Evidence map›Paper›PMID 22065639›Full record

ArticleThe Journal of cell biology2011

Cdk1 phosphorylation of the kinetochore protein Nsk1 prevents error-prone chromosome segregation.

Jun-Song Chen, Lucy X Lu, Melanie D Ohi, Kevin M Creamer, Chauca English, Janet F Partridge, Ryoma Ohi, Kathleen L Gould

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. The Effect ofLife (Basel, Switzerland) · 2025
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  3. ThemicroPublication biology · 2025
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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 4 institutions in 1 country.

Jun-Song ChenHoward Hughes Medical Institute, Vanderbilt University School of Medicine, Nashville, TN 37212, USA.
Lucy X Lu
Melanie D Ohi
Kevin M Creamer
Chauca English
Janet F Partridge
Ryoma Ohi
Kathleen L Gould
Vanderbilt University · USHoward Hughes Medical Institute · USSt. Jude Children's Research Hospital · USUniversity of Tennessee Health Science Center · US

Funding

Viral Vector Technology (VVTSR)P30CA021765 · NCI · ST. JUDE CHILDREN'S RESEARCH HOSPITAL · PI CHARLES ROBERTS · 1985 to 2026
$166.9M
Regulation of microtubule dynamics during cell divisionR01GM086610 · NIGMS · VANDERBILT UNIVERSITY · PI OHI, RYOMA · 2010 to 2023
$4.5M
Regulation anf Function of Clp 1p Protein PhosphataseR01GM068786 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MCCOLLUM, DANNEL · 2003 to 2010
$2.3M
Multifaceted Approaches for Studying the Structure and Function of SpliceosomesDP2OD004483 · OD · VANDERBILT UNIVERSITY · PI OHI, MELANIE DIANE · 2008 to 2008
$2.3M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA021765NCI NIH HHS P30CA021765NIGMS NIH HHS GM068786NIGMS NIH HHS R01 GM068786NIGMS NIH HHS R01 GM086610NIGMS NIH HHS R01GM086610NIH HHS 1DP2OD004483NIH HHS DP2 OD004483
6 · The paper itself

Abstract

Cdk1 controls many aspects of mitotic chromosome behavior and spindle microtubule (MT) dynamics to ensure accurate chromosome segregation. In this paper, we characterize a new kinetochore substrate of fission yeast Cdk1, Nsk1, which promotes proper kinetochore-MT (k-MT) interactions and chromosome movements in a phosphoregulated manner. Cdk1 phosphorylation of Nsk1 antagonizes Nsk1 kinetochore and spindle localization during early mitosis. A nonphosphorylatable Nsk1 mutant binds prematurely to kinetochores and spindle, cementing improper k-MT attachments and leading to high rates of lagging chromosomes that missegregate. Accordingly, cells lacking nsk1 exhibit synthetic growth defects with mutations that disturb MT dynamics and/or kinetochore structure, and lack of proper phosphoregulation leads to even more severe defects. Intriguingly, Nsk1 is stabilized by binding directly to the dynein light chain Dlc1 independently of the dynein motor, and Nsk1-Dlc1 forms chainlike structures in vitro. Our findings establish new roles for Cdk1 and the Nsk1-Dlc1 complex in regulating the k-MT interface and chromosome segregation.

Indexed as

Chromosome SegregationCDC2 Protein KinaseCell Cycle ProteinsChromosomes, FungalDyneinsKinetochoresMicrotubulesMitosisPhosphorylationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpindle ApparatusCDC2 Protein KinaseCell Cycle ProteinsDyneinsNsk1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID22065639
PMCPMC3257533
OpenAlexW2153655604

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.