Evidence map›Paper›PMID 24655512›Full record

ArticleBiophysical journal2014

Probing the U-shaped conformation of caveolin-1 in a bilayer.

Huan Rui, Kyle T Root, Jinwoo Lee, Kerney Jebrell Glover, Wonpil Im

Abstract read
In one paragraph

Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
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

23 citing papers in PubMed.

  1. Article
  2. Caveolin assemblies displace one bilayer leaflet to organize and bend membranes.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Membrane Compartmentalization and Scaffold Proteins in Leukocyte Migration.Frontiers in cell and developmental biology · 2020
    Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Unraveling the architecture of caveolae.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  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

5 authors.

Huan RuiDepartment of Molecular Biosciences and Center for Bioinformatics, The University of Kansas, Lawrence, Kansas.
Kyle T RootDepartment of Chemistry, Lehigh University, Bethlehem, Pennsylvania.
Jinwoo LeeDepartment of Chemistry, Lehigh University, Bethlehem, Pennsylvania.
Kerney Jebrell GloverDepartment of Chemistry, Lehigh University, Bethlehem, Pennsylvania. Electronic address: kjg206@lehigh.edu.
Wonpil ImDepartment of Molecular Biosciences and Center for Bioinformatics, The University of Kansas, Lawrence, Kansas. Electronic address: wonpil@ku.edu.

Funding

TrainingP41GM103712 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FAEDER, JAMES · 2012 to 2021
$16.3M
Investigation of Caveolin Structure, Topology, and OligomerizationR01GM093258 · NIGMS · LEHIGH UNIVERSITY · PI GLOVER, KERNEY JEBRELL · 2012 to 2016
$1.7M
NIGMS NIH HHS P41 GM103712NIGMS NIH HHS P41GM103712-S1NIGMS NIH HHS R01 GM093258NIGMS NIH HHS R01 GM093258-03
6 · The paper itself

Abstract

Caveolin induces membrane curvature and drives the formation of caveolae that participate in many crucial cell functions such as endocytosis. The central portion of caveolin-1 contains two helices (H1 and H2) connected by a three-residue break with both N- and C-termini exposed to the cytoplasm. Although a U-shaped configuration is assumed based on its inaccessibility by extracellular matrix probes, caveolin structure in a bilayer remains elusive. This work aims to characterize the structure and dynamics of caveolin-1 (D82-S136; Cav182-136) in a DMPC bilayer using NMR, fluorescence emission measurements, and molecular dynamics simulations. The secondary structure of Cav182-136 from NMR chemical shift indexing analysis serves as a guideline for generating initial structural models. Fifty independent molecular dynamics simulations (100 ns each) are performed to identify its favorable conformation and orientation in the bilayer. A representative configuration was chosen from these multiple simulations and simulated for 1 μs to further explore its stability and dynamics. The results of these simulations mirror those from the tryptophan fluorescence measurements (i.e., Cav182-136 insertion depth in the bilayer), corroborate that Cav182-136 inserts in the membrane with U-shaped conformations, and show that the angle between H1 and H2 ranges from 35 to 69°, and the tilt angle of Cav182-136 is 27 ± 6°. The simulations also reveal that specific faces of H1 and H2 prefer to interact with each other and with lipid molecules, and these interactions stabilize the U-shaped conformation.

Indexed as

Molecular Dynamics SimulationAmino Acid SequenceCaveolin 1DimyristoylphosphatidylcholineLipid BilayersMolecular Sequence DataProtein BindingProtein Structure, TertiaryCaveolin 1DimyristoylphosphatidylcholineLipid Bilayers

Identifiers

PMID24655512
PMCPMC3984989

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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.