 10.1016/j.cjca.2011.04.011 · DOI
- 2007, Inference of Macromolecular Assemblies from Crystalline State, Journal of Molecular Biology, 372, 774, 10.1016/j.jmb.2007.05.022 · DOI
- 2001, Regulation of the Atrial Natriuretic Peptide Receptor by Heat Shock Protein 90 Complexes, Journal of Biological Chemistry, 276, 11371, 10.1074/jbc.M010480200 · DOI
- 2020, Plecanatide for the treatment of constipation-predominant irritable bowel syndrome, 14, 71, 10.1080/17474124.2020.1722101 · DOI
- 2022, ColabFold: making protein folding accessible to all, Nature Methods, 19, 679, 10.1038/s41592-022-01488-1 · DOI · Paper page
- 2013. Collaboration gets the most out of software. ELife. · DOI
- 2022, HSP90-CDC37-PP5 forms a structural platform for kinase dephosphorylation, Nature Communications 2022 13:1, 13, 1, 10.1038/s41467-022-35143-2 · DOI
- 2004, Crystal structure of hormone-bound atrial natriuretic peptide receptor extracellular domain. Rotation mechanism for transmembrane signal transduction, Journal of Biological Chemistry, 279, 28625, 10.1074/JBC.M313222200/ATTACHMENT/31436558-57B4-4F07-AC3C-698401425198/MMC1.ZIP · DOI
- 2010, Reversibly bound chloride in the atrial natriuretic peptide receptor hormone-binding domain: Possible allosteric regulation and a conserved structural motif for the chloride-binding site, Protein Science, 19, 544, 10.1002/PRO.332 · DOI
- 2021, UCSF ChimeraX: Structure visualization for researchers, educators, and developers, Protein Science, 30, 70, 10.1002/pro.3943 · DOI
- 2011, Guanylyl cyclase structure, function and regulation, Cellular Signalling, 23, 1921, 10.1016/J.CELLSIG.2011.09.001 · DOI
- 1992, Dephosphorylation of the guanylyl cyclase-A receptor causes desensitization, Journal of Biological Chemistry, 267, 14531, 10.1016/S0021-9258(18)42069-8 · DOI
- 1998, Identification and Characterization of the Major Phosphorylation Sites of the B-type Natriuretic Peptide Receptor, Journal of Biological Chemistry, 273, 15533, 10.1074/JBC.273.25.15533 · DOI
- 2017, CryoSPARC: Algorithms for rapid unsupervised cryo-EM structure determination, Nature Methods, 14, 290, 10.1038/nmeth.4169 · DOI · Paper page
- 2020, Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction, Nature Methods, 17, 1214, 10.1038/s41592-020-00990-8 · DOI
- 2017, The HSP90 chaperone machinery, Nature Reviews Molecular Cell Biology 2017 18:6, 18, 345, 10.1038/nrm.2017.20 · DOI · Paper page
- 2012, Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition, Cell, 150, 987, 10.1016/J.CELL.2012.06.047 · DOI · Paper page
- 1993, Heat-stable enterotoxin activation of immunopurified guanylyl cyclase C. Modulation by adenine nucleotides, Journal of Biological Chemistry, 268, 19598, 10.1016/S0021-9258(19)36558-5 · DOI
- 2000, Structure of the dimerized hormone-binding domain of a guanylyl-cyclase-coupled receptor, Nature 2000 406:6791, 406, 101, 10.1038/35017602 · DOI
- 2014, Advances in the management of constipation-predominant irritable bowel syndrome: The role of linaclotide, Therapeutic Advances in Gastroenterology, 7, 193, 10.1177/1756283X14537882/ASSET/IMAGES/LARGE/10.1177_1756283X14537882-FIG2.JPEG · DOI
Metadata
- Authors
- Caveney, N. A., Tsutsumi, N., & Garcia, K. C.
- Affiliations
- Stanford Medicine (US)
- Howard Hughes Medical Institute (US)
- Departments of Molecular and Cellular Physiology and Structural Biology, Stanford University School of Medicine
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2023-07-12
- ISSN
- 2050-084X (ISSN-L)
- OpenAlex
- W4384028891
- Cited by
- 0
- References
- 2
- Type
- posted content
- Language
- en
- Open access
- gold
- doi.org
- Locations
- eLife (acceptedVersion, cc-by)
- Funders
- Canadian Institutes of Health Research (Postdoctoral Fellowship)
- National Institutes of Health (R01-AI51321)
- Mathers Foundation
- Ludwig Foundation
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- guanylyl cyclase C, HSP90, Cdc37, receptor structure, hypertension, inflammatory bowel disease
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
