Evidence map›Paper›PMID 22631607›Full record

ArticleJournal of the American Chemical Society2012

Monitoring lipid anchor organization in cell membranes by PIE-FCCS.

Sara B Triffo, Hector H Huang, Adam W Smith, Eldon T Chou, Jay T Groves

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. 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
3.5field-weighted citation impact, top 7% 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

23 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Clustering of the ζ-Chain Can Initiate T Cell Receptor Signaling.International journal of molecular sciences · 2020
    Article
  7. Review
  8. Article
  9. Article
  10. With or without rafts? Alternative views on cell membranes.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  11. Article
  12. Article
  13. Article
  14. E-cadherin junction formation involves an active kinetic nucleation process.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. H-Ras forms dimers on membrane surfaces via a protein-protein interface.Proceedings of the National Academy of Sciences of the United States of America · 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

5 authors at 3 institutions in 1 country.

Sara B TriffoHoward Hughes Medical Institute, Department of Chemistry, University of California, Berkeley, California 94720, USA.
Hector H Huang
Adam W Smith
Eldon T Chou
Jay T Groves
Howard Hughes Medical Institute · USLawrence Berkeley National Laboratory · USUniversity of California, Berkeley · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

This study examines the dynamic co-localization of lipid-anchored fluorescent proteins in living cells using pulsed-interleaved excitation fluorescence cross-correlation spectroscopy (PIE-FCCS) and fluorescence lifetime analysis. Specifically, we look at the pairwise co-localization of anchors from lymphocyte cell kinase (LCK: myristoyl, palmitoyl, palmitoyl), RhoA (geranylgeranyl), and K-Ras (farnesyl) proteins in different cell types. In Jurkat cells, a density-dependent increase in cross-correlation among RhoA anchors is observed, while LCK anchors exhibit a more moderate increase and broader distribution. No correlation was detected among K-Ras anchors or between any of the different anchor types studied. Fluorescence lifetime data reveal no significant Förster resonance energy transfer in any of the data. In COS 7 cells, minimal correlation was detected among LCK or RhoA anchors. Taken together, these observations suggest that some lipid anchors take part in anchor-specific co-clustering with other existing clusters of native proteins and lipids in the membrane. Importantly, these observations do not support a simple interpretation of lipid anchor-mediated organization driven by partitioning based on binary lipid phase separation.

Indexed as

AnimalsCell MembraneChlorocebus aethiopsCOS CellsFluorescence Resonance Energy TransferHumansJurkat CellsLipid BilayersLipid-Linked ProteinsLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane MicrodomainsSpectrometry, FluorescenceLipid BilayersLipid-Linked ProteinsLymphocyte Specific Protein Tyrosine Kinase p56(lck)

Identifiers

PMID22631607
PMCPMC3626236
OpenAlexW2048672868

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.