Evidence map›Paper›PMID 19864425›Full record

ArticleThe Journal of biological chemistry2010

Proteomic analysis of GLUT4 storage vesicles reveals LRP1 to be an important vesicle component and target of insulin signaling.

Mark P Jedrychowski, Carlos A Gartner, Steven P Gygi, Li Zhou, Joachim Herz, Konstantin V Kandror, Paul F Pilch

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 85 papers.

0numbers the graph read from it
0cells of the map it votes in
85citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

85 citing papers in PubMed, 135 citations in OpenAlex.

  1. Review
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  12. Protein sorting from endosomes to the TGN.Frontiers in cell and developmental biology · 2023
    Review
  13. Article
  14. Article
  15. Article
  16. GLUT4 On the move.The Biochemical journal · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Article

25 more citing papers are in PubMed but not listed here.

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

7 authors at 5 institutions in 1 country.

Mark P JedrychowskiDepartment of Biochemistry, Boston University Medical School, Boston, Massachusetts 02118, USA.
Carlos A Gartner
Steven P Gygi
Li Zhou
Joachim Herz
Konstantin V Kandror
Paul F Pilch
The University of Texas Southwestern Medical Center · USBoston Medical Center · USBoston University · USHarvard Stem Cell Institute · USHarvard University · US

Funding

PRE- AND POSTDOCTORAL TRAINING IN BIOCHEMISTRY OF AGINGT32AG000115 · NIA · BOSTON UNIVERSITY MEDICAL CAMPUS · PI POLGAR, PETER RUDOLPH · 1985 to 2012
$4.3M
Metabolism of the VLDL receptor and ApoE receptor 2R37HL063762 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI HERZ, JOACHIM J · 2010 to 2019
$4.0M
Rapamycin-sensitive pathway of T cell ActivationZ01AG000115 · NIA · NATIONAL INSTITUTE ON AGING · PI LONGO, DAN L. · 2000 to 2008
$762k
Intramural NIH HHS Z01 AG000115NHLBI NIH HHS R37 HL063762NIA NIH HHS T32 AG000115NIDDK NIH HHS DK30435
6 · The paper itself

Abstract

Insulin stimulates the translocation of intracellular GLUT4 to the plasma membrane where it functions in adipose and muscle tissue to clear glucose from circulation. The pathway and regulation of GLUT4 trafficking are complicated and incompletely understood and are likely to be contingent upon the various proteins other than GLUT4 that comprise and interact with GLUT4-containing vesicles. Moreover, not all GLUT4 intracellular pools are insulin-responsive as some represent precursor compartments, thus posing a biochemical challenge to the purification and characterization of their content. To address these issues, we immunodepleted precursor GLUT4-rich vesicles and then immunopurified GLUT4 storage vesicle (GSVs) from primary rat adipocytes and subjected them to semi-quantitative and quantitative proteomic analysis. The purified vesicles translocate to the cell surface almost completely in response to insulin, the expected behavior for bona fide GSVs. In total, over 100 proteins were identified, about 50 of which are novel in this experimental context. LRP1 (low density lipoprotein receptor-related protein 1) was identified as a major constituent of GSVs, and we show it interacts with the lumenal domains of GLUT4 and other GSV constituents. Its cytoplasmic tail interacts with the insulin-signaling pathway target, AS160 (Akt substrate of 160 kDa). Depletion of LRP1 from 3T3-L1 adipocytes reduces GLUT4 expression and correspondingly results in decreased insulin-stimulated 2-[(3)H]deoxyglucose uptake. Furthermore, adipose-specific LRP1 knock-out mice also exhibit decreased GLUT4 expression. These findings suggest LRP1 is an important component of GSVs, and its expression is needed for the formation of fully functional GSVs.

Indexed as

ProteomicsAdaptor Proteins, Vesicular TransportAdipocytesAnimalsCell FractionationCell LineCell MembraneCentrifugation, Density GradientCystinyl AminopeptidaseCytoplasmic VesiclesDeoxyglucoseGene Knockdown TechniquesGlucose Transporter Type 4GTPase-Activating ProteinsHumansInsulinAdaptor Proteins, Vesicular TransportCystinyl AminopeptidaseDeoxyglucoseGlucose Transporter Type 4GTPase-Activating ProteinsInsulinleucyl-cystinyl aminopeptidaseLow Density Lipoprotein Receptor-Related Protein-1Lrp1 protein, mouseReceptors, LDLReceptors, TransferrinRNA, Small InterferingSlc2a4 protein, ratSortilinTBC1D4 protein, ratTumor Suppressor Proteins

Identifiers

PMID19864425
PMCPMC2804154
OpenAlexW2087816256

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.