Jasmonate perception by inositol-phosphate-potentiated COI1–JAZ co-receptor
Open accessAbstract
Jasmonates are a family of plant hormones that regulate plant growth, development and responses to stress. The F-box protein CORONATINE INSENSITIVE 1 (COI1) mediates jasmonate signalling by promoting hormone-dependent ubiquitylation and degradation of transcriptional repressor JAZ proteins. Despite its importance, the mechanism of jasmonate perception remains unclear. Here we present structural and pharmacological data to show that the true Arabidopsis jasmonate receptor is a complex of both COI1 and JAZ. COI1 contains an open pocket that recognizes the bioactive hormone (3R,7S)-jasmonoyl-l-isoleucine (JA-Ile) with high specificity. High-affinity hormone binding requires a bipartite JAZ degron sequence consisting of a conserved α-helix for COI1 docking and a loop region to trap the hormone in its binding pocket. In addition, we identify a third critical component of the jasmonate co-receptor complex, inositol pentakisphosphate, which interacts with both COI1 and JAZ adjacent to the ligand. Our results unravel the mechanism of jasmonate perception and highlight the ability of F-box proteins to evolve as multi-component signalling hubs.
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
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Weak interactions between MG protein partners are echoed by low μM affinities reported for DCAF15-RBM39, DDB1-CDK12-Cyclin K, and JAZ1-COI1.
“Moreover, their weak interactions are echoed by the low μM affinities recently reported for the DCAF15-RBM39 and DDB1-CDK12-Cyclin K interacting partners22,29 as well as the bipartite degron of JAZ1 that docks to the F-box protein COI1 via an α-helix next to the binding pocket of jasmonate-isoleucine, another MG plant hormone45.”
From Defining molecular glues with a dual-nanobody cannabidiol sensor (2022) · cites this paper as [45]
Methyl jasmonate glues the E3 ligase SCF COI1 to the transcriptional repressor JAZ.
“This hormone glues the E3 ligase SCF COI1 to the transcriptional repressor JAZ.73”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [73]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Colowick, S. P., Joshi, M. D., Jagannathan, & KAPLAN, N. O. (1966) · Cited by 26,137 · see citing works
NMRPipe: A multidimensional spectral processing system based on UNIX pipes
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., & Bax, A. (1995) · Journal of Biomolecular NMR · doi:10.1007/bf00197809 · Cited by 15,994 · see citing works
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,720 · see citing works
Yung-Chi, C., & Prusoff, W. H. (1973) · Biochemical Pharmacology · doi:10.1016/0006-2952(73)90196-2 · Cited by 12,922 · see citing works
Jones, T. A., Zou, J.-Y., Cowan, S. W., & Kjeldgaard, M. (1991) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767390010224 · Cited by 12,650 · see citing works
<i>PHENIX</i> : building new software for automated crystallographic structure determination
Adams, P. D., Grosse-Kunstleve, R. W., Hung, L.-W., Ioerger, T. R., McCoy, A. J., Moriarty, N. W., Read, R. J., Sacchettini, J. C., Sauter, N. K., & Terwilliger, T. C. (2002) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444902016657 · Cited by 4,361 · see citing works
JAZ repressor proteins are targets of the SCFCOI1 complex during jasmonate signalling
