Evidence map›Paper›PMID 20053958›Full record

ReviewAmerican journal of physiology. Regulatory, integrative and comparative physiology2010

Exocytosis mechanisms underlying insulin release and glucose uptake: conserved roles for Munc18c and syntaxin 4.

Jenna L Jewell, Eunjin Oh, Debbie C Thurmond

Open access · greenAbstract readReview
In one paragraph

Review in American journal of physiology. Regulatory, integrative and comparative physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.8field-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

74 citing papers in PubMed, 127 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. A hydrophobic groove in secretagogin allows for alternate interactions with SNAP-25 and syntaxin-4 in endocrine tissues.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Molecules (Basel, Switzerland) · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

14 more citing papers are in PubMed but not listed here.

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 3 institutions in 2 countries.

Jenna L JewellDepartment of Pediatrics, Indiana University School of Medicine, Indianapolis, IN, USA.
Eunjin Oh
Debbie C Thurmond
Indiana University – Purdue University Indianapolis · USIndiana University School of MedicineLaboratoire d’immunologie intégrative du cancer · FR

Funding

Regulation of Glucose Homeostasis by Munc18 ProteinsR01DK067912 · NIDDK · INDIANA UNIV-PURDUE UNIV AT INDIANAPOLIS · PI THURMOND, DEBBIE C · 2004 to 2023
$6.5M
Cdc42-regulated insulin granule exocytosisR01DK076614 · NIDDK · INDIANA UNIVERSITY INDIANAPOLIS · PI THURMOND, DEBBIE C · 2008 to 2012
$1.6M
NIDDK NIH HHS DK067912NIDDK NIH HHS DK076614NIDDK NIH HHS R01 DK067912NIDDK NIH HHS R01 DK076614
6 · The paper itself

Abstract

Type 2 diabetes has been coined "a two-hit disease," as it involves specific defects of glucose-stimulated insulin secretion from the pancreatic beta cells in addition to defects in peripheral tissue insulin action required for glucose uptake. Both of these processes, insulin secretion and glucose uptake, are mediated by SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein core complexes composed of syntaxin, SNAP-23/25, and VAMP proteins. The SNARE core complex is regulated by the Sec1/Munc18 (SM) family of proteins, which selectively bind to their cognate syntaxin isoforms with high affinity. The process of insulin secretion uses multiple Munc18-syntaxin isoform pairs, whereas insulin action in the peripheral tissues appears to use only the Munc18c-syntaxin 4 pair. Importantly, recent reports have linked obesity and Type 2 diabetes in humans with changes in protein levels and single nucleotide polymorphisms (SNPs) of Munc18 and syntaxin isoforms relevant to these exocytotic processes, although the molecular mechanisms underlying the observed phenotypes remain incomplete (5, 104, 144). Given the conservation of these proteins in two seemingly disparate processes and the need to design and implement novel and more effective clinical interventions, it will be vitally important to delineate the mechanisms governing these conserved SNARE-mediated exocytosis events. Thus, we provide here an up-to-date historical review of advancements in defining the roles and molecular mechanisms of Munc18-syntaxin complexes in the pathophysiology of Type 2 diabetes.

Indexed as

AnimalsBlood GlucoseDiabetes Mellitus, Type 2ExocytosisHumansInsulinInsulin SecretionMunc18 ProteinsQa-SNARE ProteinsBlood GlucoseInsulinMunc18 ProteinsQa-SNARE Proteins

Identifiers

PMID20053958
PMCPMC2838661
OpenAlexW2103581805

What Socratic 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 Socratic graph.