Evidence map›Paper›PMID 18713752›Full record

ArticleThe Journal of biological chemistry2008

Self-assembly of Glut4 storage vesicles during differentiation of 3T3-L1 adipocytes.

Jun Shi, Guanrong Huang, Konstantin V Kandror

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
0.8field-weighted citation impact, top 27% 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

24 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
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  5. Review
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  7. Review
  8. Is There an Interplay Between the Functional Domains of IRAP?Frontiers in cell and developmental biology · 2020
    Review
  9. Review
  10. Article
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  12. Review
  13. Article
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  19. Article
  20. Regulation of glucose transport by insulin: traffic control of GLUT4.Nature reviews. Molecular cell biology · 2012
    Review
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.

Jun ShiBoston University School of Medicine, Boston, Massachusetts 02118, USA.
Guanrong Huang
Konstantin V Kandror
Boston University · US

Funding

INSULIN REGULATION OF CELL NUTRITIONR01DK052057 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI KANDROR, KONSTANTIN V · 1997 to 2023
$7.1M
SECRETION FROM ADIPOSE CELLSR01DK056736 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI KANDROR, KONSTANTIN V · 2000 to 2010
$2.5M
Insulin regulation of cell nutritionR56DK052057 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI KANDROR, KONSTANTIN V · 2008 to 2014
$418k
NIDDK NIH HHS DK52057NIDDK NIH HHS DK56736
6 · The paper itself

Abstract

Glut4 storage vesicles (GSVs) represent translocation-competent vesicular carriers in fat and skeletal muscle cells that deliver Glut4 to the plasma membrane in response to insulin stimulation. GSVs include three major cargo proteins: Glut4, insulin-responsive aminopeptidase (IRAP), and sortilin. Previous work has suggested that the lumenal interaction between Glut4 and sortilin and the cytoplasmic interaction between sortilin and GGA adaptors play an important role in recruitment of Glut4 into the GSVs. However, the mechanism of IRAP targeting to this compartment remains unknown. To address this question, we show that in differentiating adipocytes IRAP enters the GSVs from the "donor" membranes on day 3 of differentiation. Forced expression of sortilin in undifferentiated cells does not recruit IRAP into the vesicles. However, double expression of sortilin and Glut4 reconstitutes functional GSVs that incorporate endogenous IRAP. To explain this process, we show by a yeast two-hybrid system and chemical cross-linking that the lumenal domain of IRAP can interact with the lumenal loop of Glut4. IRAP without the lumenal domain is faithfully targeted to the donor membranes but has significantly lower insulin responsiveness than full-length IRAP. We suggest that lumenal interactions between Glut4 and IRAP play an important role in the assembly of the GSVs.

Indexed as

3T3-L1 CellsAdaptor Proteins, Vesicular TransportAdipocytesAnimalsCell DifferentiationCross-Linking ReagentsCystinyl AminopeptidaseCytosolGlucose Transporter Type 4InsulinMembrane GlycoproteinsMiceModels, BiologicalNerve Tissue ProteinsProtein ConformationProtein Structure, TertiaryAdaptor Proteins, Vesicular TransportCross-Linking ReagentsCystinyl AminopeptidaseGlucose Transporter Type 4Insulinleucyl-cystinyl aminopeptidaseMembrane GlycoproteinsNerve Tissue ProteinsSlc2a4 protein, mouseSortilin

Identifiers

PMID18713752
PMCPMC2573072
OpenAlexW2094663320

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.