Evidence map›Paper›PMID 27246912›Full record

ArticleDiabetes2016

Protein Phosphatase 1-α Regulates AS160 Ser588 and Thr642 Dephosphorylation in Skeletal Muscle.

Pragya Sharma, Edward B Arias, Gregory D Cartee

Open access · bronzeAbstract read
In one paragraph

Article in Diabetes, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.0field-weighted citation impact, top 22% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
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  5. Article
  6. Ser/Thr phosphatases: One of the key regulators of insulin signaling.Reviews in endocrine & metabolic disorders · 2022
    Review
  7. Article
  8. Excess Accumulation of Lipid Impairs Insulin Sensitivity in Skeletal Muscle.International journal of molecular sciences · 2020
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. 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

3 authors at 1 institution in 1 country.

Pragya SharmaMuscle Biology Laboratory, School of Kinesiology, University of Michigan, Ann Arbor, MI.
Edward B AriasMuscle Biology Laboratory, School of Kinesiology, University of Michigan, Ann Arbor, MI.
Gregory D CarteeMuscle Biology Laboratory, School of Kinesiology, University of Michigan, Ann Arbor, MI Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI Institute of Gerontology, University of Michigan, Ann Arbor, MI gcartee@umich.edu.
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

Akt substrate of 160 kDa (AS160) phosphorylation on Thr(642) and Ser(588) by Akt is essential for insulin's full effect on glucose transport. However, protein phosphorylation is determined by the balance of actions by kinases and phosphatases, and the specific phosphatase(s) controlling AS160 dephosphorylation is (are) unknown. Accordingly, we assessed roles of highly expressed skeletal muscle serine/threonine phosphatases (PP1, PP2A, PP2B, and PP2C) on AS160 dephosphorylation. Preliminary screening of candidate phosphatases used an AS160 dephosphorylation assay. Lysates from insulin-stimulated skeletal muscle were treated with pharmacological phosphatase inhibitors and assessed for AS160 Ser(588) and Thr(642) dephosphorylation. AS160 dephosphorylation on both phosphorylation sites was unaltered by PP2B or PP2C inhibitors. Okadaic acid (low dose inhibits PP2A; high dose inhibits PP1) delayed AS160 Ser(588) (both doses) and Thr(642) (high dose only) dephosphorylation concomitant with greater Akt phosphorylation (both doses). AS160 was coimmunoprecipitated with PP1-α but not with PP1-β, PP1-γ1, or PP2A. Recombinant inhibitor-2 protein (a selective PP1 inhibitor) delayed AS160 dephosphorylation on both phosphorylation sites without altering Akt phosphorylation. Furthermore, knockdown of PP1-α but not PP1-β or PP1-γ1 by small interfering RNA caused greater AS160 Ser(588) and Thr(642) phosphorylation concomitant with unaltered Akt phosphorylation. Together, these results identified PP1-α as a regulator of AS160 Thr(642) and Ser(588) dephosphorylation in skeletal muscle.

Indexed as

AnimalsBenzophenanthridinesCell LineGTPase-Activating ProteinsImmunoblottingImmunoprecipitationIsoquinolinesMaleMuscle, SkeletalOkadaic AcidPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Phosphatase 2RatsRats, WistarBenzophenanthridinesGTPase-Activating ProteinsIsoquinolinesOkadaic AcidPhosphoprotein PhosphatasesProtein Phosphatase 1Protein Phosphatase 2RNA, Small InterferingsanguinarineSerineTacrolimusTBC1D4 protein, rat

Identifiers

PMID27246912
PMCPMC5001182
OpenAlexW2414003099

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.