Evidence map›Paper›PMID 12609909›Full record

ArticleBiophysical journal2003

Cholesterol-induced protein sorting: an analysis of energetic feasibility.

J A Lundbaek, O S Andersen, T Werge, C Nielsen

Open access · bronzeAbstract readEvaluation Study
In one paragraph

Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

60 citing papers in PubMed, 123 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. The in silico human surfaceome.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Hydrophobic compounds reshape membrane domains.PLoS computational biology · 2014
    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

4 authors at 3 institutions in 2 countries.

J A LundbaekInstitute of Biological Psychiatry, Sct. Hans Hospital, Roskilde, DK-4000, Denmark. lundbaek@dadlnet.dk
O S Andersen
T Werge
C Nielsen
Sankt Hans Hospital · DKCornell University · USUniversity of Copenhagen · DK

Funding

Energetics of Channel-Bilayer InteractionsR01GM021342 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI ANDERSEN, OLAF S. · 1985 to 2021
$9.9M
NIGMS NIH HHS GM21342NIGMS NIH HHS R01 GM021342
6 · The paper itself

Abstract

The mechanism(s) underlying the sorting of integral membrane proteins between the Golgi complex and the plasma membrane remain uncertain because no specific Golgi retention signal has been found. Moreover one can alter a protein's eventual localization simply by altering the length of its transmembrane domain (TMD). M. S. Bretscher and S. Munro (SCIENCE: 261:1280-1281, 1993) therefore proposed a physical sorting mechanism based on the hydrophobic match between the proteins' TMD and the bilayer thickness, in which cholesterol would regulate protein sorting by increasing the lipid bilayer thickness. In this model, Golgi proteins with short TMDs would be excluded from cholesterol-enriched domains (lipid rafts) that are incorporated into transport vesicles destined for the plasma membrane. Although attractive, this model remains unproven. We therefore evaluated the energetic feasibility of a cholesterol-dependent sorting process using the theory of elastic liquid crystal deformations. We show that the distribution of proteins between cholesterol-enriched and cholesterol-poor bilayer domains can be regulated by cholesterol-induced changes in the bilayer physical properties. Changes in bilayer thickness per se, however, have only a modest effect on sorting; the major effect arises because cholesterol changes also the bilayer material properties, which augments the energetic penalty for incorporating short TMDs into cholesterol-enriched domains. We conclude that cholesterol-induced changes in the bilayer physical properties allow for effective and accurate sorting which will be important generally for protein partitioning between different membrane domains.

Indexed as

Models, BiologicalModels, MolecularCell MembraneCholesterolComputer SimulationEnergy TransferFeasibility StudiesGolgi ApparatusHydrophobic and Hydrophilic InteractionsLipid BilayersMacromolecular SubstancesMembrane ProteinsMotionProtein ConformationProtein TransportCholesterolLipid BilayersMacromolecular SubstancesMembrane Proteins

Identifiers

PMID12609909
PMCPMC1302776
OpenAlexW2012945956

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.