Evidence map›Paper›PMID 7691826›Full record

ArticleThe Journal of cell biology1993

Identification of the carboxy terminus as important for the isoform-specific subcellular targeting of glucose transporter proteins.

K J Verhey, S F Hausdorff, M J Birnbaum

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

20 citing papers in PubMed, 75 citations in OpenAlex.

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  6. Nutritional channels in breast cancer.Journal of cellular and molecular medicine · 2009
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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.

K J VerheyDepartment of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.
S F Hausdorff
M J Birnbaum
Harvard University · US

Funding

MOLECULAR BASIS OF INSULIN-RESPONSIVE GLUCOSE TRANSPORTF32DK008714 · NIDDK · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI FRIEDMAN, SHARON H · 1991 to 1993
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THE REGULATION OF GLUCOSE TRANSPORT BY INSULINR01DK039519 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI BIRNBAUM, MORRIS J · 1988 to 1995
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NIDDK NIH HHS DK39519NIDDK NIH HHS F32 DK08714
6 · The paper itself

Abstract

Differential trafficking of glucose transporters contributes significantly to the establishment of a cell's capacity for hormone-regulatable hexose uptake. In the true insulin-sensitive peripheral target tissues, muscle and adipose, the transporter isoform GLUT1 residues on the cell surface and interior of the cell whereas the highly homologous isoform GLUT4 displays virtually exclusive intracellular sequestration, allowing the latter to redistribute to the cell surface in response to hormone. These patterns are equally pronounced in cells into which the transporters have been introduced by DNA-mediated gene transfer, suggesting that signals for isoform-specific sorting are recognized in diverse cell types. To determine the primary sequences responsible for the characteristic distributions, chimeric transporters were constructed in which reciprocal domains were exchanged between GLUT1 and GLUT4. In addition, a non-disruptive, species-specific epitope "tag" was introduced into a neutral region of the transporter to allow analysis of reciprocal chimeras using a single antibody. These recombinant transporters were stably expressed in HIH 3T3 and PC12 cells by retrovirus-mediated gene transfer, and were localized by indirect immunofluorescence and laser scanning confocal microscopy, as well as by staining of plasma membrane sheets prepared from these cells. The results indicate that the carboxy-terminal 30 amino acids are primarily responsible for the differential targeting of the glucose transporter isoforms GLUT1 and GLUT4, though there is a lesser additional contribution by the amino-terminal 183 amino acids.

Indexed as

Cell CompartmentationMuscle Proteins3T3 CellsAnimalsBiological TransportBiomarkersCells, CulturedEpitopesFluorescent Antibody TechniqueGene Transfer TechniquesGlucose Transporter Type 1Glucose Transporter Type 4MiceMonosaccharide Transport ProteinsPC12 CellsRecombinant Fusion ProteinsBiomarkersEpitopesGlucose Transporter Type 1Glucose Transporter Type 4Monosaccharide Transport ProteinsMuscle ProteinsRecombinant Fusion ProteinsSlc2a1 protein, mouseSlc2a4 protein, mouse

Identifiers

PMID7691826
PMCPMC2119809
OpenAlexW2087612874

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.