Evidence map›Paper›PMID 25331450›Full record

ArticleCell research2014

Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1.

Jie Wang, Jianjun Jiang, Jue Wang, Lei Chen, Shi-Long Fan, Jia-Wei Wu, Xuelu Wang, Zhi-Xin Wang

Open access · bronzeAbstract read
In one paragraph

Article in Cell research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

47 citing papers in PubMed, 93 citations in OpenAlex.

  1. Plant cell surface receptors.The Plant journal : for cell and molecular biology · 2026
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  7. Preventing inappropriate signals pre- and post-ligand perception by a toggle switch mechanism of ERECTA.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Jie WangMOE Key Laboratory for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Jianjun JiangState Key Laboratory of Genetic Engineering and Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai 200433, China.
Jue WangMOE Key Laboratory for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Lei ChenMOE Key Laboratory for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Shi-Long FanMOE Key Laboratory for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Jia-Wei WuMOE Key Laboratory for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Xuelu Wang1] State Key Laboratory of Genetic Engineering and Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai 200433, China [2] College of Life Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, China.
Zhi-Xin WangMOE Key Laboratory for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Tsinghua University · CNFudan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Brassinosteroids (BRs) are essential steroid hormones that have crucial roles in plant growth and development. BRs are perceived by the cell-surface receptor-like kinase brassinosteroid insensitive 1 (BRI1). In the absence of BRs, the cytosolic kinase domain (KD) of BRI1 is inhibited by its auto-inhibitory carboxyl terminus, as well as by interacting with an inhibitor protein, BRI1 kinase inhibitor 1 (BKI1). How BR binding to the extracellular domain of BRI1 leads to activation of the KD and dissociation of BKI1 into the cytosol remains unclear. Here we report the crystal structure of BRI1 KD in complex with the interacting peptide derived from BKI1. We also provide biochemical evidence that BRI1-associated kinase 1 (BAK1) plays an essential role in initiating BR signaling. Steroid-dependent heterodimerization of BRI1 and BAK1 ectodomains brings their cytoplasmic KDs in the right orientation for competing with BKI1 and transphosphorylation.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCrystallography, X-RayMolecular Docking SimulationMolecular Sequence DataPhenotypePhosphorylationPlants, Genetically ModifiedProtein KinasesProtein Structure, TertiarySequence AlignmentSignal TransductionArabidopsis ProteinsBKI1 protein, ArabidopsisBRI1 protein, ArabidopsisProtein Kinases

Identifiers

PMID25331450
PMCPMC4220157
OpenAlexW2086757600

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.