Evidence map›Paper›PMID 19395409›Full record

ArticlePlant physiology2009

BIN2 functions redundantly with other Arabidopsis GSK3-like kinases to regulate brassinosteroid signaling.

Zhenyan Yan, Jun Zhao, Peng Peng, Ray K Chihara, Jianming Li

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
11.4field-weighted citation impact, top 2% 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

108 citing papers in PubMed, 218 citations in OpenAlex.

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48 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

5 authors at 1 institution in 1 country.

Zhenyan YanDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109-1048, USA.
Jun Zhao
Peng Peng
Ray K Chihara
Jianming Li
University of Michigan–Ann Arbor · US

Funding

MOLECULAR GENETIC STUDIES OF PLANT STEROID SIGNALINGR01GM060519 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LI, JIANMING · 2000 to 2008
$2.3M
NIGMS NIH HHS GM60519NIGMS NIH HHS R01 GM060519
6 · The paper itself

Abstract

GLYCOGEN SYNTHASE KINASE3 (GSK3) is a highly conserved serine/threonine kinase involved in a variety of developmental signaling processes. The Arabidopsis (Arabidopsis thaliana) genome encodes 10 GSK3-like kinases that are clustered into four groups. Forward genetic screens have so far uncovered eight mutants, all of which carry gain-of-function mutations in BRASSINOSTEROID-INSENSITIVE2 (BIN2), one of the three members in group II. Genetic and biochemical studies have implicated a negative regulatory role for BIN2 in brassinosteroid (BR) signaling. Here, we report the identification of eight ethyl methanesulfonate-mutagenized loss-of-function bin2 alleles and one T-DNA insertional mutation each for BIN2 and its two closest homologs, BIN2-Like1 and BIN2-Like2. Our genetic, biochemical, and physiological assays revealed that despite functional redundancy, BIN2 plays a dominant role among the three group II members in regulating BR signaling. Surprisingly, the bin2bil1bil2 triple T-DNA insertional mutant still responds to BR and accumulates a more phosphorylated form of a BIN2 substrate than the wild-type plant. Using the specific GSK3 inhibitor lithium chloride, we have provided strong circumstantial evidence for the involvement of other Arabidopsis GSK3-like kinases in BR signaling. Interestingly, lithium chloride treatment was able to suppress the gain-of-function bin2-1 mutation but had a much weaker effect on a strong BR receptor mutant, suggesting the presence of a BIN2-independent regulatory step downstream of BR receptor activation.

Indexed as

Signal TransductionAmino Acid SequenceArabidopsisArabidopsis ProteinsBrassinosteroidsCholestanolsDNA, BacterialGlycogen Synthase Kinase 3Lithium ChlorideMolecular Sequence DataMutagenesis, InsertionalMutant ProteinsMutationPhosphorylationProtein KinasesSequence Homology, Amino AcidArabidopsis ProteinsAt4g18710 protein, ArabidopsisbrassinolideBrassinosteroidsCholestanolsDNA, BacterialGlycogen Synthase Kinase 3Lithium ChlorideMutant ProteinsProtein KinasesSteroids, HeterocyclicT-DNA

Identifiers

PMID19395409
PMCPMC2689954
OpenAlexW2144466680

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.