Evidence map›Paper›PMID 11959995›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Modulation of protein translation by Nck-1.

Sem Kebache, Dongmei Zuo, Eric Chevet, Louise Larose

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

24 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Nck adaptors at a glance.Journal of cell science · 2021
    Article
  4. Article
  5. Sinner or Saint?: Nck Adaptor Proteins in Vascular Biology.Frontiers in cell and developmental biology · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Nck adapter proteins: functional versatility in T cells.Cell communication and signaling : CCS · 2009
    Article
  15. Evaluation of in vitro cytotoxicity and paracellular permeability of intact monolayers with mouse embryonic stem cells.Toxicology in vitro : an international journal published in association with BIBRA · 2008
    Article
  16. Article
  17. Article
  18. The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  19. Article
  20. Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 2006
    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

4 authors at 1 institution in 2 countries.

Sem KebacheDepartments of Medicine and Surgery, Polypeptide Laboratory, Division of Endocrinology, McGill University, Montreal, QC, Canada H3A 2B2.
Dongmei Zuo
Eric Chevet
Louise Larose
McGill University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In mammals, Nck represented by two genes, is a 47-kDa SH2/SH3 domain-containing protein lacking intrinsic enzymatic function. Here, we reported that the first and the third SH3 domains of Nck-1 interact with the C-terminal region of the beta subunit of the eukaryotic initiation factor 2 (eIF2 beta). Binding of eIF2 beta was specific to the SH3 domains of Nck-1, and in vivo, the interaction Nck/eIF2 beta was demonstrated by reciprocal coimmunoprecipitations. In addition, Nck was detected in a molecular complex with eIF2 beta in an enriched ribosomal fraction, whereas no other SH2/SH3 domain-containing adapters were found. Cell fractionation studies demonstrated that the presence of Nck in purified ribosomal fractions was enhanced after insulin stimulation, suggesting that growth factors dynamically regulate translocation of Nck to ribosomes. In HEK293 cells, we observed that transient overexpression of Nck-1 significantly enhanced Cap-dependent and -independent protein translation. This effect of Nck-1 required the integrity of its first and third SH3 domains originally found to interact with eIF2 beta. Finally, in vitro, Nck-1 also increased protein translation, revealing a direct role for Nck-1 in this process. Our study demonstrates that in addition to mediate receptor tyrosine kinase signaling, Nck-1 modulates protein translation potentially through its direct interaction with an intrinsic component of the protein translation machinery.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell LineDNA, ComplementaryDose-Response Relationship, DrugEukaryotic Initiation Factor-2Gene LibraryHepatocytesHumansInsulinLuciferasesMiceOncogene ProteinsPhosphorylationPrecipitin TestsProtein BindingAdaptor Proteins, Signal TransducingDNA, ComplementaryEukaryotic Initiation Factor-2InsulinLuciferasesNck proteinOncogene ProteinsReceptor, InsulinRecombinant Fusion ProteinsSucrose

Identifiers

PMID11959995
PMCPMC122782
OpenAlexW2043852445

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.