Evidence map›Paper›PMID 25415978›Full record

ArticleThe Plant cell2014

The microtubule plus-end tracking proteins SPR1 and EB1b interact to maintain polar cell elongation and directional organ growth in Arabidopsis.

Charitha Galva, Viktor Kirik, Jelmer J Lindeboom, Despoina Kaloriti, David M Rancour, Patrick J Hussey, Sebastian Y Bednarek, David W Ehrhardt, John C Sedbrook

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

33 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
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  9. Genome-Wide Identification, Characterization, and Expression Analysis ofInternational journal of molecular sciences · 2023
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  14. iScience · 2021
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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

9 authors at 4 institutions in 2 countries.

Charitha GalvaSchool of Biological Sciences, Illinois State University, Normal, Illinois 61790.
Viktor KirikSchool of Biological Sciences, Illinois State University, Normal, Illinois 61790.
Jelmer J LindeboomCarnegie Institution for Science, Stanford, California 94305.
Despoina KaloritiSchool of Biological Sciences, Illinois State University, Normal, Illinois 61790.
David M RancourDepartment of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706.
Patrick J HusseySchool of Biological and Biomedical Sciences, Durham University, Durham DH1 3LE, United Kingdom.
Sebastian Y BednarekDepartment of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706.
David W EhrhardtCarnegie Institution for Science, Stanford, California 94305.
John C SedbrookSchool of Biological Sciences, Illinois State University, Normal, Illinois 61790 jcsedbr@ilstu.edu.
Illinois State University · USCarnegie Institution for Science · USUniversity of Wisconsin–Madison · USDurham University · GB

Funding

Elucidating conserved mechanisms of noncentrosomal microtubule array formationR15GM102839 · NIGMS · ILLINOIS STATE UNIVERSITY · PI KIRIK, VIKTOR · 2013 to 2013
$288k
NIGMS NIH HHS R15 GM102839
6 · The paper itself

Abstract

The microtubule plus-end tracking proteins (+TIPs) END BINDING1b (EB1b) and SPIRAL1 (SPR1) are required for normal cell expansion and organ growth. EB proteins are viewed as central regulators of +TIPs and cell polarity in animals; SPR1 homologs are specific to plants. To explore if EB1b and SPR1 fundamentally function together, we combined genetic, biochemical, and cell imaging approaches in Arabidopsis thaliana. We found that eb1b-2 spr1-6 double mutant roots exhibit substantially more severe polar expansion defects than either single mutant, undergoing right-looping growth and severe axial twisting instead of waving on tilted hard-agar surfaces. Protein interaction assays revealed that EB1b and SPR1 bind each other and tubulin heterodimers, which is suggestive of a microtubule loading mechanism. EB1b and SPR1 show antagonistic association with microtubules in vitro. Surprisingly, our combined analyses revealed that SPR1 can load onto microtubules and function independently of EB1 proteins, setting SPR1 apart from most studied +TIPs in animals and fungi. Moreover, we found that the severity of defects in microtubule dynamics in spr1 eb1b mutant hypocotyl cells correlated well with the severity of growth defects. These data indicate that SPR1 and EB1b have complex interactions as they load onto microtubule plus ends and direct polar cell expansion and organ growth in response to directional cues.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCell EnlargementCell PolarityGenes, ReporterHypocotylMicrotubule-Associated ProteinsMicrotubulesMolecular Sequence DataMutagenesis, InsertionalPhenotypePlant RootsPlants, Genetically ModifiedTubulinTwo-Hybrid System TechniquesArabidopsis ProteinsEB1b protein, ArabidopsisEB1c protein, ArabidopsisMicrotubule-Associated ProteinsSPR1 protein, ArabidopsisTubulin

Identifiers

PMID25415978
PMCPMC4277225
OpenAlexW2045796800

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.