Evidence map›Paper›PMID 16076287›Full record

ArticleThe Biochemical journal2005

NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis.

William Chang, Jasmin N Dynek, Susan Smith

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

83 citing papers in PubMed, 143 citations in OpenAlex.

  1. Review
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  13. Review
  14. Tankyrase: a promising therapeutic target with pleiotropic action.Naunyn-Schmiedeberg's archives of pharmacology · 2023
    Review
  15. Article
  16. Review
  17. Article
  18. Article
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23 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

William ChangSkirball Institute of Biomolecular Medicine, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.
Jasmin N Dynek
Susan Smith
New York University · US

Funding

Mechanisms of Telomere FunctionR01CA095099 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SMITH, SUSAN · 2002 to 2014
$3.2M
GRADUATE PROGRAM IN CELLULAR &MOLECULAR BIOLOGYT32GM007238 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI RIFKIN, DANIEL B · 1985 to 2013
$2.7M
NCI NIH HHS R01 CA095099NCI NIH HHS R01 CA95099NIGMS NIH HHS GM07238NIGMS NIH HHS T32 GM007238
6 · The paper itself

Abstract

Tankyrase 1 is a PARP [poly(ADP-ribose) polymerase] that localizes to multiple subcellular sites, including telomeres and mitotic centrosomes. Previous studies demonstrated that cells deficient in tankyrase 1 suffered a block in resolution of sister telomeres and arrested in early anaphase [Dynek and Smith (2004) Science 304, 97-100]. This phenotype was dependent on the catalytic PARP activity of tankyrase 1. To identify critical acceptors of PARsylation [poly(ADP-ribosyl)ation] by tankyrase 1 in mitosis, tankyrase 1 immunoprecipitates were analysed for associated PARsylated proteins. We identified NuMA (nuclear mitotic apparatus protein) as a major acceptor of poly(ADP-ribose) from tankyrase 1 in mitosis. We showed by immunofluorescence and immunoprecipitation that association between tankyrase 1 and NuMA increases dramatically at the onset of mitosis, concomitant with PARsylation of NuMA. Knockdown of tankyrase 1 by siRNA (small interfering RNA) eliminates PARsylation of NuMA in mitosis, confirming tankyrase 1 as the PARP responsible for this modification. However, even in the absence of tankyrase 1 and PARsylation, NuMA localizes to spindle poles. By contrast, siRNA knockdown of NuMA results in complete loss of tankyrase 1 from spindle poles. We discuss our result in terms of a model where PARsylation of NuMA by tankyrase 1 in mitosis could play a role in sister telomere separation and/or mitotic progression.

Indexed as

MitosisAntigens, NuclearCell Cycle ProteinsGene Expression Regulation, EnzymologicHeLa CellsHumansNuclear Matrix-Associated ProteinsNuclear ProteinsPhosphorylationPoly Adenosine Diphosphate RiboseProtein BindingRNA InterferenceSpindle ApparatusTankyrasesAntigens, NuclearCell Cycle ProteinsNuclear Matrix-Associated ProteinsNuclear ProteinsNUMA1 protein, humanPoly Adenosine Diphosphate RiboseTankyrasesTNKS protein, human

Identifiers

PMID16076287
PMCPMC1276914
OpenAlexW2094343813

What OpenQuestion holds

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Registered trials

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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.