Evidence map›Paper›PMID 20231380›Full record

ArticleThe Journal of cell biology2010

Regulated targeting of protein phosphatase 1 to the outer kinetochore by KNL1 opposes Aurora B kinase.

Dan Liu, Mathijs Vleugel, Chelsea B Backer, Tetsuya Hori, Tatsuo Fukagawa, Iain M Cheeseman, Michael A Lampson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 225 papers.

0numbers the graph read from it
0cells of the map it votes in
225citing papers in PubMed
15.7field-weighted citation impact, top 1% 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

225 citing papers in PubMed, 378 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Science advances · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. A coadapted KNL1 and spindle assembly checkpoint axis orchestrates precise mitosis in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Review
  18. Article
  19. Modeling specific aneuploidies: from karyotype manipulations to biological insights.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023
    Review
  20. Review

165 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 2 countries.

Dan LiuDepartment of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
Mathijs Vleugel
Chelsea B Backer
Tetsuya Hori
Tatsuo Fukagawa
Iain M Cheeseman
Michael A Lampson
Massachusetts Institute of Technology · USUniversity of Pennsylvania · USNational Institute of Genetics · JPThe Graduate University for Advanced Studies, SOKENDAI · JP

Funding

Molecular Analysis of the Kinetochore-Microtubule InterfaceR01GM088313 · NIGMS · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI CHEESEMAN, IAIN MCPHERSON · 2009 to 2017
$3.6M
Regulation of cell division by mitotic kinasesR01GM083988 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GRISHCHUK, EKATERINA L, LAMPSON, MICHAEL · 2008 to 2017
$3.2M
NIGMS NIH HHS GM083988NIGMS NIH HHS GM088313NIGMS NIH HHS R01 GM083988NIGMS NIH HHS R01 GM088313
6 · The paper itself

Abstract

Regulated interactions between kinetochores and spindle microtubules are essential to maintain genomic stability during chromosome segregation. The Aurora B kinase phosphorylates kinetochore substrates to destabilize kinetochore-microtubule interactions and eliminate incorrect attachments. These substrates must be dephosphorylated to stabilize correct attachments, but how opposing kinase and phosphatase activities are coordinated at the kinetochore is unknown. Here, we demonstrate that a conserved motif in the kinetochore protein KNL1 directly interacts with and targets protein phosphatase 1 (PP1) to the outer kinetochore. PP1 recruitment by KNL1 is required to dephosphorylate Aurora B substrates at kinetochores and stabilize microtubule attachments. PP1 levels at kinetochores are regulated and inversely proportional to local Aurora B activity. Indeed, we demonstrate that phosphorylation of KNL1 by Aurora B disrupts the KNL1-PP1 interaction. In total, our results support a positive feedback mechanism by which Aurora B activity at kinetochores not only targets substrates directly, but also prevents localization of the opposing phosphatase.

Indexed as

Amino Acid MotifsAmino Acid SequenceAurora Kinase BAurora KinasesConserved SequenceHeLa CellsHumansMicrotubule-Associated ProteinsPhosphorylationProtein Phosphatase 1Protein Serine-Threonine KinasesRecombinant ProteinsSequence AlignmentAURKB protein, humanAurora Kinase BAurora KinasesKnl1 protein, humanMicrotubule-Associated ProteinsProtein Phosphatase 1Protein Serine-Threonine KinasesRecombinant Proteins

Identifiers

PMID20231380
PMCPMC2845083
OpenAlexW2156091753

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.