The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
The Lysin Motif Receptor-like Kinase (LysM-RLK) CERK1 Is a Major Chitin-binding Protein in Arabidopsis thaliana and Subject to Chitin-induced Phosphorylation
Open accessAbstract
Plants detect potential pathogens by sensing microbe-associated molecular patterns via pattern recognition receptors. In the dicot model plant Arabidopsis, the lysin motif (LysM)-containing chitin elicitor receptor kinase 1 (CERK1) has been shown to be essential for perception of the fungal cell wall component chitin and for resistance to fungal pathogens. Recent in vitro studies with CERK1 protein expressed heterologously in yeast suggested direct chitin binding activity. Here we show in an affinity purification approach that CERK1 is a major chitin-binding protein of Arabidopsis cells, along with several known and putative chitinases. The ectodomain of CERK1 harbors three distinct LysM domains with potential ligand binding capacity. We demonstrate that the CERK1 ectodomain binds chitin and partially deacetylated chitosan directly without any requirement for interacting proteins and that all three LysM domains are necessary for chitin binding. Ligand-induced phosphorylation events are a general feature of animal and plant signal transduction pathways. Our studies show that chitin, chitin oligomers, and chitosan rapidly induce in vivo phosphorylation of CERK1 at multiple residues in the juxtamembrane and kinase domain. Functional analyses with a kinase dead variant provide evidence that kinase activity of CERK1 is required for its chitin-dependent in vivo phosphorylation, as well as for early defense responses and downstream signaling. Collectively, our data suggest that in Arabidopsis, CERK1 is a major chitin, chitosan, and chito-oligomer binding component and that chitin signaling depends on CERK1 post-translational modification and kinase activity.
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
Boller, T., & Felix, G. (2009) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.57.032905.105346 · Cited by 3,387
Chitosan as antimicrobial agent: applications and mode of action.
Rabea, E. I., Badawy, M. E.-T., Stevens, C. V., Smagghe, G., & Steurbaut, W. (2003) · Biomacromolecules · doi:10.1021/bm034130m · Cited by 3,123
Gómez-Gómez, L., & Boller, T. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80265-8 · Cited by 2,280
CERK1, a LysM receptor kinase, is essential for chitin elicitor signaling in Arabidopsis
Miya, A., Albert, P., Shinya, T., Desaki, Y., Ichimura, K., Shirasu, K., Narusaka, Y., Kawakami, N., Kaku, H., & Shibuya, N. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705147104 · Cited by 1,427
Plant recognition of symbiotic bacteria requires two LysM receptor-like kinases
Radutoiu, S., Madsen, L. H., Madsen, E. B., Felle, H. H., Umehara, Y., Grønlund, M., Sato, S., Nakamura, Y., Tabata, S., Sandal, N., et al. (2003) · Nature · doi:10.1038/nature02039 · Cited by 1,221
BRI1/BAK1, a Receptor Kinase Pair Mediating Brassinosteroid Signaling
Nam, K. H., & Li, J. (2002) · Cell · doi:10.1016/s0092-8674(02)00814-0 · Cited by 1,217
Plant cells recognize chitin fragments for defense signaling through a plasma membrane receptor
Kaku, H., Nishizawa, Y., Ishii-Minami, N., Akimoto-Tomiyama, C., Dohmae, N., Takio, K., Minami, E., & Shibuya, N. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508882103 · Cited by 1,166
A receptor kinase gene of the LysM type is involved in legumeperception of rhizobial signals
Madsen, E. B., Madsen, L. H., Radutoiu, S., Olbryt, M., Rakwalska, M., Szczyglowski, K., Sato, S., Kaneko, T., Tabata, S., Sandal, N., et al. (2003) · Nature · doi:10.1038/nature02045 · Cited by 1,018
LysM Domain Receptor Kinases Regulating Rhizobial Nod Factor-Induced Infection
Limpens, E., Franken, C., Smit, P., Willemse, J., Bisseling, T., & Geurts, R. (2003) · Science · doi:10.1126/science.1090074 · Cited by 868
BRI1 is a critical component of a plasma-membrane receptor for plant steroids
Wang, Z.-Y., Seto, H., Fujioka, S., Yoshida, S., & Chory, J. (2001) · Nature · doi:10.1038/35066597 · Cited by 846
Cited by
Chitin-Induced Dimerization Activates a Plant Immune Receptor
Liu, T., Liu, Z., Song, C., Hu, Y., Han, Z., She, J., Fan, F., Wang, J., Jin, C., Chang, J., et al. (2012) · Science · doi:10.1126/science.1218867 · Cited by 680
The role of the cell wall in plant immunity
Malinovsky, F. G., Fangel, J. U., & Willats, W. G. T. (2014) · Frontiers in Plant Science · doi:10.3389/fpls.2014.00178 · Cited by 555
Chitosan Effects on Plant Systems
Malerba, M., & Cerana, R. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17070996 · Cited by 528
Multiple effects of chitosan on plant systems: Solid science or hype
Hadwiger, L. A. (2013) · Plant Science · doi:10.1016/j.plantsci.2013.03.007 · Cited by 358
Hu, Y., Dong, Q., & Yu, D. (2012) · Plant Science · doi:10.1016/j.plantsci.2011.12.003 · Cited by 323
Metadata
- Authors
- Petutschnig, E. K., Jones, A. M. E., Serazetdinova, L., Lipka, U., & Lipka, V.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-09
- Volume
- 285
- Issue
- 37
- Pages
- 28902-28911
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2121660927
- Cited by
- 486
- References
- 39
- FWCI
- 37.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: The Lysin Motif Receptor-like Kinase (LysM-RLK) CERK1 Is a Major Chitin-binding Protein in Arabidopsis thaliana and Subject to Chitin-induced Phosphorylation. https://app.cochat.ai/papers/10.1074/jbc.m110.116657
- The paper
- Petutschnig, E. K., Jones, A. M. E., Serazetdinova, L., Lipka, U., & Lipka, V. (2010). The Lysin Motif Receptor-like Kinase (LysM-RLK) CERK1 Is a Major Chitin-binding Protein in Arabidopsis thaliana and Subject to Chitin-induced Phosphorylation. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m110.116657
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
