Evidence map›Paper›PMID 16595635›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse.

Marcus Lettau, Jing Qian, Andreas Linkermann, Mathieu Latreille, Louise Larose, Dieter Kabelitz, Ottmar Janssen

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Sinner or Saint?: Nck Adaptor Proteins in Vascular Biology.Frontiers in cell and developmental biology · 2021
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. The effector T cell response to influenza infection.Current topics in microbiology and immunology · 2015
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Cytotoxic immunological synapses.Immunological reviews · 2010
    Review
  17. Review
  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

7 authors at 3 institutions in 2 countries.

Marcus LettauInstitute for Immunology, University Hospital Schleswig-Holstein Campus Kiel, 24105 Kiel, Germany.
Jing Qian
Andreas Linkermann
Mathieu Latreille
Louise Larose
Dieter Kabelitz
Ottmar Janssen
University Hospital Schleswig-Holstein · DEMcGill University · CAUniversity of Lübeck · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Fas ligand (FasL) is a key death factor of cytotoxic T lymphocytes and natural killer cells. It is stored intracellularly as a transmembrane protein of secretory lysosomes. Upon activation, these vesicles are transported to the cytotoxic immunological synapse (IS), and FasL becomes exposed to the cell surface to trigger cell death through ligation of its receptor Fas (CD95) on the target cell. We propose that the FasL-associated adaptor protein Nck is involved in the actin-dependent transport of FasL-bearing secretory lysosomes to the IS. Nck binds to the proline-rich portion of FasL and alters its subcellular distribution when coexpressed in 293T cells. In T lymphocytes, endogenous Nck partially colocalizes with lysosome-associated FasL. When T cell clones or lines are exposed to target cells, both proteins and other components of secretory lysosomes (i.e., granzyme B or cathepsin D) are transported to the cell-cell interface. The present data suggest that T cell receptor engagement provokes a rapid, tyrosine kinase- and actin-dependent transport of Nck-associated FasL-carrying lysosomes to the contact area. Our observations support the previous notion that the unique cytoplasmic tail of FasL is crucial for its directed transport to the cell surface and into the assembling cytotoxic IS.

Indexed as

Adaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsBinding SitesCD4-Positive T-LymphocytesCell LineClone CellsCytotoxicity, ImmunologicFas Ligand ProteinHumansLysosomesMembrane GlycoproteinsOncogene ProteinsProtein BindingRecombinant Fusion ProteinsRecombinant ProteinsT-Lymphocytes, CytotoxicAdaptor Proteins, Signal TransducingApoptosis Regulatory ProteinsFASLG protein, humanFas Ligand ProteinMembrane GlycoproteinsNck proteinOncogene ProteinsRecombinant Fusion ProteinsRecombinant ProteinsTumor Necrosis Factors

Identifiers

PMID16595635
PMCPMC1458672
OpenAlexW1987604347

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.