Evidence map›Paper›PMID 28880478›Full record

ReviewDiabetes, obesity & metabolism2017

Role of G-proteins in islet function in health and diabetes.

Anjaneyulu Kowluru

Open access · bronzeAbstract readReview
In one paragraph

Review in Diabetes, obesity & metabolism, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

24 citing papers in PubMed, 33 citations in OpenAlex.

  1. Trial
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  9. Review
  10. RhoG-Rac1 Signaling Pathway Mediates Metabolic Dysfunction of the Pancreatic Beta-Cells Under Chronic Hyperglycemic Conditions.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2021
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Review
  16. Gene Expression Profiling of Type 2 Diabetes Mellitus by Bioinformatics Analysis.Computational and mathematical methods in medicine · 2020
    Article
  17. Article
  18. Review
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Anjaneyulu Kowluruβ-Cell Biochemistry Laboratory, John D. Dingell VA Medical Center, and Department of Pharmaceutical Sciences, Wayne State University, Detroit, Michigan.ORCID 0000-0003-1700-0077
Wayne State University · US

Funding

Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Martin G Myers · 2013 to 2026
$24.3M
Role of Ras in Retinal Cell Death in DiabetesR01EY014370 · NEI · WAYNE STATE UNIVERSITY · PI KOWLURU, RENU A. · 2004 to 2023
$4.8M
NADPH Oxidase, Mitochondrial Dysfunction and Diabetic RetinopathyR01EY022230 · NEI · WAYNE STATE UNIVERSITY · PI KOWLURU, ANJANEYULU, KOWLURU, RENU A. · 2012 to 2022
$3.4M
Protein Prenyltransferases in Glucose-Stimulated Insulin SecretionR01DK074921 · NIDDK · WAYNE STATE UNIVERSITY · PI KOWLURU, ANJANEYULU · 2007 to 2010
$1.0M
Mechanisms of Islet Beta Cell Dysfunction in DiabetesI01BX000469 · VA · JOHN D DINGELL VA MEDICAL CENTER · PI KOWLURU, ANJANEYULU · 2009 to 2013
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Novel Regulators of Islet Beta-Cell Function in Health and DiabetesI01BX002801 · VA · JOHN D DINGELL VA MEDICAL CENTER · PI KOWLURU, ANJANEYULU · 2015 to 2018
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BLRD VA I01 BX000469BLRD VA I01 BX002801NEI NIH HHS R01 EY014370NEI NIH HHS R01 EY022230NIDDK NIH HHS P30 DK020572NIDDK NIH HHS R01 DK074921
6 · The paper itself

Abstract

Glucose-stimulated insulin secretion (GSIS) involves interplay between metabolic and cationic events. Seminal contributions from multiple laboratories affirm essential roles for small G-proteins (Rac1, Cdc42, Arf6, Rab27A) in GSIS. Activation of these signalling proteins promotes cytoskeletal remodeling, transport and docking of insulin granules on the plasma membrane for exocytotic secretion of insulin. Evidence in rodent and human islets suggests key roles for lipidation (farnesylation and geranylgeranylation) of these G-proteins for their targeting to appropriate cellular compartments for optimal regulation of effectors leading to GSIS. Interestingly, however, inhibition of prenylation appears to cause mislocalization of non-prenylated, but (paradoxically) activated G-proteins, in "inappropriate" compartments leading to activation of stress kinases and onset of mitochondrial defects, loss in GSIS and apoptosis of the islet β-cell. This review highlights our current understanding of roles of G-proteins and their post-translational lipidation (prenylation) signalling networks in islet function in normal health, metabolic stress (glucolipotoxicity and ER stress) and diabetes. Critical knowledge gaps that need to be addressed for the development of therapeutics to halt defects in these signalling steps in β-cells in models of impaired insulin secretion and diabetes are also highlighted and discussed.

Indexed as

ExocytosisModels, BiologicalADP-Ribosylation Factor 6ADP-Ribosylation FactorsAnimalsApoptosisBlood Glucosecdc42 GTP-Binding ProteinDiabetes MellitusEndoplasmic Reticulum StressGene Expression Regulation, EnzymologicGTP-Binding ProteinsHumansInsulinInsulin SecretionIslets of LangerhansADP-Ribosylation Factor 6ADP-Ribosylation FactorsARF6 protein, humanBlood Glucosecdc42 GTP-Binding ProteinGTP-Binding ProteinsInsulinrab27 GTP-Binding Proteinsrac1 GTP-Binding ProteinfarnesylationgeranylgeranylationG-proteinsislet β-cellNADPH oxidaseRac1

Identifiers

PMID28880478
PMCPMC5657296
OpenAlexW2752051883

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.