Evidence map›Paper›PMID 23444368›Full record

ArticleJournal of cell science2013

A role for Rab14 in the endocytic trafficking of GLUT4 in 3T3-L1 adipocytes.

Sam E Reed, Lorna R Hodgson, Shuang Song, Margaret T May, Eoin E Kelly, Mary W McCaffrey, Cynthia C Mastick, Paul Verkade, Jeremy M Tavaré

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

51 citing papers in PubMed, 73 citations in OpenAlex.

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  11. GLUT4 On the move.The Biochemical journal · 2022
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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

9 authors at 2 institutions in 2 countries.

Sam E ReedSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, UK.
Lorna R Hodgson
Shuang Song
Margaret T May
Eoin E Kelly
Mary W McCaffrey
Cynthia C Mastick
Paul Verkade
Jeremy M Tavaré
University of Bristol · GBUniversity of Nevada, Reno · US

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0900177
6 · The paper itself

Abstract

Insulin enhances the uptake of glucose into adipocytes and muscle cells by promoting the redistribution of the glucose transporter isoform 4 (GLUT4) from intracellular compartments to the cell surface. Rab GTPases regulate the trafficking itinerary of GLUT4 and several have been found on immunopurified GLUT4 vesicles. Specifically, Rab14 has previously been implicated in GLUT4 trafficking in muscle although its role, if any, in adipocytes is poorly understood. Analysis of 3T3-L1 adipocytes using confocal microscopy demonstrated that endogenous GLUT4 and endogenous Rab14 exhibited a partial colocalisation. However, when wild-type Rab14 or a constitutively-active Rab14Q70L mutant were overexpressed in these cells, the colocalisation with both GLUT4 and IRAP became extensive. Interestingly, this colocalisation was restricted to enlarged 'ring-like' vesicular structures (mean diameter 1.3 µm), which were observed in the presence of overexpressed wild-type Rab14 and Rab14Q70L, but not an inactive Rab14S25N mutant. These enlarged vesicles contained markers of early endosomes and were rapidly filled by GLUT4 and transferrin undergoing endocytosis from the plasma membrane. The Rab14Q70L mutant reduced basal and insulin-stimulated cell surface GLUT4 levels, probably by retaining GLUT4 in an insulin-insensitive early endosomal compartment. Furthermore, shRNA-mediated depletion of Rab14 inhibited the transit of GLUT4 through early endosomal compartments towards vesicles and tubules in the perinuclear region. Given the previously reported role of Rab14 in trafficking between endosomes and the Golgi complex, we propose that the primary role of Rab14 in GLUT4 trafficking is to control the transit of internalised GLUT4 from early endosomes into the Golgi complex, rather than direct GLUT4 translocation to the plasma membrane.

Indexed as

3T3-L1 CellsAdipocytesAmino Acid SubstitutionAnimalsCell MembraneEndocytosisEndosomesGlucose Transporter Type 4Golgi ApparatusHypoglycemic AgentsInsulinMiceMutation, MissenseProtein Transportrab GTP-Binding ProteinsGlucose Transporter Type 4Hypoglycemic AgentsInsulinRab14 protein, mouserab GTP-Binding ProteinsSlc2a4 protein, mouseAdipocyteGLUT4InsulinIntracellular traffickingRab14

Identifiers

PMID23444368
PMCPMC3666250
OpenAlexW2085692110

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.