Evidence map›Paper›PMID 18945931›Full record

ArticlePlant physiology2008

Arabidopsis casein kinase 1-like 6 contains a microtubule-binding domain and affects the organization of cortical microtubules,.

Gili Ben-Nissan, Weier Cui, Dong-Jin Kim, Yaodong Yang, Byung-Chun Yoo, Jung-Youn Lee

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

42 citing papers in PubMed, 89 citations in OpenAlex.

  1. Plant signaling & behavior · 2026
    Article
  2. Molecular genetic characterization ofbioRxiv : the preprint server for biology · 2025
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  3. Article
  4. Visualizing the dynamics of plant energy organelles.Biochemical Society transactions · 2023
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  9. Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  10. Article
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  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The Molybdenum Cofactor Biosynthesis Network:Frontiers in plant science · 2017
    Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Gili Ben-NissanDepartment of Plant and Soil Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, Delaware 19711, USA.
Weier Cui
Dong-Jin Kim
Yaodong Yang
Byung-Chun Yoo
Jung-Youn Lee
University of Delaware · USDuPont (United States) · US

Funding

TOWARDS SOLID-STATE NMR STRUCTURES OF GPCRSP20RR015588 · NCRR · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2000 to 2009
$18.2M
NCRR NIH HHS P20 RR-15588
6 · The paper itself

Abstract

Members of the casein kinase 1 (CK1) family are evolutionarily conserved eukaryotic protein kinases that are involved in various cellular, physiological, and developmental processes in yeast and metazoans, but the biological roles of CK1 members in plants are not well understood. Here, we report that an Arabidopsis (Arabidopsis thaliana) CK1 member named casein kinase 1-like 6 (CKL6) associates with cortical microtubules in vivo and phosphorylates tubulins in vitro. The unique C-terminal domain of CKL6 was shown to contain the signal that allows localization of CKL6 to the cortical microtubules. This domain on its own was sufficient to associate with microtubules in vivo and to bind tubulins in vitro. CKL6 was able to phosphorylate soluble tubulins as well as microtubule polymers, and its endogenous activity was found to associate with a tubulin-enriched subcellular fraction. Two major in vitro phosphorylation sites were mapped to serine-413 and serine-420 of tubulin beta. Ectopic expression of wild-type CKL6 or a kinase-inactive mutant form induced alterations in cortical microtubule organization and anisotropic cell expansion. Collectively, these results demonstrate that CKL6 is a protein kinase containing a novel tubulin-binding domain and plays a role in anisotropic cell growth and shape formation in Arabidopsis through the regulation of microtubule organization, possibly through the phosphorylation of tubulins.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesCell EnlargementCell ShapeMicrotubulesMolecular Sequence DataPhenotypePhosphorylationProtein KinasesSequence AlignmentSerineTubulinArabidopsis ProteinsPAPK1 protein, ArabidopsisProtein KinasesSerineTubulin

Identifiers

PMID18945931
PMCPMC2593671
OpenAlexW2117912943

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.