Evidence map›Paper›PMID 20082308›Full record

ArticleProtein science : a publication of the Protein Society2010

The adapter protein Nck: role of individual SH3 and SH2 binding modules for protein interactions in T lymphocytes.

Marcus Lettau, Jennifer Pieper, Alyn Gerneth, Beate Lengl-Janssen, Matthias Voss, Andreas Linkermann, Hendrik Schmidt, Christoph Gelhaus, Matthias Leippe, Dieter Kabelitz and 1 more

2 registry-linked trialsOpen access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to 2 registered trials, which are not on this map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 19% 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.

NCT05218434 phase1completednot on this mapstarted 2021, after this paper: background citation

A Randomised, Double-blind, Placebo-controlled, Study of the Safety, Tolerability, and Pharmacokinetics of AX-158 Following Administration of Single and, Multiple Ascending Oral Doses and Food Effect Sub-study in Healthy Male Volunteers

TypeinterventionalSponsorArtax Biopharma IncRan2021 to 2022Enrolled64ConditionsAutoimmune DiseasesArmsAX-158
NCT05725057 phase1 / phase2completednot on this mapstarted 2023, after this paper: background citation

A Phase 2a, Proof of Concept Study Evaluating the Safety and Tolerability of AX-158 in Patients With Mild to Moderate Plaque Psoriasis

TypeinterventionalSponsorArtax Biopharma IncRan2023 to 2024Enrolled31ConditionsPsoriasis, Plaque PsoriasisArmsAX-158, Placebo
3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 44 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. T cell receptor (TCR) signaling in health and disease.Signal transduction and targeted therapy · 2021
    Review
  6. Sinner or Saint?: Nck Adaptor Proteins in Vascular Biology.Frontiers in cell and developmental biology · 2021
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. PSF: nuclear busy-body or nuclear facilitator?Wiley interdisciplinary reviews. RNA
    Review
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

11 authors at 1 institution in 1 country.

Marcus LettauMolecular Immunology, Institute for Immunology, Christian-Albrechts University, D-24105 Kiel, Germany. lettau@immunologie.uni-kiel.de
Jennifer Pieper
Alyn Gerneth
Beate Lengl-Janssen
Matthias Voss
Andreas Linkermann
Hendrik Schmidt
Christoph Gelhaus
Matthias Leippe
Dieter Kabelitz
Ottmar Janssen
Kiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nck is a ubiquitously expressed, primarily cytosolic adapter protein consisting of one SH2 domain and three SH3 domains. It links receptor and nonreceptor tyrosine kinases to actin cytoskeleton reorganizing proteins. In T lymphocytes, Nck is a crucial component of signaling pathways for T cell activation and effector function. It recruits actin remodeling proteins to T cell receptor (TCR)-associated activation clusters and thereby initiates changes in cell polarity and morphology. Moreover, Nck is crucial for the TCR-induced mobilization of secretory vesicles to the cytotoxic immunological synapse. To identify the interactome of Nck in human T cells, we performed a systematic screen for interaction partners in untreated or pervanadate-treated cells. We used GST fusion proteins containing full length Nck, the combined SH3 domains or the individual SH3 and SH2 domains to precipitate putative Nck interactors from cellular lysates. Protein bands were excised from gels, processed by tryptic in-gel digestion and analyzed by mass spectrometry. Using this approach, we confirmed previously established interactions (e.g., with Slp76, CD3 epsilon, WASP, and WIPF1) and identified several novel putative Nck-binding proteins. We subsequently verified the SH2 domain binding to the actin-binding protein HIP55 and to FYB/ADAP, and the SH3-mediated binding to the nuclear proteins SFPQ/NONO. Using laser scanning microscopy, we provide new evidence for a nuclear localization of Nck in human T cells. Our data highlight the fundamental role of Nck in the TCR-to-cytoskeleton crosstalk and point to yet unknown nuclear functions of Nck also in T lymphocytes.

Indexed as

src Homology DomainsAdaptor Proteins, Signal TransducingBinding SitesHumansJurkat CellsMicroscopy, ConfocalOncogene ProteinsReceptors, Antigen, T-CellT-LymphocytesAdaptor Proteins, Signal TransducingNck proteinOncogene ProteinsReceptors, Antigen, T-Cell

Identifiers

PMID20082308
PMCPMC2867007
OpenAlexW1990633607

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.