Evidence map›Paper›PMID 11566789›Full record

ArticleBiophysical journal2001

Binding of cross-linked glycosylphosphatidylinositol-anchored proteins to discrete actin-associated sites and cholesterol-dependent domains.

K Suzuki, M P Sheetz

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Signaling clusters in the cell membrane.Current opinion in cell biology · 2011
    Review
  5. Membrane domains and flagellar pocket boundaries are influenced by the cytoskeleton in African trypanosomes.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  6. Activation of T cells by cross-linking Qa-2, the ped gene product, requires Fyn.American journal of reproductive immunology (New York, N.Y. : 1989) · 2007
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  14. Article
  15. 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

2 authors at 1 institution in 1 country.

K SuzukiDepartment of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710, USA.
M P Sheetz
Duke University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mechanism by which cross-linked glycosylphosphatidylinositol (GPI)-anchored proteins are immobilized has been a mystery because both the binding to a transmembrane protein and attachment to a rigid cytoskeleton are needed. Using laser tweezers surface scanning resistance (SSR) technology, we obtained physical evidence for cross-linked GPI-anchored protein, Qa-2, binding to a transmembrane protein and for diffusion to discrete cytoskeleton attachment sites. At low levels of cross-linking of Qa-2 molecules, the resistance to lateral movement was that expected of monomeric lipid-anchored proteins, and no specific binding to cytoskeleton-attached structures was observed. When aggregates of the GPI-anchored protein, Qa-2, were scanned across plasma membranes, the background resistance was much higher than expected for a GPI-anchored protein alone and submicron domains of even higher resistance were observed (designated as elastic or non-elastic barriers) at a density of 82 (61 elastic and 21 small non-elastic barriers) per 100 microm(2). Elastic barriers involved weak but specific bonds to the actin cytoskeleton (broken by forces of 2 or 4 pN and were removed by cytochalasin D). Small non-elastic barriers (50-100 nm) depended upon membrane cholesterol and were closely correlated with caveolae density. Thus, cross-linked GPI-anchored proteins can diffuse through the membrane in complex with a transmembrane protein and bind weakly to discrete cytoskeleton attachment sites either associated with flexible actin networks or sphingolipid-cholesterol rich microdomains in live cell membranes. Our SSR measurements provide the first description of the physical characteristics of the interactions between rafts and stable membrane structures.

Indexed as

ActinsAnimalsBinding SitesCarcinoma, HepatocellularCaveolaeCell MembraneCholesterolCross-Linking ReagentsCytoskeletonFluoresceinGlycosylphosphatidylinositolsHistocompatibility Antigens Class IMiceMicroscopy, ConfocalPhosphatidylethanolaminesProtein Structure, TertiaryActinsCholesterolCross-Linking ReagentsFluoresceinGlycosylphosphatidylinositolsHistocompatibility Antigens Class IPhosphatidylethanolaminesQ surface antigens

Identifiers

PMID11566789
PMCPMC1301690
OpenAlexW2090456368

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.