Evidence map›Paper›PMID 28575660›Full record

ArticleMolecular cell2017

The F-box Protein KIB1 Mediates Brassinosteroid-Induced Inactivation and Degradation of GSK3-like Kinases in Arabidopsis.

Jia-Ying Zhu, Yuyao Li, Dong-Mei Cao, Hongjuan Yang, Eunkyoo Oh, Yang Bi, Shengwei Zhu, Zhi-Yong Wang

Open access · greenAbstract read
In one paragraph

Article in Molecular cell, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
23.8field-weighted citation impact, top 1% 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

67 citing papers in PubMed, 147 citations in OpenAlex.

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  18. Frontiers in plant science · 2024
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7 more citing papers are in PubMed but not listed here.

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 3 institutions in 3 countries.

Jia-Ying ZhuDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA.
Yuyao LiDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA.
Dong-Mei CaoKey Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China; Institute of Horticulture, Shanxi Academy of Agriculture Sciences, Taiyuan 030031, China.
Hongjuan YangDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA; Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Eunkyoo OhDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA; Department of Bioenergy Science and Technology, Chonnam National University, Gwangju 61186, South Korea.
Yang BiDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA; Department of Biology, Stanford University, Stanford, CA 94305, USA.
Shengwei ZhuDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA; Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Zhi-Yong WangDepartment of Plant Biology, Carnegie Institution for Science, Stanford, CA 94305, USA. Electronic address: zywang24@stanford.edu.
Carnegie Institution for Science · USDepartment of Plant Biology · USChinese Academy of Sciences · CN

Funding

Genetic Biochemical Studies of Signaling in Growth and AcclimationR01GM066258 · NIGMS · CARNEGIE INSTITUTION OF WASHINGTON, D.C. · PI ZHIYONG WANG · 2002 to 2026
$10.5M
NIGMS NIH HHS R01 GM066258
6 · The paper itself

Abstract

The glycogen synthase kinase-3 (GSK3) family kinases are central cellular regulators highly conserved in all eukaryotes. In Arabidopsis, the GSK3-like kinase BIN2 phosphorylates a range of proteins to control broad developmental processes, and BIN2 is degraded through unknown mechanism upon receptor kinase-mediated brassinosteroid (BR) signaling. Here we identify KIB1 as an F-box E3 ubiquitin ligase that promotes the degradation of BIN2 while blocking its substrate access. Loss-of-function mutations of KIB1 and its homologs abolished BR-induced BIN2 degradation and caused severe BR-insensitive phenotypes. KIB1 directly interacted with BIN2 in a BR-dependent manner and promoted BIN2 ubiquitination in vitro. Expression of an F-box-truncated KIB1 caused BIN2 accumulation but dephosphorylation of its substrate BZR1 and activation of BR responses because KIB1 blocked BIN2 binding to BZR1. Our study demonstrates that KIB1 plays an essential role in BR signaling by inhibiting BIN2 through dual mechanisms of blocking substrate access and promoting degradation.

Indexed as

ArabidopsisArabidopsis ProteinsBinding SitesBrassinosteroidsCatalytic DomainDNA-Binding ProteinsEnzyme ActivationEnzyme StabilityF-Box ProteinsGenotypeGlycogen Synthase Kinase 3MutationNuclear ProteinsPhenotypePlant Growth RegulatorsPlants, Genetically ModifiedArabidopsis ProteinsAt4g18710 protein, ArabidopsisbrassinolideBrassinosteroidsBRI1 protein, ArabidopsisBZR1 protein, ArabidopsisDNA-Binding ProteinsF-Box ProteinsGlycogen Synthase Kinase 3KIB1 protein, ArabidopsisNuclear ProteinsPlant Growth RegulatorsProteasome Endopeptidase ComplexProtein KinasesSteroids, HeterocyclicUbiquitin-Protein LigasesArabidopsisBIN2brassinosteroidE3 ubiquitin ligaseF-box proteinGSK3GSK3 degradationproteasomesteroid hormoneubiquitination

Identifiers

PMID28575660
PMCPMC5935450
OpenAlexW2621151921

What OpenQuestion holds

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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.