Evidence map›Paper›PMID 20200159›Full record

ArticleThe Journal of biological chemistry2010

The LAMMER kinase homolog, Lkh1, regulates Tup transcriptional repressors through phosphorylation in Schizosaccharomyces pombe.

Won-Hwa Kang, Yun-Hee Park, Hee-Moon Park

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
–field-weighted citation impact
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.

  1. Article
  2. Article
  3. Pleiotropic roles of LAMMER kinase, Lkh1 in stress responses and virulence ofFrontiers in cellular and infection microbiology · 2024
    Article
  4. Review
  5. Article
  6. The LAMMER Kinase MoKns1 Regulates Growth, Conidiation and Pathogenicity inInternational journal of molecular sciences · 2022
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
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.

Won-Hwa KangDepartment of Microbiology, School of Bioscience and Biotechnology, Chungnam National University, Gung-dong 220, Yuseong-gu, Daejeon 305-764, Korea.
Yun-Hee Park
Hee-Moon Park

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Disruption of the fission yeast LAMMER kinase, Lkh1, gene resulted in diverse phenotypes, including adhesive filamentous growth and oxidative stress sensitivity, but an exact cellular function had not been assigned to Lkh1. Through an in vitro pull-down approach, a transcriptional repressor, Tup12, was identified as an Lkh1 binding partner. Interactions between Lkh1 and Tup11 or Tup12 were confirmed by in vitro and in vivo binding assays. Tup proteins were phosphorylated by Lkh1 in a LAMMER motif-dependent manner. The LAMMER motif was also necessary for substrate recognition in vitro and cellular function in vivo. Transcriptional activity assays using promoters negatively regulated by Tup11 and Tup12 showed 6 or 2 times higher activity in the Delta lkh1 mutant than the wild type, respectively. Northern analysis revealed derepressed expression of the fbp1(+) mRNA in Delta lkh1 and in Delta tup11 Delta tup12 mutant cells under repressed conditions. Delta lkh1 and Delta tup11 Delta tup12 mutant cells showed flocculation, which was reversed by co-expression of Tup11 and -12 with Ssn6. Here, we presented a new aspect of the LAMMER kinase by demonstrating that the activities of global transcriptional repressors, Tup11 and Tup12, were positively regulated by Lkh1-mediated phosphorylation.

Indexed as

Amino Acid MotifsGene DeletionPhosphorylationPromoter Regions, GeneticProtein BindingProtein KinasesRepressor ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsTranscription, Geneticlkh1 protein, S pombeProtein KinasesRepressor ProteinsSchizosaccharomyces pombe ProteinsTup11 protein, S pombeTup12 protein, S pombe

Identifiers

PMID20200159
PMCPMC2859543

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Registered trials

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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.