Evidence map›Paper›PMID 19496615›Full record

ArticleBiochemistry2009

IgE receptor-mediated alteration of membrane-cytoskeleton interactions revealed by mass spectrometric analysis of detergent-resistant membranes.

Xuemei Han, Norah L Smith, Dwaipayan Sil, David A Holowka, Fred W McLafferty, Barbara A Baird

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Proteomic Analysis of Lipid Rafts from RBL-2H3 Mast Cells.International journal of molecular sciences · 2019
    Article
  2. Thy-1, a Pathfinder Protein for the Post-genomic Era.Frontiers in cell and developmental biology · 2018
    Review
  3. The Continuing Mystery of Lipid Rafts.Journal of molecular biology · 2016
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Lipid rafts in mast cell biology.Journal of lipids · 2011
    Article
  10. 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

6 authors at 1 institution in 1 country.

Xuemei HanDepartment of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA.
Norah L Smith
Dwaipayan Sil
David A Holowka
Fred W McLafferty
Barbara A Baird
Cornell University · US

Funding

STUCTURE-FUNCTION RELATIONSHIPS OF IMMUNORECEPTORSR01AI018306 · NIAID · CORNELL UNIVERSITY ITHACA · PI BAIRD, BARBARA A · 1985 to 2014
$5.3M
MASS SPECTROMETRY IN BIOMEDICAL RESEARCHR01GM016609 · NIGMS · CORNELL UNIVERSITY ITHACA · PI MC LAFFERTY, FRED WARREN · 1985 to 2010
$1.9M
MASS SPECTROMETRY IN BIOMEDICAL RESEARCHR37GM016609 · NIGMS · CORNELL UNIVERSITY ITHACA · PI MC LAFFERTY, FRED W · 1992 to 2001
$639k
NIAID NIH HHS AI018306NIAID NIH HHS R01 AI018306NIGMS NIH HHS GM016609NIGMS NIH HHS R01 GM016609NIGMS NIH HHS R37 GM016609
6 · The paper itself

Abstract

We use electrospray ionization mass spectrometry to quantify >100 phospholipid (PL) components in detergent-resistant membrane (DRM) domains that are related to ordered membrane compartments commonly known as lipid rafts. We previously compared PL compositions of DRMs with plasma membrane vesicles and whole cell lipid extracts from RBL mast cells, and we made the initial observation that antigen stimulation of IgE receptors (FcepsilonRI) causes a significant change in the PL composition of DRMs [Fridriksson, E. K., et al. (1999) Biochemistry 38, 8056-8063]. We now characterize the signaling requirements and time course for this change, which is manifested as an increase in the recovery of polyunsaturated PL in DRM, particularly in phosphatidylinositol species. We find that this change is largely independent of tyrosine phosphorylation, stimulated by engagement of FcepsilonRI, and can be activated by Ca(2+) ionophore in a manner independent of antigen stimulation. Unexpectedly, we found that inhibitors of actin polymerization (cytochalasin D and latrunculin A) cause a similar, but more rapid, change in the PL composition of DRMs in the absence of FcepsilonRI activation, indicating that perturbations in the actin cytoskeleton affect the organization of plasma membrane domains. Consistent with this interpretation, a membrane-permeable stabilizer of F-actin, jasplakinolide, prevents antigen-stimulated changes in DRM PL composition. These results are confirmed by a detailed analysis of multiple experiments, showing that receptor and cytochalasin D-stimulated changes in DRM lipid composition follow first-order kinetics. Analysis in terms of the number of double bonds in the fatty acid chains is valid for total PL of the major headgroups and for headgroups individually. In this manner, we show that, on average, concentrations of saturated or monounsaturated PL decrease in the DRM, whereas concentrations of PL with two or more double bonds (polyunsaturated PL) increase due to cytoskeletal perturbation. We find that these changes are independent of fatty acid chain length. Our mass spectrometric analyses provide a detailed accounting of receptor-activated alterations in the plasma membrane that are regulated by the actin cytoskeleton.

Indexed as

Cell MembraneCytoskeletonDetergentsKineticsPhospholipidsReceptors, IgESpectrometry, Mass, Electrospray IonizationDetergentsPhospholipidsReceptors, IgE

Identifiers

PMID19496615
PMCPMC2767325
OpenAlexW2028557317

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.