Evidence map›Paper›PMID 22493697›Full record

ArticlePloS one2012

Cholesterol depletion in adipocytes causes caveolae collapse concomitant with proteosomal degradation of cavin-2 in a switch-like fashion.

Michael R Breen, Marta Camps, Francisco Carvalho-Simoes, Antonio Zorzano, Paul F Pilch

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 65 citations in OpenAlex.

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  15. Review
  16. Lung Endothelial Transcytosis.Comprehensive Physiology · 2020
    Review
  17. Caveolae as Potential Hijackable Gates in Cell Communication.Frontiers in cell and developmental biology · 2020
    Review
  18. Article
  19. Review
  20. 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

5 authors at 3 institutions in 2 countries.

Michael R BreenDepartment of Biochemistry, Boston University School of Medicine, Boston, Massachusetts, United States of America.
Marta Camps
Francisco Carvalho-Simoes
Antonio Zorzano
Paul F Pilch
Boston University · USUniversitat de Barcelona · ESCentro de Investigación Biomédica en Red Diabetes y Enfermedades Metabólicas Asociadas · ES

Funding

TRAINING PROGRAM IN ENDOCRINE AND METABOLIC RESEARCHT32DK007201 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CORKEY, BARBARA E., KANDROR, KONSTANTIN V · 1986 to 2023
$6.4M
ACTIVATION OF HEXOSE TRANSPORT BY INSULINR01DK030425 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI PILCH, PAUL F · 1986 to 2012
$3.5M
Role of Caveolae in Signaling in Fat CellsR01DK056935 · NIDDK · BOSTON UNIVERSITY MEDICAL CAMPUS · PI PILCH, PAUL F · 2001 to 2010
$2.6M
NIDDK NIH HHS DK07201NIDDK NIH HHS DK30425NIDDK NIH HHS DK56935NIDDK NIH HHS R01 DK030425NIDDK NIH HHS R01 DK056935NIDDK NIH HHS T32 DK007201
6 · The paper itself

Abstract

Caveolae, little caves of cell surfaces, are enriched in cholesterol, a certain level of which is required for their structural integrity. Here we show in adipocytes that cavin-2, a peripheral membrane protein and one of 3 cavin isoforms present in caveolae from non-muscle tissue, is degraded upon cholesterol depletion in a rapid fashion resulting in collapse of caveolae. We exposed 3T3-L1 adipocytes to the cholesterol depleting agent methyl-β-cyclodextrin, which results in a sudden and extensive degradation of cavin-2 by the proteasome and a concomitant movement of cavin-1 from the plasma membrane to the cytosol along with loss of caveolae. The recovery of cavin-2 at the plasma membrane is cholesterol-dependent and is required for the return of cavin-1 from the cytosol to the cell surface and caveolae restoration. Expression of shRNA directed against cavin-2 also results in a cytosolic distribution of cavin-1 and loss of caveolae. Taken together, these data demonstrate that cavin-2 functions as a cholesterol responsive component of caveolae that is required for cavin-1 localization to the plasma membrane, and caveolae structural integrity.

Indexed as

3T3-L1 CellsAdipocytesAnimalsbeta-CyclodextrinsCaveolaeCholesterolFibroblastsGenetic VectorsHEK293 CellsHumansHydroxymethylglutaryl-CoA Reductase InhibitorsLentivirusMembrane ProteinsMicePrimary Cell CultureProteasome Endopeptidase Complexbeta-CyclodextrinsCavin1 protein, mouseCholesterolHydroxymethylglutaryl-CoA Reductase InhibitorsMembrane Proteinsmethyl-beta-cyclodextrinProteasome Endopeptidase ComplexProtein IsoformsRNA-Binding ProteinsRNA, Small Interfering

Identifiers

PMID22493697
PMCPMC3321009
OpenAlexW2032470185

What OpenQuestion holds

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LicenceCC BY
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.