Evidence map›Paper›PMID 18287541›Full record

ArticleMolecular biology of the cell2008

Ste20-related protein kinase LOSK (SLK) controls microtubule radial array in interphase.

Anton V Burakov, Olga N Zhapparova, Olga V Kovalenko, Liudmila A Zinovkina, Ekaterina S Potekhina, Nina A Shanina, Dieter G Weiss, Sergei A Kuznetsov, Elena S Nadezhdina

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In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  9. Activity of the Ste20-like kinase, SLK, is enhanced by homodimerization.American journal of physiology. Renal physiology · 2011
    Article
  10. Article
  11. Review
  12. Article
  13. The mammalian family of sterile 20p-like protein kinases.Pflugers Archiv : European journal of physiology · 2009
    Review
  14. Article
  15. LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylation.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  16. Review
  17. 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

9 authors at 4 institutions in 2 countries.

Anton V BurakovInstitute of Protein Research, Russian Academy of Science, 142290 Pushchino, Moscow Region, Russian Federation.
Olga N Zhapparova
Olga V Kovalenko
Liudmila A Zinovkina
Ekaterina S Potekhina
Nina A Shanina
Dieter G Weiss
Sergei A Kuznetsov
Elena S Nadezhdina
Physico-Technical Institute · RULomonosov Moscow State University · RUUniversity of Rostock · DEInstitute of Protein Research · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interphase microtubules are organized into a radial array with centrosome in the center. This organization is a subject of cellular regulation that can be driven by protein phosphorylation. Only few protein kinases that regulate microtubule array in interphase cells have been described. Ste20-like protein kinase LOSK (SLK) was identified as a microtubule and centrosome-associated protein. In this study we have shown that the inhibition of LOSK activity by dominant-negative mutant K63R-DeltaT or by LOSK depletion with RNAi leads to unfocused microtubule arrangement. Microtubule disorganization is prominent in Vero, CV-1, and CHO-K1 cells but less distinct in HeLa cells. The effect is a result neither of microtubule stabilization nor of centrosome disruption. In cells with suppressed LOSK activity centrosomes are unable to anchor or to cap microtubules, though they keep nucleating microtubules. These centrosomes are depleted of dynactin. Vero cells overexpressing K63R-DeltaT have normal dynactin "comets" at microtubule ends and unaltered morphology of Golgi complex but are unable to polarize it at the wound edge. We conclude that protein kinase LOSK is required for radial microtubule organization and for the proper localization of Golgi complex in various cell types.

Indexed as

InterphaseAnimalsCatalytic DomainCell LineCell PolarityCentrosomeDiffusionGenes, DominantGolgi ApparatusHippo KinasesHumansMicrotubulesMutant ProteinsPeptide FragmentsProtein BindingProtein Serine-Threonine KinasesHippo KinasesMutant ProteinsPeptide FragmentsProtein Serine-Threonine KinasesSLK protein, human

Identifiers

PMID18287541
PMCPMC2366846
OpenAlexW2165163773

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.