Evidence map›Paper›PMID 23455152›Full record

ArticleThe EMBO journal2013

Dynactin helps target Polo-like kinase 1 to kinetochores via its left-handed beta-helical p27 subunit.

Ting-Yu Yeh, Anna K Kowalska, Brett R Scipioni, Frances Ka Yan Cheong, Meiying Zheng, Urszula Derewenda, Zygmunt S Derewenda, Trina A Schroer

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.9field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

8 authors at 2 institutions in 1 country.

Ting-Yu YehDepartment of Biology, Johns Hopkins University, Baltimore, MD, USA.
Anna K Kowalska
Brett R Scipioni
Frances Ka Yan Cheong
Meiying Zheng
Urszula Derewenda
Zygmunt S Derewenda
Trina A Schroer
Johns Hopkins University · USUniversity of Virginia · US

Funding

Women's Oncology Program - WONP30CA044579 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI Thomas P. Loughran · 1987 to 2026
$72.1M
CELLULAR AND MOLECULAR BIOLOGYT32GM007231 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI VAN DOREN, MARK B · 1985 to 2020
$18.4M
REGULATION OF CYTOPLASMIC DYNEIN-BASED VESICLE TRANSPORTR01GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 1990 to 2012
$4.3M
Molecular Mechanisms of Neuronal MigrationsR01NS036267 · NINDS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI DEREWENDA, ZYGMUNT S · 1998 to 2011
$3.4M
Regulation of Cytoplasmic Dynein Based Vesicle TransportR56GM044589 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SCHROER, TRINA A · 2008 to 2008
$410k
NCI NIH HHS P30 CA044579NIGMS NIH HHS GM044589NIGMS NIH HHS R01 GM044589NIGMS NIH HHS R56 GM044589NIGMS NIH HHS T32 GM007231NIGMS NIH HHS T32 GM07231NINDS NIH HHS NS036267NINDS NIH HHS R01 NS036267
6 · The paper itself

Abstract

Dynactin is a protein complex required for the in vivo function of cytoplasmic dynein, a microtubule (MT)-based motor. Dynactin binds both dynein and MTs via its p150(Glued) subunit, but little is known about the 'pointed-end complex' that includes the protein subunits Arp11, p62 and the p27/p25 heterodimer. Here, we show that the p27/p25 heterodimer undergoes mitotic phosphorylation by cyclin-dependent kinase 1 (Cdk1) at a single site, p27 Thr186, to generate an anchoring site for polo-like kinase 1 (Plk1) at kinetochores. Removal of p27/p25 from dynactin results in reduced levels of Plk1 and its phosphorylated substrates at kinetochores in prometaphase, which correlates with aberrant kinetochore-MT interactions, improper chromosome alignment and abbreviated mitosis. To investigate the structural implications of p27 phosphorylation, we determined the structure of human p27. This revealed an unusual left-handed β-helix domain, with the phosphorylation site located within a disordered, C-terminal segment. We conclude that dynactin plays a previously undescribed regulatory role in the spindle assembly checkpoint by recruiting Plk1 to kinetochores and facilitating phosphorylation of important downstream targets.

Indexed as

AnimalsCattleCell Cycle ProteinsCell LineChick EmbryoDynactin ComplexHumansKinetochoresMiceMicrotubule-Associated ProteinsMicrotubulesPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProtein Structure, TertiaryProtein SubunitsCell Cycle ProteinsDCTN1 protein, humanDctn1 protein, mouseDynactin ComplexMicrotubule-Associated ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProtein SubunitsProto-Oncogene Proteins

Identifiers

PMID23455152
PMCPMC3616283
OpenAlexW2073028067

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.