Evidence map›Paper›PMID 19477941›Full record

ArticleEndocrinology2009

The glucose transporter 2 undergoes plasma membrane endocytosis and lysosomal degradation in a secretagogue-dependent manner.

June Chunqiu Hou, Dumaine Williams, Jérôme Vicogne, Jeffrey E Pessin

Open access · bronzeAbstract read
In one paragraph

Article in Endocrinology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

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  11. 1-Palmitoyl-2-Linoleoyl-3-Acetyl-Molecular and cellular biology · 2019
    Article
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  16. Pancreatic function, type 2 diabetes, and metabolism in aging.International journal of endocrinology · 2012
    Article
  17. Article
  18. 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

4 authors at 3 institutions in 2 countries.

June Chunqiu HouNorth General Hospital , New York, New York 10035, USA.
Dumaine Williams
Jérôme Vicogne
Jeffrey E Pessin
Albert Einstein College of Medicine · USInstitut de Biologie de Lille · FRYork General Hospital · US

Funding

Stable Isotope and Metabolomics CoreP60DK020541 · NIDDK · YESHIVA UNIVERSITY · PI FLEISCHER, NORMAN S. · 1986 to 2014
$29.8M
Translational Research CoreP30DK020541 · NIDDK · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI STREAMSON C CHUA · 2015 to 2026
$27.7M
REGULATION OF THE INSULIN RECEPTOR KINASER01DK033823 · NIDDK · UNIVERSITY OF IOWA · PI KURLAND, IRWIN JACK, PESSIN, JEFFREY E. · 1986 to 2022
$6.7M
Intracellular signaling by the insulin receptor kinaseR37DK033823 · NIDDK · STATE UNIVERSITY NEW YORK STONY BROOK · PI PESSIN, JEFFREY E. · 2005 to 2014
$4.2M
INTRACELLULAR TRAFFICKING OF GLUT4 CONTAINING VESICLESR01DK055811 · NIDDK · UNIVERSITY OF IOWA · PI PESSIN, JEFFREY E. · 2000 to 2009
$3.3M
NIDDK NIH HHS DK20541NIDDK NIH HHS DK33823NIDDK NIH HHS DK55811NIDDK NIH HHS P30 DK020541NIDDK NIH HHS P60 DK020541NIDDK NIH HHS R01 DK033823NIDDK NIH HHS R01 DK055811NIDDK NIH HHS R37 DK033823
6 · The paper itself

Abstract

In beta-cells of the pancreas, the glucose transporter (GLUT)-2 facilitative glucose transporter protein is localized to the plasma membrane and functions as part of the glucose sensing mechanism for the stimulation of insulin secretion. We observed that expressed GLUT2 protein in the cultured Min6B1 cell line undergoes enhanced endocytosis at high extracellular glucose concentrations that stimulate insulin secretion. Moreover, the internalized GLUT2 protein undergoes rapid degradation induced by chronic high-glucose or arginine stimulation but does not undergo plasma membrane recycling or accumulation in any microscopically apparent intracellular membrane compartment. The rapid degradation of GLUT2 was prevented by lysosomal inhibition (chloroquine) concomitant with the accumulation of GLUT2 in endomembrane structures. In contrast, neither endocytosis nor the lack of internal membrane localized GLUT2 remained completely unaffected by proteosomal inhibition (lactacystin) or an heat shock protein-90 inhibitor (geldanamycin). Moreover, the endocytosis and degradation of GLUT2 was specific for beta-cells because expression of GLUT2 in 3T3L1 adipocytes remained cell surface localized and did not display a rapid rate of degradation. Together, these data demonstrate that hyperglycemia directly affects beta-cell function and activates a trafficking pathway that results in the rapid endocytosis and degradation of the cell surface GLUT2 glucose transporter.

Indexed as

3T3-L1 CellsAcetylcysteineAnimalsBenzoquinonesCell MembraneChloroquineEndocytosisExocytosisGlucose Transporter Type 1Glucose Transporter Type 2Glucose Transporter Type 4Lactams, MacrocyclicLysosomesMiceAcetylcysteineBenzoquinonesChloroquinegeldanamycinGlucose Transporter Type 1Glucose Transporter Type 2Glucose Transporter Type 4lactacystinLactams, MacrocyclicSlc2a1 protein, mouseSlc2a2 protein, mouseSlc2a4 protein, mouse

Identifiers

PMID19477941
PMCPMC2736072
OpenAlexW2089415483

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.