Evidence map›Paper›PMID 10611313›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Development of an in vitro reconstitution assay for glucose transporter 4 translocation.

G Inoue, B Cheatham, C R Kahn

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

1 citing paper in PubMed, 18 citations in OpenAlex.

  1. 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

3 authors at 2 institutions in 1 country.

G InoueResearch Division, Joslin Diabetes Center, Department of Medicine, Brigham and Women's Hospital, and Harvard Medical School, Boston, MA 02215, USA.
B Cheatham
C R Kahn
Brigham and Women's Hospital · USJoslin Diabetes Center · US

Funding

SPECIAL ASSAY COREP30DK036836 · NIDDK · JOSLIN DIABETES CENTER · PI JEAN E. SCHAFFER · 1986 to 2026
$50.5M
INSULIN RECEPTOR STRUCTURE AND TURNOVERR37DK031036 · NIDDK · JOSLIN DIABETES CENTER · PI KAHN, C RONALD · 2000 to 2019
$12.9M
The Insulin Receptor and Its Signaling MechanismsR01DK031036 · NIDDK · JOSLIN DIABETES CENTER · PI C RONALD KAHN · 1986 to 2026
$4.2M
DEFINING THE MOLECULAR COMPONENTS OF GLUT4 TRANSLOCATIONR01DK051668 · NIDDK · JOSLIN DIABETES CENTER · PI MARATOS-FLIER, ELEFTHERIA · 1997 to 2001
$293k
NIDDK NIH HHS 5 P30 DK 36836NIDDK NIH HHS DK 31036NIDDK NIH HHS DK 51668NIDDK NIH HHS P30 DK036836NIDDK NIH HHS R01 DK031036NIDDK NIH HHS R37 DK031036
6 · The paper itself

Abstract

In an attempt to define the mechanism of insulin-regulated glucose transporter 4 (Glut4) translocation, we have developed an in vitro reconstitution assay. Donor membranes from 3T3-L1 adipocytes transfected with mycGlut4 were incubated with plasma membrane (PM) from nontransfected 3T3-L1 cells, and the association was assessed by using two types of centrifugation assays. Association of mycGlut4 vesicles derived from donor membranes with the PM was concentration-, temperature-, time-, and Ca(2+)-dependent but ATP-independent. Addition of a syntaxin 4 fusion protein produced a biphasic response, increasing association at low concentration and inhibiting association at higher concentrations. PM from insulin-stimulated cells showed an enhanced association as compared with those from untreated cells. Use of donor membranes from insulin-stimulated cells further enhanced the association and also enhanced association to the PM from isolated rat adipocytes. Addition of cytosol, GTP, or guanosine 5'-[gamma-thio]triphosphate decreased the association. In summary, insulin-induced Glut4 translocation can be reconstituted in vitro to a limited extent by using isolated membranes. This association appears to involve protein-protein interactions among the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complex proteins. Finally, the ability of insulin to enhance association depends on insulin-induced changes in the PM and, to a lesser extent, in the donor membranes.

Indexed as

Muscle Proteins3T3 CellsAdipocytesAnimalsBiological TransportCations, DivalentCell CompartmentationCell MembraneGlucose Transporter Type 4InsulinIntracellular MembranesMembrane ProteinsMiceMonosaccharide Transport ProteinsNucleotidesProto-Oncogene Proteins c-mycCations, DivalentGlucose Transporter Type 4InsulinMembrane ProteinsMonosaccharide Transport ProteinsMuscle ProteinsNucleotidesProto-Oncogene Proteins c-mycQa-SNARE ProteinsRecombinant Fusion ProteinsSlc2a4 protein, mouse

Identifiers

PMID10611313
PMCPMC24748
OpenAlexW2058549767

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.