Evidence map›Paper›PMID 19945409›Full record

ArticleCell metabolism2009

A negative regulatory pathway of GLUT4 trafficking in adipocyte: new function of RIP140 in the cytoplasm via AS160.

Ping-Chih Ho, Yi-Wei Lin, Yao-Chen Tsui, Pawan Gupta, Li-Na Wei

Open access · bronzeAbstract read
In one paragraph

Article in Cell metabolism, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

36 citing papers in PubMed, 58 citations in OpenAlex.

  1. Article
  2. Review
  3. Skin aging: Dermal adipocytes metabolically reprogram dermal fibroblasts.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. 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
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. A proteolytic pathway that controls glucose uptake in fat and muscle.Reviews in endocrine & metabolic disorders · 2014
    Review
  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

5 authors at 1 institution in 2 countries.

Ping-Chih HoDepartment of Pharmacology, University of Minnesota Medical School, Minneapolis, MN 55455, USA.
Yi-Wei Lin
Yao-Chen Tsui
Pawan Gupta
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

Receptor-interacting protein 140 (RIP140), a nuclear receptor corepressor, is important for lipid and glucose metabolism. In adipocytes, RIP140 can be phosphorylated by protein kinase C epsilon (PKCvarepsilon), followed by arginine methylation, and exported to the cytoplasm. This study demonstrates for the first time a cytoplasmic function for RIP140: to counteract insulin-stimulated glucose transporter 4 (GLUT4) membrane partitioning and glucose uptake in adipocytes. Cytoplasmic RIP140 interacts with the Akt substrate AS160, thereby impeding AS160 phosphorylation by Akt; this in turn reduces GLUT4 trafficking. This signal transduction pathway can be recapitulated in the epididymal adipocytes of diet-induced obese mice: nuclear PKCvarepsilon is activated, cytoplasmic RIP140 increases, and GLUT4 trafficking and glucose uptake are reduced. The data reveal a new, cytoplasmic function for RIP140 as a negative regulator of GLUT4 trafficking and glucose uptake, and shed insight into the regulation of basal and insulin-stimulated glucose disposal by a nuclear-initiated counteracting mechanism.

Indexed as

Adaptor Proteins, Signal TransducingAdipocytesAnimalsCell LineCytoplasmDown-RegulationGlucoseGlucose Transporter Type 4GTPase-Activating ProteinsMiceMice, ObeseNuclear ProteinsNuclear Receptor Interacting Protein 1Protein Kinase C-epsilonProtein TransportProto-Oncogene Proteins c-aktAdaptor Proteins, Signal TransducingGlucoseGlucose Transporter Type 4GTPase-Activating ProteinsNuclear ProteinsNuclear Receptor Interacting Protein 1Protein Kinase C-epsilonProto-Oncogene Proteins c-aktTbc1d4 protein, mouse

Identifiers

PMID19945409
PMCPMC2787476
OpenAlexW2006082012

What OpenQuestion holds

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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.