Evidence map›Paper›PMID 20739507›Full record

ArticleAmerican journal of physiology. Endocrinology and metabolism2010

Glucose-induced ERM protein activation and translocation regulates insulin secretion.

James P Lopez, Jerrold R Turner, Louis H Philipson

Open access · greenAbstract read
In one paragraph

Article in American journal of physiology. Endocrinology and metabolism, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. ETS Transcription Factors in Immune Cells and Immune-Related Diseases.International journal of molecular sciences · 2024
    Review
  2. Article
  3. Review
  4. Potential Role of Moesin in Regulating Mast Cell Secretion.International journal of molecular sciences · 2023
    Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
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  16. Review
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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

3 authors at 1 institution in 1 country.

James P LopezDept. of Medicine, The Univ. of Chicago, IL 60637, USA.
Jerrold R Turner
Louis H Philipson
University of Chicago · US

Funding

ULTRASTRUCTURE AND CYTOMORPHOLOGY COREP30DK042086 · NIDDK · UNIVERSITY OF CHICAGO · PI CHANG, EUGENE B · 1990 to 2025
$29.8M
TRANSGENIC COREP60DK020595 · NIDDK · UNIVERSITY OF CHICAGO · PI BELL, GRAEME I · 1985 to 2012
$25.5M
ZO-1-MEDIATED PROTEIN INTERACTIONS: REGULATORS AND INTEGRATORS OF DIVERSE EPITHELIAL FUNCTIONS IN HEALTH AND DISEASER01DK061931 · NIDDK · UNIVERSITY OF CHICAGO · PI JERROLD R. TURNER · 2001 to 2026
$15.0M
POTASSIUM CHANNEL EXPRESSION IN PANCREATIC B CELLSR01DK048494 · NIDDK · UNIVERSITY OF CHICAGO · PI PHILIPSON, LOUIS H. · 1995 to 2011
$2.8M
IMAGING BETA CELL FUNCTION WITH BIOSENSORSR01DK063493 · NIDDK · UNIVERSITY OF CHICAGO · PI PHILIPSON, LOUIS H. · 2002 to 2007
$1.5M
Minority Predoctoral Fellowship ProgramF31DK076171 · NIDDK · UNIVERSITY OF CHICAGO · PI LOPEZ, JAMES P · 2006 to 2009
$159k
NIDDK NIH HHS 5F31 DK-076171NIDDK NIH HHS DK-061931NIDDK NIH HHS DK-20595NIDDK NIH HHS DK-42086NIDDK NIH HHS DK-48494NIDDK NIH HHS DK-63493
6 · The paper itself

Abstract

A key step in regulating insulin secretion is insulin granule trafficking to the plasma membrane. Using live-cell time-lapse confocal microscopy, we observed a dynamic association of insulin granules with filamentous actin and PIP2-enriched structures. We found that the scaffolding protein family ERM, comprising ezrin, radixin, and moesin, are expressed in β-cells and target both F-actin and PIP2. Furthermore, ERM proteins are activated via phosphorylation in a glucose- and calcium-dependent manner. This activation leads to a translocation of the ERM proteins to sites on the cell periphery enriched in insulin granules, the exocyst complex docking protein Exo70, and lipid rafts. ERM scaffolding proteins also participate in insulin granule trafficking and docking to the plasma membrane. Overexpression of a truncated dominant-negative ezrin construct that lacks the ERM F-actin binding domain leads to a reduction in insulin granules near the plasma membrane and impaired secretion. Conversely, overexpression of a constitutively active ezrin results in more granules near the cell periphery and an enhancement of insulin secretion. Diabetic mouse islets contain less active ERM, suggestive of a novel mechanism whereby impairment of insulin granule trafficking to the membrane through a complex containing F-actin, PIP2, Exo70, and ERM proteins contributes to defective insulin secretion.

Indexed as

AnimalsCell MembraneCell MovementCytoskeletal ProteinsDiabetes Mellitus, Type 2DNA-Binding ProteinsFemaleInsulinInsulin-Secreting CellsInsulin SecretionMaleMiceMice, Inbred C57BLMice, ObeseMicroscopy, ConfocalTranscription FactorsCytoskeletal ProteinsDNA-Binding ProteinsEtv5 protein, mouseExo70 protein, mouseInsulinTranscription FactorsVesicular Transport Proteins

Identifiers

PMID20739507
PMCPMC2980361
OpenAlexW2118598883

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.