Evidence map›Paper›PMID 21118996›Full record

ArticleMolecular biology of the cell2011

Homodimerization of Nemo-like kinase is essential for activation and nuclear localization.

Shizuka Ishitani, Kenji Inaba, Kunihiro Matsumoto, Tohru Ishitani

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Atypical MAPKs in cancer.The FEBS journal · 2025
    Review
  4. Article
  5. Therapeutic Targeting of Nemo-like Kinase in Primary and Acquired Endocrine-resistant Breast Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. β-Catenin-related protein WRM-1 is a multifunctional regulatory subunit of the LIT-1 MAPK complex.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Article
  14. On the electrostatic properties of homodimeric proteins.Journal of theoretical & computational chemistry · 2014
    Article
  15. Article
  16. Polyglutamine disease toxicity is regulated by Nemo-like kinase in spinocerebellar ataxia type 1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  17. Article
  18. Article
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

4 authors at 2 institutions in 1 country.

Shizuka IshitaniDivision of Cell Regulation Systems, Department of Post-Genome Science Center, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.
Kenji Inaba
Kunihiro Matsumoto
Tohru Ishitani
Kyushu University · JPNagoya University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nemo-like kinase (NLK) is an evolutionarily conserved protein kinase that phosphorylates several transcription factors. However, the molecular mechanisms that regulate NLK activity have been poorly understood. Here we show that homodimerization of NLK is required for its activation and nuclear localization. Biochemical analysis revealed that NLK is activated through intermolecular autophosphorylation of NLK dimers at Thr-286. Mutation of NLK at Cys-425, which corresponds to the defect in the Caenorhabditis elegans NLK homologue lit-1, prevented NLK dimerization, rendering NLK defective in both nuclear localization and kinase activity. By contrast, the external addition of nerve growth factor, which has been previously identified as an NLK activator, induced dimerization and Thr-286 autophosphorylation of endogenous NLK proteins. In addition, both dimerization and Thr-286 phosphorylation of NLK were found to be essential for induction of neurite-like cellular processes by NLK. The present findings suggest that dimerization is an initial key event required for the functional activation of NLK.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceAnimalsCysteineEnzyme ActivationHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsMolecular Sequence DataMutagenesis, Site-DirectedNerve Growth FactorNeuritesPC12 CellsPhosphorylationProtein MultimerizationCysteineIntracellular Signaling Peptides and ProteinsNerve Growth FactorNLK protein, humanProtein Serine-Threonine KinasesThreonine

Identifiers

PMID21118996
PMCPMC3020921
OpenAlexW2155222830

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.