Evidence map›Paper›PMID 27966646›Full record

ArticleScientific reports2016

Insulin-induced Effects on the Subcellular Localization of AKT1, AKT2 and AS160 in Rat Skeletal Muscle.

Xiaohua Zheng, Gregory D Cartee

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. AKT ISOFORMS-AS160-GLUT4: The defining axis of insulin resistance.Reviews in endocrine & metabolic disorders · 2021
    Review
  5. Role of Akt isoforms in neuronal insulin signaling and resistance.Cellular and molecular life sciences : CMLS · 2021
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The cell biology of systemic insulin function.The Journal of cell biology · 2018
    Review
  11. Review
  12. Biochemical and cellular properties of insulin receptor signalling.Nature reviews. Molecular cell biology · 2018
    Review
  13. Article
  14. Article
  15. 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

2 authors at 1 institution in 1 country.

Xiaohua ZhengMuscle Biology Laboratory, School of Kinesiology, University of Michigan, Ann Arbor, MI, USA.
Gregory D CarteeMuscle Biology Laboratory, School of Kinesiology, University of Michigan, Ann Arbor, MI, USA.
University of Michigan–Ann Arbor · US

Funding

Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Mehboob A Hussain · 2013 to 2026
$24.3M
Skeletal Muscle Glucose Uptake: Exercise and InsulinR01DK071771 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARTEE, GREGORY D. · 2006 to 2020
$4.5M
NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R01 DK071771
6 · The paper itself

Abstract

AKT1 and AKT2, the AKT isoforms that are highly expressed in skeletal muscle, have distinct and overlapping functions, with AKT2 more important for insulin-stimulated glucose metabolism. In adipocytes, AKT2 versus AKT1 has greater susceptibility for insulin-mediated redistribution from cytosolic to membrane localization, and insulin also causes subcellular redistribution of AKT Substrate of 160 kDa (AS160), an AKT2 substrate and crucial mediator of insulin-stimulated glucose transport. Although skeletal muscle is the major tissue for insulin-mediated glucose disposal, little is known about AKT1, AKT2 or AS160 subcellular localization in skeletal muscle. The major aim of this study was to determine insulin's effects on the subcellular localization and phosphorylation of AKT1, AKT2 and AS160 in skeletal muscle. Rat skeletal muscles were incubated ex vivo ± insulin, and differential centrifugation was used to isolate cytosolic and membrane fractions. The results revealed that: 1) insulin increased muscle membrane localization of AKT2, but not AKT1; 2) insulin increased AKT2 phosphorylation in the cytosol and membrane fractions; 3) insulin increased AS160 localization to the cytosol and membranes; and 4) insulin increased AS160 phosphorylation in the cytosol, but not membranes. These results demonstrate distinctive insulin effects on the subcellular redistribution of AKT2 and its substrate AS160 in skeletal muscle.

Indexed as

AndrostadienesAnimalsBiological TransportCell MembraneCytosolGene Expression RegulationGTPase-Activating ProteinsInsulinMaleMuscle, SkeletalPhosphorylationProto-Oncogene Proteins c-aktRatsWortmanninAkt1 protein, ratAkt2 protein, ratAndrostadienesGTPase-Activating ProteinsInsulinProto-Oncogene Proteins c-aktTBC1D4 protein, ratWortmannin

Identifiers

PMID27966646
PMCPMC5155274
OpenAlexW2562873642

What OpenQuestion holds

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LicenceCC BY
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.