Evidence map›Paper›PMID 23531692›Full record

ArticlePlant signaling & behavior2013

The emerging function of IQD proteins as scaffolds in cellular signaling and trafficking.

Steffen Abel, Katharina Bürstenbinder, Jens Müller

Open access · bronzeAbstract read
In one paragraph

Article in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.7field-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

36 citing papers in PubMed, 65 citations in OpenAlex.

  1. Review
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  12. Integrative analysis of grapevine (Frontiers in nutrition · 2023
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  16. Fruit shape lociFrontiers in plant science · 2022
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  18. Horticulture research · 2022
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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

3 authors at 2 institutions in 2 countries.

Steffen AbelDepartment of Molecular Signal Processing; Leibniz Institute of Plant Biochemistry; Halle, Germany; Institute of Biochemistry and Biotechnology; Martin-Luther-University Halle-Wittenberg; Halle, Germany; Department of Plant Sciences; University of California-Davis; Davis, USA.
Katharina Bürstenbinder
Jens Müller
Leibniz Institute of Plant Biochemistry · DEMartin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium (Ca(2+)) signaling modules are essential for adjusting plant growth and performance to environmental constraints. Differential interactions between sensors of Ca(2+) dynamics and their molecular targets are at the center of the transduction process. Calmodulin (CaM) and CaM-like (CML) proteins are principal Ca(2+)-sensors in plants that govern the activities of numerous downstream proteins with regulatory properties. The families of IQ67-Domain (IQD) proteins are a large class of plant-specific CaM/CML-targets (e.g., 33 members in A. thaliana) which share a unique domain of multiple varied CaM retention motifs in tandem orientation. Genetic studies in Arabidopsis and tomato revealed first roles for IQD proteins related to basal defense response and plant development. Molecular, biochemical and histochemical analysis of Arabidopsis IQD1 demonstrated association with microtubules as well as targeting to the cell nucleus and nucleolus. In vivo binding to CaM and kinesin light chain-related protein-1 (KLCR1) suggests a Ca(2+)-regulated scaffolding function of IQD1 in kinesin motor-dependent transport of multiprotein complexes. Furthermore, because IQD1 interacts in vitro with single-stranded nucleic acids, the prospect arises that IQD1 and other IQD family members facilitate cellular RNA localization as one mechanism to control and fine-tune gene expression and protein sorting.

Indexed as

Calcium SignalingArabidopsisArabidopsis ProteinsCalmodulinCalmodulin-Binding ProteinsMicrotubule-Associated ProteinsArabidopsis ProteinsCalmodulinCalmodulin-Binding ProteinsIQD1 protein, ArabidopsisMicrotubule-Associated Proteinscalciumcalmodulin-bindingcellular signalingcytoskeletonIQ motifkinesinmicrotubulesscaffold proteins

Identifiers

PMID23531692
PMCPMC3909082
OpenAlexW2127620425

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.