Thines, B. C., Katsir, L., Melotto, M., Niu, Y., Mandaokar, A. D., Liu, G., Nomura, K., He, S. Y., Howe, G. A., & Browse, J. (2007) · Nature · doi:10.1038/nature05960 · Cited by 2,530 · see citing works
Self-citationThe JAZ family of repressors is the missing link in jasmonate signalling
Chini, A., Fonseca, S., Santos-Fernandez, G., Adie, B. A. T., Chico, J. M., Lorenzo, Ó., García‐Casado, G., López‐Vidriero, I., Lozano, F. M., Ponce, M. R., et al. (2007) · Nature · doi:10.1038/nature06006 · Cited by 2,426 · see citing works
The F-box protein TIR1 is an auxin receptor
Dharmasiri, N., Dharmasiri, S., & Estelle, M. (2005) · Nature · doi:10.1038/nature03543 · Cited by 2,083 · see citing works
The Arabidopsis F-box protein TIR1 is an auxin receptor
Kepinski, S., & Leyser, O. (2005) · Nature · doi:10.1038/nature03542 · Cited by 1,716 · see citing works
Mechanism of auxin perception by the TIR1 ubiquitin ligase
Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688 · see citing works
Self-citationCOI1 : An Arabidopsis Gene Required for Jasmonate-Regulated Defense and Fertility
Xie, D., Feys, B., James, S., Nieto‐Rostro, M., & Turner, J. G. (1998) · Science · doi:10.1126/science.280.5366.1091 · Cited by 1,657 · see citing works
Lorenzo, Ó., Chico, J. M., Sánchez‐Serrano, J. J., & Solano, R. (2004) · The Plant Cell · doi:10.1105/tpc.022319 · Cited by 1,348 · see citing works
Staswick, P., & Tiryaki, İ. (2004) · The Plant Cell · doi:10.1105/tpc.104.023549 · Cited by 1,119 · see citing works
Using NMRView to Visualize and Analyze the NMR Spectra of Macromolecules
Johnson, B. A. (2004) · Humana Press eBooks · doi:10.1385/1-59259-809-9:313 · Cited by 1,032 · see citing works
(+)-7-iso-Jasmonoyl-L-isoleucine is the endogenous bioactive jasmonate
Fonseca, S., Chini, A., Hámberg, M., Adie, B. A. T., Porzel, A., Kramell, R., Miersch, O., Wasternack, C. H., & Solano, R. (2009) · Nature Chemical Biology · doi:10.1038/nchembio.161 · Cited by 1,008 · see citing works
Feys, B. J., Benedetti, C. E., Penfold, C. N., & Turner, J. G. (1994) · The Plant Cell · doi:10.1105/tpc.6.5.751 · Cited by 1,007 · see citing works
Jasmonate Passes Muster: A Receptor and Targets for the Defense Hormone
Browse, J. (2008) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.043008.092007 · Cited by 946 · see citing works
Self-citationKatsir, L., Schilmiller, A. L., Staswick, P., He, S. Y., & Howe, G. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802332105 · Cited by 822 · see citing works
Self-citationThe Arabidopsis CORONATINE INSENSITIVE1 Protein Is a Jasmonate Receptor
Yan, J., Zhang, C., Gu, M., Bai, Z., Zhang, W., Qi, T., Cheng, Z.-W., Peng, W., Luo, H., Nan, F., et al. (2009) · The Plant Cell · doi:10.1105/tpc.109.065730 · Cited by 794 · see citing works
Gibberellin-induced DELLA recognition by the gibberellin receptor GID1
Murase, K., Hirano, Y., Sun, T., & Hakoshima, T. (2008) · Nature · doi:10.1038/nature07519 · Cited by 789 · see citing works
A gate–latch–lock mechanism for hormone signalling by abscisic acid receptors
Melcher, K., Ng, L.-M., Zhou, X. E., Soon, F.-F., Xu, Y., Suino-Powell, K. M., Park, S.-Y., Weiner, J. J., Fujii, H., Chinnusamy, V., et al. (2009) · Nature · doi:10.1038/nature08613 · Cited by 731 · see citing works
A Downstream Mediator in the Growth Repression Limb of the Jasmonate Pathway
Yan, Y., Stolz, S., Chételat, A., Reymond, P., Pagni, M., Dubugnon, L., & Farmer, E. E. (2007) · The Plant Cell · doi:10.1105/tpc.107.050708 · Cited by 703 · see citing works
Structural basis of abscisic acid signalling
