Evidence map›Paper›PMID 19150978›Full record

ArticleThe Journal of biological chemistry2009

PML3 Orchestrates the Nuclear Dynamics and Function of TIP60.

Quan Wu, Haixiang Hu, Jianping Lan, Chibuzo Emenari, Zhiyong Wang, Kang-Sang Chang, He Huang, Xuebiao Yao

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  4. Review
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  9. Article
  10. MOZ increases p53 acetylation and premature senescence through its complex formation with PML.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  11. Connecting chromatin modifying factors to DNA damage response.International journal of molecular sciences · 2013
    Article
  12. Differential Roles of PML Isoforms.Frontiers in oncology · 2013
    Article
  13. Article
  14. Article
  15. Article
  16. 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

8 authors at 6 institutions in 2 countries.

Quan WuAnhui Key Laboratory for Cellular Dynamics and Chemical Biology and National Laboratory for Physical Sciences at Nanoscale, Hefei 230027, China.
Haixiang Hu
Jianping Lan
Chibuzo Emenari
Zhiyong Wang
Kang-Sang Chang
He Huang
Xuebiao Yao
Hefei National Center for Physical Sciences at Nanoscale · CNMorehouse School of Medicine · USAir Force General Hospital PLA · CNThe University of Texas MD Anderson Cancer Center · USZhejiang Provincial People's Hospital · CNZhejiang University · CN

Funding

TRANSCRIPTION FACTORS AND PROSTATE CANCERG12RR003034 · NCRR · MOREHOUSE SCHOOL OF MEDICINE · PI ZHAO, XUEYING · 1986 to 2011
$32.4M
TRAINING AND CAREER DEVELOPMENTU54CA118948 · NCI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Timiya S Nolan · 2005 to 2026
$26.6M
Atlanta Clinical and Translational Science Institute (ACTSI) RenewalUL1TR000454 · NCATS · EMORY UNIVERSITY · PI STEPHENS, DAVID S · 2012 to 2016
$25.8M
The function of ezrin in stimulus-coupled acid secretionR01DK056292 · NIDDK · UNIVERSITY OF WISCONSIN MADISON · PI YAO, XUEBIAO · 1999 to 2012
$2.5M
NCATS NIH HHS UL1 TR000454NCI NIH HHS CA118948NCI NIH HHS CA92080NCRR NIH HHS G-12-RR03034NIDDK NIH HHS DK56292
6 · The paper itself

Abstract

The promyelocytic leukemia (PML) protein is a major component to govern the PML nuclear body (NB) assembly and function. Although it is well defined that PML NB is a site recruiting sumoylated proteins, the mechanism by which PML protein regulates the process remains unclear. Here we show that PML3, a specific PML isoform, interacts with and recruits TIP60 to PML NBs. Our biochemical characterization demonstrates that PML3 physically interacts with TIP60 via its N-terminal 364 amino acids. Importantly, this portion of TIP60 is sufficient to target to the PML NBs, suggesting that PML3-TIP60 interaction is sufficient for targeting TIP60 to the NBs. The PML3-TIP60 interaction is specific, since the region of TIP60 binding is not conserved in other PML isoforms. The physical interaction between PML3 and TIP60 protects TIP60 from Mdm2-mediated degradation, suggesting that PML3 competes with MDM2 for binding to TIP60. Fluorescence recovery after photobleaching analysis indicates that the PML3-TIP60 interaction modulates the nuclear body distribution and mobility of TIP60. Conversely, the distribution and mobility of TIP60 are perturbed in PML3-deficient cells, accompanied by aberrations in DNA damage-repairing response. Thus, PML3 orchestrates the distribution, dynamics, and function of TIP60. Our findings suggest a novel regulatory mechanism by which the PML3 and TIP60 tumor suppressors cooperate to ensure genomic stability.

Indexed as

Cell NucleusGenomic InstabilityHeLa CellsHistone AcetyltransferasesHumansLysine Acetyltransferase 5Nuclear ProteinsPromyelocytic Leukemia ProteinProtein BindingProtein IsoformsProtein Structure, TertiaryProto-Oncogene Proteins c-mdm2Transcription FactorsTumor Suppressor ProteinsHistone AcetyltransferasesKAT5 protein, humanLysine Acetyltransferase 5MDM2 protein, humanNuclear ProteinsPML protein, humanPromyelocytic Leukemia ProteinProtein IsoformsProto-Oncogene Proteins c-mdm2Transcription FactorsTumor Suppressor Proteins

Identifiers

PMID19150978
PMCPMC2659233
OpenAlexW1990290492

What OpenQuestion 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 OpenQuestion graph.