Evidence map›Paper›PMID 18922800›Full record

ArticleThe Journal of biological chemistry2008

Requirements for protein phosphorylation and the kinase activity of polo-like kinase 1 (Plk1) for the kinetochore function of mitotic arrest deficiency protein 1 (Mad1).

Ya-Hui Chi, Kerstin Haller, Michael D Ward, O John Semmes, Yan Li, Kuan-Teh Jeang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. MAD1: Kinetochore Receptors and Catalytic Mechanisms.Frontiers in cell and developmental biology · 2018
    Review
  5. Article
  6. Article
  7. Structure of human Mad1 C-terminal domain reveals its involvement in kinetochore targeting.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  8. Article
  9. Article
  10. Review
  11. The nuclear envelopathies and human diseases.Journal of biomedical science · 2009
    Review
  12. Viral transformation and aneuploidy.Environmental and molecular mutagenesis · 2009
    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

6 authors at 3 institutions in 1 country.

Ya-Hui ChiMolecular Virology Section, Laboratory of Molecular Microbiology, NIAID, National Institutes of Health, Bethesda, Maryland 20892, USA.
Kerstin Haller
Michael D Ward
O John Semmes
Yan Li
Kuan-Teh Jeang
Eastern Virginia Medical School · USNational Institute of Allergy and Infectious Diseases · USNational Institutes of Health · US

Funding

Mechanisms of Cellular Transformation by HTLV-1ZIAAI001023 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI JEANG, KUAN-TEH · 2009 to 2013
$4.2M
HTLV-I TAX MEDIATED DEREGULATION OF CELL STATER01CA076595 · NCI · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI SEMMES, OLIVER JOHN · 1999 to 2016
$2.9M
NCI NIH HHS R01 CA076595
6 · The paper itself

Abstract

Mitotic arrest deficiency protein 1 (Mad1) is associated with microtubule-unattached kinetochores in mitotic cells and is a component of the spindle assembly checkpoint (SAC). Here, we have studied the phosphorylation of Mad1 and mapped using liquid chromatography-tandem mass spectrometry several phosphorylated amino acids in this protein. One phosphorylated residue, Thr680, was characterized to be important for the kinetochore localization of Mad1 and its SAC function. We also found that in mitotic cells Mad1 co-immunoprecipitated with Plk1. Depletion of cellular Plk1 using small interfering RNAs and inhibition of the kinase activity of Plk1 using a kinase-dead mutant or a small molecule inhibitor attenuated Mad1 phosphorylation and its association with kinetochores. Collectively, these findings indicate mechanistic roles contributed by protein phosphorylation and Plk1 to the SAC activity of Mad1.

Indexed as

Cell Cycle ProteinsChromatography, LiquidHeLa CellsHumansKinetochoresMass ScreeningMitosisNuclear ProteinsPhosphorylationPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, Small InterferingCell Cycle ProteinsMAD1L1 protein, humanNuclear ProteinsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNA, Small Interfering

Identifiers

PMID18922800
PMCPMC2602915
OpenAlexW2019188180

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.