Evidence map›Paper›PMID 18769144›Full record

ArticleCell cycle (Georgetown, Tex.)2008

ATM kinase is a master switch for the Delta Np63 alpha phosphorylation/degradation in human head and neck squamous cell carcinoma cells upon DNA damage.

Yiping Huang, Tanusree Sen, Jatin Nagpal, Sunil Upadhyay, Barry Trink, Edward Ratovitski, David Sidransky

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

37 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. The dual role of p63 in cancer.Frontiers in oncology · 2023
    Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. p63-related signaling at a glance.Journal of cell science · 2020
    Review
  10. Article
  11. Article
  12. IL-1β Inflammatory Cytokine-InducedInternational journal of molecular sciences · 2019
    Article
  13. Article
  14. Article
  15. The Regulation of Tumor Suppressor p63 by the Ubiquitin-Proteasome System.International journal of molecular sciences · 2016
    Review
  16. PMS2 expression in epithelial ovarian cancer is posttranslationally regulated by Akt and essential for platinum-induced apoptosis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  17. Review
  18. Article
  19. Article
  20. Article
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

7 authors at 1 institution in 1 country.

Yiping HuangDepartment of Dermatology, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21231, USA.
Tanusree Sen
Jatin Nagpal
Sunil Upadhyay
Barry Trink
Edward Ratovitski
David Sidransky
Johns Hopkins University · US

Funding

The Role of P40 in Squamous Cell CarcinomasR01DE013561 · NIDCR · JOHNS HOPKINS UNIVERSITY · PI SIDRANSKY, DAVID · 2000 to 2009
$2.8M
NIDCR NIH HHS R01 DE013561
6 · The paper itself

Abstract

We previously found that the pro-apoptotic DNA damaging agent, cisplatin, mediated the proteasome-dependent degradation of Delta Np63 alpha associated with its increased phosphorylated status. Since Delta Np63 alpha usually plays an opposite role to p53 and TAp63 in human cancers, we tested the notion that phosphorylation events induced by DNA damage would affect the protein degradation of Delta Np63 alpha in HNSCC cells upon cisplatin exposure. We found that Delta Np63 alpha is phosphorylated in the time-dependent fashion at the following positions: S385, T397 and S466, which were surrounded by recognition motifs for ATM, CDK2 and p70s6K kinases, respectively. We showed that chemical agents or siRNA inhibiting the activity of ATM, CDK2 and p70s6K kinases blocked degradation of Delta Np63 alpha in HNSCC cells after cisplatin exposure. Site-specific mutagenesis of Delta Np63 alpha residues targeted for phosphorylation by ATM, CDK2 or p70s6k led to dramatic modulation of Delta Np63 alpha degradation. Finally, we demonstrated that the Delta Np63 alpha protein is a target for direct in vitro phosphorylation by ATM, CDK2 or p70s6K. Our results implicate specific kinases, and target phosphorylation sites in the degradation of Delta Np63 alpha following DNA damage.

Indexed as

DNA DamageProtein Processing, Post-TranslationalAmino Acid MotifsAmino Acid SequenceAtaxia Telangiectasia Mutated ProteinsCarcinoma, Squamous CellCell Cycle ProteinsCell Line, TumorCisplatinCyclin-Dependent Kinase 2DNA-Binding ProteinsHead and Neck NeoplasmsHumansMolecular Sequence DataMutationPhosphorylationAtaxia Telangiectasia Mutated ProteinsATM protein, humanCDK2 protein, humanCell Cycle ProteinsCisplatinCyclin-Dependent Kinase 2DNA-Binding ProteinsPhosphoserinePhosphothreonineProtein Kinase InhibitorsProtein Serine-Threonine KinasesRibosomal Protein S6 Kinases, 70-kDaRNA, Small InterferingTP63 protein, humanTrans-ActivatorsTranscription FactorsTumor Suppressor Proteins

Identifiers

PMID18769144
PMCPMC3069617
OpenAlexW2012518641

What OpenQuestion holds

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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.