Evidence map›Paper›PMID 24972320›Full record

ArticleJournal of proteomics2014

Quantitative phosphoproteomics reveals novel phosphorylation events in insulin signaling regulated by protein phosphatase 1 regulatory subunit 12A.

Xiangmin Zhang, Danjun Ma, Michael Caruso, Monique Lewis, Yue Qi, Zhengping Yi

Abstract read
In one paragraph

Article in Journal of proteomics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 37 citations in OpenAlex.

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  5. Ser/Thr phosphatases: One of the key regulators of insulin signaling.Reviews in endocrine & metabolic disorders · 2022
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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.

Xiangmin ZhangDepartment of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA.
Danjun MaDepartment of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA.
Michael CarusoDepartment of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA.
Monique LewisDepartment of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA.
Yue QiDepartment of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA.
Zhengping YiDepartment of Pharmaceutical Sciences, College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA. Electronic address: zhengping.yi@wayne.edu.
Wayne State University · 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
Human Skeletal Muscle Proteome and Phosphoproteome in Obesity and Type 2 DiabetesR01DK081750 · NIDDK · WAYNE STATE UNIVERSITY · PI YI, ZHENGPING · 2009 to 2017
$3.0M
NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R01 DK081750NIDDK NIH HHS R01DK081750NIDDK NIH HHS R01DK081750-04S1
6 · The paper itself

Abstract

Serine/threonine protein phosphatase 1 regulatory subunit 12A (PPP1R12A) modulates the activity and specificity of the catalytic subunit of protein phosphatase 1, regulating various cellular processes via dephosphorylation. Nonetheless, little is known about phosphorylation events controlled by PPP1R12A in skeletal muscle insulin signaling. Here, we used quantitative phosphoproteomics to generate a global picture of phosphorylation events regulated by PPP1R12A in a L6 skeletal muscle cell line, which were engineered for inducible PPP1R12A knockdown. Phosphoproteomics revealed 3876 phosphorylation sites (620 were novel) in these cells. Furthermore, PPP1R12A knockdown resulted in increased overall phosphorylation in L6 cells at the basal condition, and changed phosphorylation levels for 698 sites (assigned to 295 phosphoproteins) at the basal and/or insulin-stimulated conditions. Pathway analysis on the 295 phosphoproteins revealed multiple significantly enriched pathways related to insulin signaling, such as mTOR signaling and RhoA signaling. Moreover, phosphorylation levels for numerous regulatory sites in these pathways were significantly changed due to PPP1R12A knockdown. These results indicate that PPP1R12A indeed plays a role in skeletal muscle insulin signaling, providing novel insights into the biology of insulin action. This new information may facilitate the design of experiments to better understand mechanisms underlying skeletal muscle insulin resistance and type 2 diabetes. BIOLOGICAL SIGNIFICANCE: These results identify a large number of potential new substrates of serine/threonine protein phosphatase 1 and suggest that serine/threonine protein phosphatase 1 regulatory subunit 12A indeed plays a regulatory role in multiple pathways related to insulin action, providing novel insights into the biology of skeletal muscle insulin signaling. This information may facilitate the design of experiments to better understand the molecular mechanism responsible for skeletal muscle insulin resistance and associated diseases, such as type 2 diabetes and cardiovascular diseases.

Indexed as

ProteomicsAnimalsCell LineDiabetes Mellitus, Type 2HumansInsulinInsulin ResistanceMuscle ProteinsMyosin-Light-Chain PhosphatasePhosphorylationProtein Phosphatase 1RatsrhoA GTP-Binding ProteinSignal TransductionTOR Serine-Threonine KinasesInsulinMTOR protein, humanmTOR protein, ratMuscle ProteinsMyosin-Light-Chain PhosphatasePPP1R12A protein, humanPpp1r12a protein, ratProtein Phosphatase 1rhoA GTP-Binding ProteinRHOA protein, humanTOR Serine-Threonine KinasesInsulin signalingProtein phosphatase 1 (PP1)Quantitative phosphoproteomicsSerine/threonine protein phosphatase 1 regulatory subunit 12A (PPP1R12A)SILACSkeletal muscle

Identifiers

PMID24972320
PMCPMC4254023
OpenAlexW2046783870

What OpenQuestion holds

Textmetadata
LicenceTDM
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.