Evidence map›Paper›PMID 17053781›Full record

ArticleThe EMBO journal2006

Suppression of receptor interacting protein 140 repressive activity by protein arginine methylation.

M D Mostaqul Huq, Pawan Gupta, Nien-Pei Tsai, Roger White, Malcolm G Parker, Li-Na Wei

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

61 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Targeting PRMT7-mediated monomethylation of MAVS enhances antiviral innate immune responses and inhibits RNA virus replication.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Protein arginine methylation in transcription and epigenetic regulation.Frontiers in epigenetics and epigenomics · 2023
    Review
  14. Article
  15. Article
  16. Review
  17. Structure, Activity, and Function of PRMT1.Life (Basel, Switzerland) · 2021
    Review
  18. Article
  19. Review
  20. Article

1 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

M D Mostaqul HuqDepartment of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455-0217, USA.
Pawan Gupta
Nien-Pei Tsai
Roger White
Malcolm G Parker
Li-Na Wei
University of Minnesota Medical Center · USImperial College London · GB

Funding

Subcellular Targeting/Packaging of Opioids/ReceptorsP50DA011806 · NIDA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI LOH, HORACE · 1998 to 2012
$14.0M
Studies of nuclear receptor corepressor, NRIP1, in vitamin A signaling pathwaysR01DK060521 · NIDDK · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WEI, LI-NA · 2002 to 2022
$6.9M
TR2 NUCLEAR RECEPTOR IN VITAMIN A SIGNALING PATHWAYSR01DK054733 · NIDDK · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WEI, LI-NA · 1999 to 2021
$5.7M
Studies of Mouse Kappa Opioid Receptor Gene RegulationR01DA011190 · NIDA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WEI, LI-NA · 1997 to 2011
$3.3M
Studies of the Mouse Kappa Opioid Receptor GeneK02DA013926 · NIDA · UNIVERSITY OF MINNESOTA TWIN CITIES · PI WEI, LI-NA · 2002 to 2011
$1.2M
NCI NIH HHS CA 90089NIDA NIH HHS DA11190NIDA NIH HHS DA11806NIDA NIH HHS K02 DA013926NIDA NIH HHS K02-DA13926NIDA NIH HHS P50 DA011806NIDA NIH HHS R01 DA011190NIDDK NIH HHS DK54733NIDDK NIH HHS DK60521NIDDK NIH HHS R01 DK054733NIDDK NIH HHS R01 DK060521
6 · The paper itself

Abstract

Receptor interacting protein 140 (RIP140), a ligand-dependent corepressor for nuclear receptors, can be modified by arginine methylation. Three methylated arginine residues, at Arg-240, Arg-650, and Arg-948, were identified by mass spectrometric analysis. Site-directed mutagenesis studies demonstrated the functionality of these arginine residues. The biological activity of RIP140 was suppressed by protein arginine methyltransferase 1 (PRMT1) due to RIP140 methylation, which reduced the recruitment of histone deacetylases to RIP140 and facilitated its nuclear export by enhancing interaction with exportin 1. A constitutive negative (Arg/Ala) mutant of RIP140 was resistant to the effect of PRMT1, and a constitutive positive (Arg/Phe) mutation mimicked the effect of arginine methylation. The biological activities of the wild type and the mutant proteins were examined in RIP140-null MEF cells. This study uncovered a novel means to inactivate, or suppress, RIP140, and demonstrated protein arginine methylation as a critical type of modification for corepressor.

Indexed as

Active Transport, Cell NucleusAdaptor Proteins, Signal TransducingAnimalsArginineCell NucleusChlorocebus aethiopsCOS CellsExportin 1 ProteinHumansKaryopherinsMethylationNuclear ProteinsNuclear Receptor Interacting Protein 1Protein-Arginine N-MethyltransferasesProtein Processing, Post-TranslationalReceptors, Cytoplasmic and NuclearAdaptor Proteins, Signal TransducingArginineExportin 1 ProteinKaryopherinsNRIP1 protein, humanNuclear ProteinsNuclear Receptor Interacting Protein 1PRMT1 protein, humanProtein-Arginine N-MethyltransferasesReceptors, Cytoplasmic and NuclearRepressor Proteins

Identifiers

PMID17053781
PMCPMC1630415
OpenAlexW2145366585

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.