Evidence map›Paper›PMID 21965678›Full record

ArticleThe Journal of biological chemistry2011

SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function.

Lin Cong, Suresh B Pakala, Kazufumi Ohshiro, Da-Qiang Li, Rakesh Kumar

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

17 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Regulation of SUMOylation on RNA metabolism in cancers.Frontiers in molecular biosciences · 2023
    Review
  5. Article
  6. Article
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  14. Review
  15. Review
  16. Article
  17. Function and regulation of SUMO proteases.Nature reviews. Molecular cell biology · 2012
    Review
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

5 authors at 2 institutions in 2 countries.

Lin CongDepartment of Biochemistry and Molecular Biology, School of Medicine and Health Sciences, George Washington University, Washington, D. C. 20037.
Suresh B PakalaDepartment of Biochemistry and Molecular Biology, School of Medicine and Health Sciences, George Washington University, Washington, D. C. 20037.
Kazufumi OhshiroDepartment of Biochemistry and Molecular Biology, School of Medicine and Health Sciences, George Washington University, Washington, D. C. 20037.
Da-Qiang LiDepartment of Biochemistry and Molecular Biology, School of Medicine and Health Sciences, George Washington University, Washington, D. C. 20037.
Rakesh KumarDepartment of Biochemistry and Molecular Biology, School of Medicine and Health Sciences, George Washington University, Washington, D. C. 20037; Cancer Research Program, Rajiv Gandhi Centre for Biotechnology, Thiruvananthapuram 695014, India. Electronic address: bcmrxk@gwumc.edu.
George Washington University · USRajiv Gandhi Centre for Biotechnology · IN

Funding

Role of Metastatic Tumor Antigen-1 in Mammary GlandR01CA098823 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KUMAR, RAKESH · 2003 to 2013
$3.1M
NCI NIH HHS CA98823NCI NIH HHS CA98823-S1NCI NIH HHS R01 CA098823
6 · The paper itself

Abstract

Metastasis tumor antigen 1 (MTA1), a component of the Mi-2·nucleosome remodeling and deacetylase complex, plays a crucial role in gene transcription, but the mechanism involved remains largely unknown. Here, we report that MTA1 is a substrate for small ubiquitin-related modifier 2/3 (SUMO2/3) in vivo. Protein inhibitor of activated STAT (PIAS) proteins enhance SUMOylation of MTA1 and may participate in paralog-selective SUMOylation, whereas sentrin/SUMO-specific protease 1 (SENP1) and 2 may act as deSUMOylation enzymes for MTA1. Moreover, MTA1 contains a functional SUMO-interacting motif (SIM) at its C terminus, and SIM is required for the efficient SUMOylation of MTA1. SUMO conjugation on Lys-509, which is located within the SUMO consensus site, together with SIM synergistically regulates the co-repressor activity of MTA1 on PS2 transcription, probably by recruiting HDAC2 onto the PS2 promoter. Interestingly, MTA1 may up-regulate the expression of SUMO2 via interaction with RNA polymerase II and SP1 at the SUMO2 promoter. These findings not only provide novel mechanistic insights into the regulation of the transcriptional repressor function of MTA1 by SUMOylation and SIM but also uncover a potential function of MTA1 in modulating the SUMOylation pathway.

Indexed as

Gene Expression RegulationAmino Acid MotifsAnimalsCell Line, TumorChlorocebus aethiopsCOS CellsGlutathione TransferaseHistone Deacetylase 2Histone DeacetylasesHumansIn Vitro TechniquesLysineModels, BiologicalProtein BindingProtein Processing, Post-TranslationalProtein Structure, TertiaryGlutathione TransferaseHDAC2 protein, humanHistone Deacetylase 2Histone DeacetylasesLysineMTA1 protein, humanRepressor ProteinsRNA, Small InterferingSUMO-1 ProteinSUMO1 protein, humanTrans-Activators

Identifiers

PMID21965678
PMCPMC3243521
OpenAlexW2016729738

What OpenQuestion holds

Textmetadata
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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.