Evidence map›Paper›PMID 23469926›Full record

ArticleTraffic (Copenhagen, Denmark)2013

Overexpression of caveolin-1 is sufficient to phenocopy the behavior of a disease-associated mutant.

Caroline A Hanson, Kimberly R Drake, Michelle A Baird, Bing Han, Lewis J Kraft, Michael W Davidson, Anne K Kenworthy

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2013. 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
1.8field-weighted citation impact, top 18% 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, 34 citations in OpenAlex.

  1. Review
  2. Membrane Tension Regulation is Required for Wound Repair.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
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  6. Review
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  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Assembly and Turnover of Caveolae: What Do We Really Know?Frontiers in cell and developmental biology · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  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

7 authors at 3 institutions in 1 country.

Caroline A HansonDepartment of Molecular Physiology & Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Kimberly R Drake
Michelle A Baird
Bing Han
Lewis J Kraft
Michael W Davidson
Anne K Kenworthy
Vanderbilt University · USFlorida State University · USNational High Magnetic Field Laboratory · US

Funding

Caveolar Defects Underlie the Genetic Origins of PAHR01HL111259 · NHLBI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI KENWORTHY, ANNE K, LOYD, JAMES E · 2012 to 2016
$3.5M
Regulation of Microdomain Structure in Living CellsR01GM073846 · NIGMS · VANDERBILT UNIVERSITY · PI KENWORTHY, ANNE K · 2006 to 2010
$1.3M
NHLBI NIH HHS R01 HL111259NIGMS NIH HHS R01 GM073846
6 · The paper itself

Abstract

Mutations and alterations in caveolin-1 expression levels have been linked to a number of human diseases. How misregulation of caveolin-1 contributes to disease is not fully understood, but has been proposed to involve the intracellular accumulation of mutant forms of the protein. To better understand the molecular basis for trafficking defects that trap caveolin-1 intracellularly, we compared the properties of a GFP-tagged version of caveolin-1 P132L, a mutant form of caveolin-1 previously linked to breast cancer, with wild-type caveolin-1. Unexpectedly, wild-type caveolin-1-GFP also accumulated intracellularly, leading us to examine the mechanisms underlying the abnormal localization of the wild type and mutant protein in more detail. We show that both the nature of the tag and cellular context impact the subcellular distribution of caveolin-1, demonstrate that even the wild-type form of caveolin-1 can function as a dominant negative under some conditions, and identify specific conformation changes associated with incorrectly targeted forms of the protein. In addition, we find intracellular caveolin-1 is phosphorylated on Tyr14, but phosphorylation is not required for mistrafficking of the protein. These findings identify novel properties of mistargeted forms of caveolin-1 and raise the possibility that common trafficking defects underlie diseases associated with overexpression and mutations in caveolin-1.

Indexed as

Mutation, MissensePhenotypeAnimalsBreast NeoplasmsCaveolin 1Chlorocebus aethiopsCOS CellsFemaleHeLa CellsHumansPhosphorylationProtein ConformationProtein TransportCaveolin 1

Identifiers

PMID23469926
PMCPMC3674505
OpenAlexW1834307561

What OpenQuestion holds

Textmetadata
LicenceTDM
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.