Evidence map›Paper›PMID 16767160›Full record

ArticleOncogene2006

Regulation of SV40 large T-antigen stability by reversible acetylation.

T Shimazu, Y Komatsu, K I Nakayama, H Fukazawa, S Horinouchi, M Yoshida

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

21 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  7. Viral epigenetics.Methods in molecular biology (Clifton, N.J.) · 2015
    Review
  8. Article
  9. Article
  10. Acetylation and deacetylation--novel factors in muscle wasting.Metabolism: clinical and experimental · 2013
    Review
  11. Article
  12. Regulation of inositol 1,3,4-trisphosphate 5/6-kinase (ITPK1) by reversible lysine acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  13. Nonhistone protein acetylation as cancer therapy targets.Expert review of anticancer therapy · 2010
    Review
  14. Article
  15. Article
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

6 authors at 5 institutions in 1 country.

T ShimazuChemical Genetics Laboratory, RIKEN, Hirosawa 2-1, Wako, Saitama, Japan.
Y Komatsu
K I Nakayama
H Fukazawa
S Horinouchi
M Yoshida
Japan Science and Technology Agency · JPAdvanced Life Science Institute · JPNational Institute of Infectious Diseases · JPRIKEN · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Reversible acetylation on protein lysine residues has been shown to regulate the function of both nuclear proteins such as histones and p53 and cytoplasmic proteins such as alpha-tubulin. To identify novel acetylated proteins, we purified several proteins by the affinity to an anti-acetylated-lysine antibody from cells treated with trichostatin A (TSA). Among the proteins identified, here we report acetylation of the SV40 large T antigen (T-Ag). The acetylation site was determined to be lysine-697, which is located adjacent to the C-terminal Cdc4 phospho-degron (CPD). Overexpression of the CBP acetyltransferase acetylated T-Ag, whereas HDAC1, HDAC3 and SIRT1 bound and deacetylated T-Ag. The acetylation and deacetylation occurred independently of p53, a binding partner of T-Ag, but the acetylation was enhanced in the presence of p53. T-Ag in the cells treated with TSA and NA or the acetylation mimic mutant (K697Q) became unstable in COS-7 cells, suggesting that acetylation regulates stability of T-Ag. Indeed, NIH3T3 cells stably expressing K697Q showed decreased anchorage-independent growth compared with those expressing wild type or the K697R mutant. These results demonstrate that acetylation destabilizes T-Ag and regulates the transforming activity of T-Ag in NIH3T3 cells.

Indexed as

AcetylationAmino Acid SequenceAnimalsAntigens, Polyomavirus TransformingBase SequenceChlorocebus aethiopsChromatography, High Pressure LiquidCOS CellsDNA PrimersHistone DeacetylasesMiceMolecular Sequence DataSirtuin 1SirtuinsSpectrometry, Mass, Electrospray IonizationAntigens, Polyomavirus TransformingDNA PrimersHistone DeacetylasesSIRT1 protein, humanSirtuin 1Sirtuins

Identifiers

PMID16767160
OpenAlexW2121168046

What Socratic 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 Socratic graph.