Evidence map›Paper›PMID 11701883›Full record

ArticleThe Plant cell2001

14-3-3 proteins regulate intracellular localization of the bZIP transcriptional activator RSG.

D Igarashi, S Ishida, J Fukazawa, Y Takahashi

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

95 citing papers in PubMed, 212 citations in OpenAlex.

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35 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

D IgarashiDepartment of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo, Tokyo 113-0033, Japan.
S Ishida
J Fukazawa
Y Takahashi
The University of Tokyo · JPTokyo University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gibberellins (GAs) are essential regulators of many aspects of plant development, including stem elongation, seed germination, and flowering. RSG is a transcriptional activator with a basic leucine zipper domain that regulates endogenous amounts of GAs through the control of a GA biosynthetic enzyme. The ubiquitous expression of RSG in plant organs suggests an involvement of post-transcriptional and/or post-translational modifications of the transcription factor. Here, we identify the 14-3-3 signaling proteins as RSG binding partners. The mutant version of RSG that could not bind to 14-3-3 proteins exhibited a higher transcriptional activity than did wild-type RSG. Consistent with this observation, the mutant RSG that could not bind to 14-3-3 proteins was localized predominantly in the nucleus, whereas wild-type RSG was distributed throughout the cell. Using the nuclear export inhibitor leptomycin B, we also showed that RSG, apparently statically localized in the cytoplasm, is capable of shuttling in and out of the nucleus. These results suggest that 14-3-3 proteins negatively modulate RSG, which is involved in the regulation of endogenous amounts of GAs, by controlling its intracellular localization.

Indexed as

Plant Proteins14-3-3 ProteinsAmino Acid SequenceArabidopsisBase SequenceBasic-Leucine Zipper Transcription FactorsConserved SequenceDimerizationHumansLeucine ZippersMAP Kinase Signaling SystemMolecular Sequence DataMutagenesis, Site-DirectedNicotianaPlasmidsProtein Transport14-3-3 ProteinsBasic-Leucine Zipper Transcription FactorsPlant ProteinsRecombinant ProteinsRepressor ProteinsRSG protein, Nicotiana tabacumTrans-ActivatorsTranscription FactorsTyrosine 3-Monooxygenase

Identifiers

PMID11701883
PMCPMC139466
OpenAlexW2138019596

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.