Evidence map›Paper›PMID 29263426›Full record

ArticleNature communications2017

Whole proteome analysis of human tankyrase knockout cells reveals targets of tankyrase-mediated degradation.

Amit Bhardwaj, Yanling Yang, Beatrix Ueberheide, Susan Smith

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

63 citing papers in PubMed, 106 citations in OpenAlex.

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  19. Tankyrase: a promising therapeutic target with pleiotropic action.Naunyn-Schmiedeberg's archives of pharmacology · 2023
    Review
  20. Article

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

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

4 authors at 1 institution in 1 country.

Amit BhardwajKimmel Center for Biology and Medicine at the Skirball Institute, Department of Pathology, New York University School of Medicine, New York, NY, 10016, USA.
Yanling YangProteomics Laboratory, Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, 10016, USA.
Beatrix UeberheideProteomics Laboratory, Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, 10016, USA.
Susan SmithKimmel Center for Biology and Medicine at the Skirball Institute, Department of Pathology, New York University School of Medicine, New York, NY, 10016, USA. susan.smith@med.nyu.edu.
New York University · US

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
Mechanisms of Sister Telomere Cohesion and ResolutionR01CA116352 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SMITH, SUSAN · 2007 to 2016
$3.1M
NCI NIH HHS P30 CA016087NIH HHS 1S10OD010582-01A1NIH HHS R01CA116352
6 · The paper itself

Abstract

Tankyrase 1 and 2 are poly(ADP-ribose) polymerases that function in pathways critical to cancer cell growth. Tankyrase-mediated PARylation marks protein targets for proteasomal degradation. Here, we generate human knockout cell lines to examine cell function and interrogate the proteome. We show that either tankyrase 1 or 2 is sufficient to maintain telomere length, but both are required to resolve telomere cohesion and maintain mitotic spindle integrity. Quantitative analysis of the proteome of tankyrase double knockout cells using isobaric tandem mass tags reveals targets of degradation, including antagonists of the Wnt/β-catenin signaling pathway (NKD1, NKD2, and HectD1) and three (Notch 1, 2, and 3) of the four Notch receptors. We show that tankyrases are required for Notch2 to exit the plasma membrane and enter the nucleus to activate transcription. Considering that Notch signaling is commonly activated in cancer, tankyrase inhibitors may have therapeutic potential in targeting this pathway.

Indexed as

Adaptor Proteins, Signal TransducingCalcium-Binding ProteinsCarrier ProteinsCell LineGene Knockout TechniquesHumansProteasome Endopeptidase ComplexProteomeProteomicsReceptor, Notch1Receptor, Notch2Receptor, Notch3Spindle ApparatusTankyrasesTelomere HomeostasisUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingCalcium-Binding ProteinsCarrier ProteinsHECTD1 protein, humanNKD1 protein, humanNKD2 protein, humanNOTCH1 protein, humanNOTCH2 protein, humanNOTCH3 protein, humanProteasome Endopeptidase ComplexProteomeReceptor, Notch1Receptor, Notch2Receptor, Notch3TankyrasesTNKS2 protein, humanTNKS protein, humanUbiquitin-Protein Ligases

Identifiers

PMID29263426
PMCPMC5738441
OpenAlexW2771937306

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.