Evidence map›Paper›PMID 18628823›Full record

ArticlePloS one2008

PKCepsilon stimulated arginine methylation of RIP140 for its nuclear-cytoplasmic export in adipocyte differentiation.

Pawan Gupta, Ping-Chih Ho, M D Mostaqul Huq, Amjad Ali Khan, Nien-Pei Tsai, Li-Na Wei

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Deletion of Nrip1 Extends Female Mice Longevity, Increases Autophagy, and Delays Cell Senescence.The journals of gerontology. Series A, Biological sciences and medical sciences · 2018
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  20. Cholesterol regulation of receptor-interacting protein 140 via microRNA-33 in inflammatory cytokine production.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2011
    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

6 authors at 1 institution in 1 country.

Pawan GuptaDepartment of Pharmacology, University of Minnesota Medical School, Minneapolis, Minnesota, United States of America.
Ping-Chih Ho
M D Mostaqul Huq
Amjad Ali Khan
Nien-Pei Tsai
Li-Na Wei
University of Minnesota Medical Center · US

Funding

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
NIDA NIH HHS DA11190NIDA NIH HHS K02 DA013926NIDA NIH HHS K02-DA13926NIDA NIH HHS R01 DA011190NIDDK NIH HHS DK54733NIDDK NIH HHS DK60521NIDDK NIH HHS R01 DK054733NIDDK NIH HHS R01 DK060521
6 · The paper itself

Abstract

backgroundReceptor interacting protein 140 (RIP140) is a versatile transcriptional co-repressor that plays roles in diverse metabolic processes including fat accumulation in adipocytes. Previously we identified three methylated arginine residues in RIP140, which rendered its export to the cytoplasm; but it was unclear what triggered RIP140 arginine methylation. METHODOLOGY/PRINCIPAL

findingsIn this study, we determined the activated PKCepsilon as the specific trigger for RIP140 arginine methylation and its subsequent export. We identified two PKCepsilon-phosphorylated residues of RIP140, Ser-102 and Ser-1003, which synergistically stimulated direct binding of RIP140 by 14-3-3 that recruited protein arginine methyl transferase 1 to methylate RIP140. The methylated RIP140 then preferentially recruited exportin 1 for nuclear export. As a result, the nuclear gene-repressive activity of RIP140 was reduced. In RIP140 null adipocyte cultures, the defect in fat accumulation was effectively rescued by the phosphorylation-deficient mutant RIP140 that resided predominantly in the nucleus, but less so by the phospho-mimetic RIP140 that was exported to the cytoplasm. CONCLUSIONS/SIGNIFICANCE: This study uncovers a novel means, via a cascade of protein modifications, to inactivate, or suppress, the nuclear action of an important transcription coregulator RIP140, and delineates the first specific phosphorylation-arginine methylation cascade that could alter protein subcellular distribution and biological activity.

Indexed as

14-3-3 Proteins3T3-L1 CellsActive Transport, Cell NucleusAdaptor Proteins, Signal TransducingAdipocytesAnimalsArginineCell DifferentiationCell NucleusChlorocebus aethiopsCOS CellsCytoplasmDNA MethylationIntracellular Signaling Peptides and ProteinsMethyltransferasesMice14-3-3 ProteinsAdaptor Proteins, Signal TransducingArginineIntracellular Signaling Peptides and ProteinsMethyltransferasesNRIP1 protein, humanNuclear ProteinsNuclear Receptor Interacting Protein 1PRMT2 protein, humanProtein-Arginine N-MethyltransferasesProtein Kinase C-epsilon

Identifiers

PMID18628823
PMCPMC2440817
OpenAlexW1981698873

What OpenQuestion holds

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LicenceCC BY
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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.