Miyazono, K., Miyakawa, T., Sawano, Y., Kubota, K., Kang, H., Asano, A., Miyauchi, Y., Takahashi, M., Zhi, Y., Fujita, Y., et al. (2009) · Nature · doi:10.1038/nature08583 · Cited by 578 · see citing works
The abscisic acid receptor PYR1 in complex with abscisic acid
Santiago, J., Dupeux, F., Round, A. R., Antoni, R., Park, S., Jamin, M., Cutler, S. R., Rodrı́guez, P. L., & Márquez, J. A. (2009) · Nature · doi:10.1038/nature08591 · Cited by 536 · see citing works
Structural Mechanism of Abscisic Acid Binding and Signaling by Dimeric PYR1
Nishimura, N., Hitomi, K., Arvai, A. S., Rambo, R. P., Hitomi, C., Cutler, S. R., Schroeder, J. I., & Getzoff, E. D. (2009) · Science · doi:10.1126/science.1181829 · Cited by 493 · see citing works
Structural insights into the mechanism of abscisic acid signaling by PYL proteins
Yin, P., Fan, H., Hao, Q., Yuan, X., Wu, D., Pang, Y., Yan, C., Li, W., Wang, J., & Yan, N. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1730 · Cited by 462 · see citing works
Chung, H. S., & Howe, G. A. (2009) · The Plant Cell · doi:10.1105/tpc.108.064097 · Cited by 449 · see citing works
Self-citationA rapid wound signal activates the systemic synthesis of bioactive jasmonates in Arabidopsis
Koo, A. J., Gao, X., Jones, A. D., & Howe, G. A. (2009) · The Plant Journal · doi:10.1111/j.1365-313x.2009.03924.x · Cited by 437 · see citing works
Self-citationMelotto, M., Mecey, C., Niu, Y., et al. (2008) · The Plant Journal · doi:10.1111/j.1365-313x.2008.03566.x · Cited by 406 · see citing works
Structural basis for gibberellin recognition by its receptor GID1
Shimada, A., Ueguchi‐Tanaka, M., Nakatsu, T., Nakajima, M., Naoe, Y., Ohmiya, H., Kato, H., & Matsuoka, M. (2008) · Nature · doi:10.1038/nature07546 · Cited by 373 · see citing works
The role of JAR1 in Jasmonoyl-l-isoleucine production during Arabidopsis wound response
Suza, W. P., & Staswick, P. (2008) · Planta · doi:10.1007/s00425-008-0694-4 · Cited by 257 · see citing works
Expression of the Arabidopsis jasmonate signalling repressor JAZ1/TIFY10A is stimulated by auxin
Grunewald, W., Vanholme, B., Pauwels, L., et al. (2009) · EMBO Reports · doi:10.1038/embor.2009.103 · Cited by 201 · see citing works
Alternative splicing expands the repertoire of dominant JAZ repressors of jasmonate signaling
Chung, H. S., Cooke, T. F., DePew, C. L., et al. (2010) · The Plant Journal · doi:10.1111/j.1365-313x.2010.04265.x · Cited by 190 · see citing works
Nettleton, E. J., Sunde, M., Lai, Z., Kelly, J. W., Dobson, C. M., & Robinson, C. V. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1937 · Cited by 174 · see citing works
Stephens, L., Hawkins, P. T., STANLEY, A. F., et al. (1991) · Biochemical Journal · doi:10.1042/bj2750485 · Cited by 107 · see citing works
Simultaneous measurement of multiple membrane ATPases in microtiter plates
Sadrzadeh, S. M. H., Vincenzi, F. F., & Hinds, T. R. (1993) · Journal of Pharmacological and Toxicological Methods · doi:10.1016/1056-8719(93)90013-5 · Cited by 29 · see citing works
Self-citationStrategy for synthesis of the isoleucine conjugate of epi-jasmonic acid
Ogawa, N., & Kobayashi, Y. (2008) · Tetrahedron Letters · doi:10.1016/j.tetlet.2008.09.144 · Cited by 16 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Wasternack, C., & Hause, B. (2013) · Annals of Botany · doi:10.1093/aob/mct067 · Cited by 2,629 · see citing works
Ubiquitin ligases: structure, function, and regulation
Zheng, N., & Shabek, N. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060815-014922 · Cited by 1,499 · see citing works
