Evidence map›Paper›PMID 20040600›Full record

ArticleThe Journal of biological chemistry2010

Direct observation and quantitative analysis of Lck exchange between plasma membrane and cytosol in living T cells.

Lars Zimmermann, Wolfgang Paster, Julian Weghuber, Paul Eckerstorfer, Hannes Stockinger, Gerhard J Schütz

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
1.7field-weighted citation impact, top 18% 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, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. T cell receptor (TCR) signaling in health and disease.Signal transduction and targeted therapy · 2021
    Review
  7. Lck bound to coreceptor is less active than free Lck.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Targeting protein lipidation in disease.Trends in molecular medicine · 2012
    Review
  19. Review
  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

6 authors at 2 institutions in 1 country.

Lars ZimmermannBiophysics Institute, Johannes Kepler University Linz, Altenbergerstrasse 69, A-4040 Linz, Austria.
Wolfgang Paster
Julian Weghuber
Paul Eckerstorfer
Hannes Stockinger
Gerhard J Schütz
Johannes Kepler University of Linz · ATMedical University of Vienna · AT

Funding

Austrian Science Fund FWF Y 250
6 · The paper itself

Abstract

Palmitoylation represents a common motif for anchorage of cytosolic proteins to the plasma membrane. Being reversible, it allows for controlled exchange between cytosolic and plasma membrane-bound subpopulations. In this study, we present a live cell single molecule approach for quantifying the exchange kinetics of plasma membrane and cytosolic populations of fluorescently labeled Lck, the key Src family kinase involved in early T cell signaling. Total internal reflection (TIR) fluorescence microscopy was employed for confining the analysis to membrane-proximal molecules. Upon photobleaching Lck-YFP in TIR configuration, fluorescence recovery proceeds first via the cytosol outside of the evanescent field, so that in the early phase fluorescence signal arises predominantly from membrane-proximal cytosolic Lck. The diffusion constant of each molecule allowed us to distinguish whether the molecule has already associated with the plasma membrane or was still freely diffusing in the cytosol. From the number of molecules that inserted during the recovery time we quantified the insertion kinetics: on average, membrane-proximal molecules within the evanescent field needed approximately 400 ms to be inserted. The average lifetime of Lck in the plasma membrane was estimated at 50 s; together with the mobility of 0.26 microm(2)/s this provides sufficient time to explore the surface of the whole T cell before dissociation into the cytosol. Experiments on palmitoylation-deficient Lck mutants yielded similar on-rates, but substantially increased off-rates. We discuss our findings based on a model for the plasma membrane association and dissociation kinetics of Lck, which accounts for reversible palmitoylation on cysteine 3 and 5.

Indexed as

Cell MembraneCytosolCysteineDiffusionHumansJurkat CellsKineticsLymphocyte Specific Protein Tyrosine Kinase p56(lck)Microscopy, FluorescencePalmitatesProtein Processing, Post-TranslationalProtein TransportSignal TransductionT-LymphocytesCysteineLymphocyte Specific Protein Tyrosine Kinase p56(lck)Palmitates

Identifiers

PMID20040600
PMCPMC2825400
OpenAlexW2013829463

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.