Evidence map›Paper›PMID 22735455›Full record

ArticleNature communications2012

Protein L-isoaspartyl methyltransferase regulates p53 activity.

Jae-Cheol Lee, Sung-Ung Kang, Yeji Jeon, Jong Woo Park, Jueng-Soo You, Shin-Won Ha, Narkhyun Bae, Gert Lubec, So Hee Kwon, Ju-Seog Lee and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

38 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Repair of Isoaspartyl Residues by PCMT1 and Kidney Fibrosis.Journal of the American Society of Nephrology : JASN · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. DNA Double-Strand Breaks as Pathogenic Lesions in Neurological Disorders.International journal of molecular sciences · 2022
    Review
  16. Article
  17. Article
  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

12 authors at 3 institutions in 3 countries.

Jae-Cheol LeeResearch Center for Epigenome Regulation, School of Pharmacy, Sungkyunkwan University, Suwon 440-746, Republic of Korea.
Sung-Ung Kang
Yeji Jeon
Jong Woo Park
Jueng-Soo You
Shin-Won Ha
Narkhyun Bae
Gert Lubec
So Hee Kwon
Ju-Seog Lee
Eun-Jung Cho
Jeung-Whan Han
Sungkyunkwan University · KRMedical University of Vienna · ATYonsei University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein methylation plays important roles in most, if not all, cellular processes. Lysine and arginine methyltransferases are known to regulate the function of histones and non-histone proteins through the methylation of specific sites. However, the role of the carboxyl-methyltransferase protein L-isoaspartyl methyltransferase (PIMT) in the regulation of protein functions is relatively less understood. Here we show that PIMT negatively regulates the tumour suppressor protein p53 by reducing p53 protein levels, thereby suppressing the p53-mediated transcription of target genes. In addition, PIMT depletion upregulates the proapoptotic and checkpoint activation functions of p53. Moreover, PIMT destabilizes p53 by enhancing the p53-HDM2 interaction. These PIMT effects on p53 stability and activity are attributed to the PIMT-mediated methylation of p53 at isoaspartate residues 29 and 30. Our study provides new insight into the molecular mechanisms by which PIMT suppresses the p53 activity through carboxyl methylation, and suggests a therapeutic target for cancers.

Indexed as

Cell Line, TumorChromatin ImmunoprecipitationFlow CytometryHumansImmunoblottingImmunoprecipitationProtein BindingProtein D-Aspartate-L-Isoaspartate MethyltransferaseReal-Time Polymerase Chain ReactionTandem Mass SpectrometryTumor Suppressor Protein p53Protein D-Aspartate-L-Isoaspartate MethyltransferaseTumor Suppressor Protein p53

Identifiers

PMID22735455
PMCPMC3621463
OpenAlexW2072787000

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.