Structural basis of PROTAC cooperative recognition for selective protein degradation
Gadd, M. S., Testa, A., Lucas, X., Chan, K.-H., Chen, W., Lamont, D. J., Zengerle, M., & Ciulli, A. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2329 · Cited by 1,242 · see citing works
A novel cereblon modulator recruits GSPT1 to the CRL4CRBN ubiquitin ligase
Matyskiela, M. E., Lu, G., Ito, T., Pagarigan, B., Lu, C.-C., Miller, K., Fang, W., Wang, N.-Y., Nguyen, D., Houston, J., et al. (2016) · Nature · doi:10.1038/nature18611 · Cited by 701 · see citing works
Modulators of Protein–Protein Interactions
Milroy, L.-G., Grossmann, T. N., Hennig, S., Brunsveld, L., & Ottmann, C. (2014) · Chemical Reviews · doi:10.1021/cr400698c · Cited by 497 · see citing works
Development of targeted protein degradation therapeutics
Chamberlain, P. P., & Hamann, L. G. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0362-y · Cited by 489 · see citing works
Drugging the undruggables: exploring the ubiquitin system for drug development
Huang, X., & Dixit, V. M. (2016) · Cell Research · doi:10.1038/cr.2016.31 · Cited by 427 · see citing works
Jasmonate-responsive transcription factors regulating plant secondary metabolism
Zhou, M., & Memelink, J. (2016) · Biotechnology Advances · doi:10.1016/j.biotechadv.2016.02.004 · Cited by 378 · see citing works
Molecular Glues for Targeted Protein Degradation: From Serendipity to Rational Discovery
Dong, G., Ding, Y., He, S., & Sheng, C. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00895 · Cited by 369 · see citing works
Self-citationSantiago, J., Henzler, C., & Hothorn, M. (2013) · Science · doi:10.1126/science.1242468 · Cited by 357 · see citing works
WD40 repeat domain proteins: a novel target class?
Schapira, M., Tyers, M., Torrent, M., & Arrowsmith, C. H. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.179 · Cited by 335 · see citing works
A Cereblon Modulator (CC-220) with Improved Degradation of Ikaros and Aiolos
Matyskiela, M. E., Zhang, W., Man, H.-W., Muller, G., Khambatta, G., Baculi, F., Hickman, M., LeBrun, L., Pagarigan, B., Carmel, G., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01921 · Cited by 309 · see citing works
Hughes, S. J., & Ciulli, A. (2017) · Essays in Biochemistry · doi:10.1042/ebc20170041 · Cited by 240 · see citing works
Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15
Faust, T. B., Yoon, H., Nowak, R. P., Donovan, K. A., Li, Z., Cai, Q., Eleuteri, N. A., Zhang, T., Gray, N. S., & Fischer, E. S. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0378-3 · Cited by 218 · see citing works
Structural regulation of cullin-RING ubiquitin ligase complexes
Duda, D. M., Scott, D. C., Calabrese, M. F., Zimmerman, E. S., Zheng, N., & Schulman, B. A. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.01.003 · Cited by 205 · see citing works
Self-citationChasing molecular glue degraders: screening approaches
Domostegui, A., Nieto-Barrado, L., Perez-Lopez, C., & Mayor-Ruiz, C. (2022) · Chemical Society Reviews · doi:10.1039/d2cs00197g · Cited by 200 · see citing works
Haven't got a glue: Protein surface variation for the design of molecular glue degraders
Kozicka, Z., & Thomä, N. H. (2021) · Cell Chemical Biology · doi:10.1016/j.chembiol.2021.04.009 · Cited by 170 · see citing works
Defining molecular glues with a dual-nanobody cannabidiol sensor
Cao, S., Kang, S., Mao, H., Yao, J., Gu, L., & Zheng, N. (2022) · Nature Communications · doi:10.1038/s41467-022-28507-1 · Cited by 125 · see citing works
