Evidence map›Paper›PMID 24942739›Full record

ArticleThe Journal of biological chemistry2014

The nuclear localization of γ-tubulin is regulated by SadB-mediated phosphorylation.

Greta Eklund, Stefan Lang, Johan Glindre, Åsa Ehlén, Maria Alvarado-Kristensson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
1.1field-weighted citation impact, top 26% 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, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Targeting TUBG1 in RB1-negative tumors.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  5. Article
  6. Centrosome Movements Are TUBG1-Dependent.International journal of molecular sciences · 2023
    Article
  7. Review
  8. γ-Tubulin in microtubule nucleation and beyond.Frontiers in cell and developmental biology · 2022
    Review
  9. Article
  10. Review
  11. Targeting cytoskeletal phosphorylation in cancer.Exploration of targeted anti-tumor therapy · 2021
    Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  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

5 authors at 1 institution in 1 country.

Greta EklundFrom the Division of Molecular Pathology, Department of Laboratory Medicine, Lund University, Skåne University Hospital, SE-20502 Malmö, Sweden.
Stefan LangFrom the Division of Molecular Pathology, Department of Laboratory Medicine, Lund University, Skåne University Hospital, SE-20502 Malmö, Sweden.
Johan GlindreFrom the Division of Molecular Pathology, Department of Laboratory Medicine, Lund University, Skåne University Hospital, SE-20502 Malmö, Sweden.
Åsa EhlénFrom the Division of Molecular Pathology, Department of Laboratory Medicine, Lund University, Skåne University Hospital, SE-20502 Malmö, Sweden.
Maria Alvarado-KristenssonFrom the Division of Molecular Pathology, Department of Laboratory Medicine, Lund University, Skåne University Hospital, SE-20502 Malmö, Sweden maria.alvarado-kristensson@med.lu.se.
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

γ-Tubulin is an important cell division regulator that arranges microtubule assembly and mitotic spindle formation. Cytosolic γ-tubulin nucleates α- and β-tubulin in a growing microtubule by forming the ring-shaped protein complex γTuRC. Nuclear γ-tubulin also regulates S-phase progression by moderating the activities of E2 promoter-binding factors. The mechanism that regulates localization of γ-tubulin is currently unknown. Here, we demonstrate that the human Ser/Thr kinase SadB short localizes to chromatin and centrosomes. We found that SadB-mediated phosphorylation of γ-tubulin on Ser(385) formed chromatin-associated γ-tubulin complexes that moderate gene expression. In this way, the C-terminal region of γ-tubulin regulates S-phase progression. In addition, chromatin levels of γ-tubulin were decreased by the reduction of SadB levels or expression of a non-phosphorylatable Ala(385)-γ-tubulin but were enhanced by expression of SadB, wild-type γ-tubulin, or a phosphomimetic Asp(385)-γ-tubulin mutant. Our results demonstrate that SadB kinases regulate the cellular localization of γ-tubulin and thereby control S-phase progression.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCell Line, TumorCell NucleusDNA PrimersGene ExpressionHumansMiceMolecular Sequence DataNIH 3T3 CellsPhosphorylationPolymerase Chain ReactionProtein KinasesSequence Homology, Amino AcidTubulinDNA PrimersProtein KinasesTubulinCell CycleCentrosomeNucleusPhosphorylationTubulin

Identifiers

PMID24942739
PMCPMC4118101
OpenAlexW2051672408

What OpenQuestion holds

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LicenceCC BY
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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.