Evidence map›Paper›PMID 22761437›Full record

ArticleThe Journal of biological chemistry2012

Sequestosome 1/p62, a scaffolding protein, is a newly identified partner of IRS-1 protein.

Thangiah Geetha, Chen Zheng, Nilmini Vishwaprakash, Tom L Broderick, Jeganathan Ramesh Babu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
1.2field-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

17 citing papers in PubMed, 30 citations in OpenAlex.

  1. Trial
  2. Review
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  4. Article
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  6. Article
  7. Absence of IQGAP1 Protein Leads to Insulin Resistance.The Journal of biological chemistry · 2017
    Article
  8. Review
  9. Review
  10. Protein Scaffolds Control Localized Protein Kinase Cζ Activity.The Journal of biological chemistry · 2016
    Article
  11. IRS-1 Functions as a Molecular Scaffold to Coordinate IGF-I/IGFBP-2 Signaling During Osteoblast Differentiation.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2016
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Role of p62/SQSTM1 in liver physiology and pathogenesis.Experimental biology and medicine (Maywood, N.J.) · 2013
    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 1 country.

Thangiah GeethaDepartment of Nutrition, Dietetics, and Hospitality Management, Auburn University, Auburn, AL 36849, USA.
Chen Zheng
Nilmini Vishwaprakash
Tom L Broderick
Jeganathan Ramesh Babu
Auburn University · USMidwestern University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Defects in the insulin-signaling pathway may lead to the development of skeletal muscle insulin resistance, which is one of the earliest abnormalities detected in individuals with the metabolic syndrome and predisposes them to develop type 2 diabetes. Previous studies have shown that deletion of the mouse sequestosome 1/p62 gene results in mature-onset obesity that progresses to insulin and leptin resistance and, ultimately, type 2 diabetes. Sequestosome 1/p62 is involved in receptor-mediated signal transduction and functions as an intracellular signal modulator or adaptor protein. Insulin receptor substrate-1 (IRS-1) plays a central role in transducing the insulin signal via phosphorylation, protein-protein interactions, and protein modifications. Mapping studies demonstrated that the SH(2) domain at the amino terminus of sequestosome 1/p62 interacts with IRS-1 upon insulin stimulation. Further, IRS-1 interacts with p62 through its YMXM motifs at Tyr-608, Tyr-628, and/or Tyr-658 in a manner similar to its interaction with p85 of phosphoinositol 3-kinase. Overexpression of p62 increased phosphorylation of Akt, GLUT4 translocation, and glucose uptake, providing evidence that p62 participates in the insulin-signaling pathway through its interactions with IRS-1.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsCHO CellsCricetinaeCricetulusDNA-Binding ProteinsHeat-Shock ProteinsHumansInsulinInsulin Receptor Substrate ProteinsMicePeptide MappingPhosphatidylinositol 3-KinasesPhosphorylationProtein TransportAdaptor Proteins, Signal TransducingDNA-Binding ProteinsGLUT4 enhancer factor, mouseHeat-Shock ProteinsInsulinInsulin Receptor Substrate ProteinsIrs1 protein, mousePhosphatidylinositol 3-KinasesProto-Oncogene Proteins c-aktSequestosome-1 ProteinSqstm1 protein, mouseTranscription Factors

Identifiers

PMID22761437
PMCPMC3436154
OpenAlexW1984259171

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.