Evidence map›Paper›PMID 10833523›Full record

ArticleThe Journal of biological chemistry2000

Palmitoylation of caveolin-1 is required for cholesterol binding, chaperone complex formation, and rapid transport of cholesterol to caveolae.

A Uittenbogaard, E J Smart

RetractedOpen access · hybridAbstract readRetracted Publication
PubMed Publisher
In one paragraph

Article in The Journal of biological chemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

58 citing papers in PubMed, 174 citations in OpenAlex.

  1. MAVS Cys508 palmitoylation promotes its aggregation on the mitochondrial outer membrane and antiviral innate immunity.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Review
  4. Caveolin-1: An Oxidative Stress-Related Target for Cancer Prevention.Oxidative medicine and cellular longevity · 2017
    Review
  5. From embryonic development to human diseases: The functional role of caveolae/caveolin.Birth defects research. Part C, Embryo today : reviews · 2016
    Review
  6. There Is No Simple Model of the Plasma Membrane Organization.Frontiers in cell and developmental biology · 2016
    Review
  7. Article
  8. Article
  9. Article
  10. Channelopathies from mutations in the cardiac sodium channel protein complex.Journal of molecular and cellular cardiology · 2013
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Regulation of cholesterol homeostasis.Cellular and molecular life sciences : CMLS · 2012
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

A UittenbogaardDepartment of Physiology, University of Kentucky Medical School, Lexington 40536, USA.
E J Smart
University of Kentucky · US

Funding

CAVEOLAE MEDIATED REGULATION OF ATHEROGENESISR01HL058475 · NHLBI · UNIVERSITY OF KENTUCKY · PI SMART, ERIC J · 1999 to 2000
$105k
CAVEOLAE MEDIATED REGULATION OF ATHEROGENESISR29HL058475 · NHLBI · UNIVERSITY OF KENTUCKY · PI SMART, ERIC J · 1997 to 1998
–
NHLBI NIH HHS HL58475
6 · The paper itself

Abstract

We previously demonstrated that a caveolin-chaperone complex transports newly synthesized cholesterol from the endoplasmic reticulum through the cytoplasm to caveolae. Caveolin-1 has a 33-amino acid hydrophobic domain and three sites of palmitoylation in proximity to the hydrophobic domain. In the present study, we hypothesized that palmitoylation of caveolin-1 is necessary for binding of cholesterol, formation of a caveolin-chaperone transport complex, and rapid, direct transport of cholesterol to caveolae. To test this hypothesis, four caveolin-1 constructs were generated that substituted an alanine for a cysteine at position 133, 143, or 156 or all three sites (triple mutant). These mutated caveolins and wild type caveolin-1 were stably expressed in the lymphoid cell line, L1210-JF, which does not express caveolin-1, does not form a caveolin-chaperone complex, and does not transport newly synthesized cholesterol to caveolae. All of the caveolins were expressed and the proteins localized to plasma membrane caveolae. Wild type caveolin-1 and mutant 133 assembled into complete transport complexes and rapidly (10-20 min) transported cholesterol to caveolae. Caveolin mutants 143 and 156 did not assemble into complete transport complexes, weakly associated with cholesterol, and transported small amounts of cholesterol to caveolae. The triple mutant did not assemble into complete transport complexes and did not associate with cholesterol. We conclude that palmitoylation of caveolin-1 at positions 143 and 156 is required for cholesterol binding and transport complex formation.

Indexed as

CaveolinsAnimalsBiological TransportCaveolin 1Cell LineCell MembraneCholesterolChromatography, Thin LayerDNA, ComplementaryElectrophoresis, Polyacrylamide GelHumansImmunoblottingLymphocytesMembrane ProteinsMiceMutagenesisCAV1 protein, humanCav1 protein, mouseCaveolin 1CaveolinsCholesterolDNA, ComplementaryMembrane ProteinsPalmitates

Identifiers

PMID10833523
OpenAlexW2006506278

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.