Self-citationCereblon modulators: Low molecular weight inducers of protein degradation
Chamberlain, P. P., & Cathers, B. E. (2019) · Drug Discovery Today: Technologies · doi:10.1016/j.ddtec.2019.02.004 · Cited by 106 · see citing works
Jasmonates: Biosynthesis, perception and signal transduction
Griffiths, G. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190085 · Cited by 103 · see citing works
Cold stress improves the production of artemisinin depending on the increase in endogenous jasmonate
Liu, W., Wang, H., Chen, Y., Zhu, S., Chen, M., Lan, X., Chen, G., & Liao, Z. (2017) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1493 · Cited by 68 · see citing works
UM171 glues asymmetric CRL3–HDAC1/2 assembly to degrade CoREST corepressors
Yeo, M. J. R., Zhang, O., Xie, X., Nam, E., Payne, N. C., Gosavi, P. M., Kwok, H. S., Iram, I., Lee, C., Li, J., et al. (2025) · Nature · doi:10.1038/s41586-024-08532-4 · Cited by 58 · see citing works
Self-citation
- Authors
- Sheard, L. B., Tan, X., Mao, H., Withers, J., Ben-Nissan, G., Hinds, T. R., Kobayashi, Y., Hsu, F.-F., Sharon, M., Browse, J., He, S. Y., Rizo, J., Howe, G. A., & Zheng, N.
- Affiliations
- University of Washington (US)
- Michigan State University (US)
- Tokyo Institute of Technology (JP)
- Washington University in St. Louis (US)
- Weizmann Institute of Science (IL)
- Washington State University (US)
- The University of Texas Southwestern Medical Center (US)
- Howard Hughes Medical Institute (US)
- Corresponding author
- Zheng, Ning
- ORCID
- Venue
- Nature
- Published
- 2010-10-06
- Volume
- 468
- Issue
- 7322
- Pages
- 400-405
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC2988090
- OpenAlex
- W2156475745
- Cited by
- 1,497
- References
- 38
- Citations by year
- 2026: 97 · 2025: 114 · 2024: 105 · 2023: 93 · 2022: 105 · 2021: 110 · 2020: 115 · 2019: 110 · 2018: 72 · 2017: 100 · 2016: 93 · 2015: 88 · 2014: 81 · 2013: 82 · 2012: 71
- FWCI
- 82.09
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- ResearchWorks at the University of Washington (University of Washington) (submittedVersion)
- Tokyo Tech Research Repository (Tokyo Institute of Technology) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (R01CA107134)
- National Institute of General Medical Sciences (R01GM057795, T32-GM07270, R01GM57795, T32GM007270)
- National Institute of Allergy and Infectious Diseases (R01AI068718)
- National Institute of Diabetes and Digestive and Kidney Diseases (P30DK056341)
- Argonne National Laboratory
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
- Life Sciences › Agricultural and Biological Sciences › Insect Science › Insect-Plant Interactions and Control
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
- Keywords
- COI1, JAZ proteins, inositol pentakisphosphate, F-box protein, jasmonoyl-L-isoleucine, hormone-receptor complex, ubiquitination, transcriptional repressor, Arabidopsis thaliana, plant hormone signaling, ligand specificity, plant defense response
- MeSH terms
- Amino Acid Sequence, Amino Acids, Binding Sites, Cyclopentanes, Indenes, Inositol Phosphates, Isoleucine, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Plant Growth Regulators, Protein Binding, Repressor Proteins, Signal Transduction, Arabidopsis, Protein Structure, Tertiary, Crystallography, X-Ray, Arabidopsis Proteins, F-Box Proteins, Oxylipins
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
