Evidence map›Paper›PMID 23204523›Full record

ArticleThe Journal of biological chemistry2013

Arabidopsis calmodulin-binding protein IQ67-domain 1 localizes to microtubules and interacts with kinesin light chain-related protein-1.

Katharina Bürstenbinder, Tatyana Savchenko, Jens Müller, Aaron W Adamson, Gina Stamm, Raymond Kwong, Brandon J Zipp, Dhurvas Chandrasekaran Dinesh, Steffen Abel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

58 citing papers in PubMed, 123 citations in OpenAlex.

  1. Horticulture research · 2026
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  2. A CaPlants (Basel, Switzerland) · 2026
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  8. The ER-PM interaction is essential for cytokinesis and recruits the actin cytoskeleton through the SCAR/WAVE complex.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  12. Functional Analysis of thePlants (Basel, Switzerland) · 2024
    Article
  13. Article
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  17. Mutation ofInternational journal of molecular sciences · 2023
    Article
  18. Review
  19. Integrative analysis of grapevine (Frontiers in nutrition · 2023
    Article
  20. Genome-Wide Identification of theInternational journal of molecular sciences · 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

9 authors at 2 institutions in 2 countries.

Katharina BürstenbinderDepartment of Molecular Signal Processing, Leibniz Institute of Plant Biochemistry, D-06120 Halle, Germany.
Tatyana Savchenko
Jens Müller
Aaron W Adamson
Gina Stamm
Raymond Kwong
Brandon J Zipp
Dhurvas Chandrasekaran Dinesh
Steffen Abel
University of California, Davis · USLeibniz Institute of Plant Biochemistry · DE

Funding

UC Davis MCB T32 Administrative Supplement to Recognize Excellence in Diversity, Equity, Inclusion, and Accessibility (DEIA) MentorshipT32GM007377 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI CHEDIN, FREDERIC LOUIS · 1985 to 2023
$9.9M
NIGMS NIH HHS T32 GM007377
6 · The paper itself

Abstract

Calcium (Ca(2+)) is a key second messenger in eukaryotes and regulates diverse cellular processes, most notably via calmodulin (CaM). In Arabidopsis thaliana, IQD1 (IQ67 domain 1) is the founding member of the IQD family of putative CaM targets. The 33 predicted IQD proteins share a conserved domain of 67 amino acids that is characterized by a unique arrangement of multiple CaM recruitment motifs, including so-called IQ motifs. Whereas IQD1 has been implicated in the regulation of defense metabolism, the biochemical functions of IQD proteins remain to be elucidated. In this study we show that IQD1 binds to multiple Arabidopsis CaM and CaM-like (CML) proteins in vitro and in yeast two-hybrid interaction assays. CaM overlay assays revealed moderate affinity of IQD1 to CaM2 (K(d) ∼ 0.6 μm). Deletion mapping of IQD1 demonstrated the importance of the IQ67 domain for CaM2 binding in vitro, which is corroborated by interaction of the shortest IQD member, IQD20, with Arabidopsis CaM/CMLs in yeast. A genetic screen of a cDNA library identified Arabidopsis kinesin light chain-related protein-1 (KLCR1) as an IQD1 interactor. The subcellular localization of GFP-tagged IQD1 proteins to microtubules and the cell nucleus in transiently and stably transformed plant tissues (tobacco leaves and Arabidopsis seedlings) suggests direct interaction of IQD1 and KLCR1 in planta that is supported by GFP∼IQD1-dependent recruitment of RFP∼KLCR1 and RFP∼CaM2 to microtubules. Collectively, the prospect arises that IQD1 and related proteins provide Ca(2+)/CaM-regulated scaffolds for facilitating cellular transport of specific cargo along microtubular tracks via kinesin motor proteins.

Indexed as

Gene Expression Regulation, PlantAmino Acid MotifsArabidopsisArabidopsis ProteinsBinding SitesCalciumCalcium SignalingCalmodulinCalmodulin-Binding ProteinsGene LibraryKinesinsKineticsMicroscopy, FluorescenceMicrotubule-Associated ProteinsMicrotubulesProtein BindingArabidopsis ProteinsCalciumCalmodulinCalmodulin-Binding ProteinsIQD1 protein, ArabidopsisKinesinsMicrotubule-Associated ProteinsProtein IsoformsRecombinant Fusion Proteins

Identifiers

PMID23204523
PMCPMC3548496
OpenAlexW2030402778

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.