Evidence map›Paper›PMID 16847311›Full record

ArticleMolecular and cellular biology2006

Association between SAP and FynT: Inducible SH3 domain-mediated interaction controlled by engagement of the SLAM receptor.

Riyan Chen, Sylvain Latour, Xiaochu Shi, André Veillette

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-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

14 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
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  5. The Immunomodulatory Functions of Diacylglycerol Kinase ζ.Frontiers in cell and developmental biology · 2016
    Review
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
  12. Review
  13. Itk tyrosine kinase substrate docking is mediated by a nonclassical SH2 domain surface of PLCgamma1.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  14. 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

4 authors at 2 institutions in 3 countries.

Riyan ChenLaboratory of Molecular Oncology, Clinical Research Institute of Montreal, Montréal, Québec, Canada.
Sylvain Latour
Xiaochu Shi
André Veillette
Clinical Research Institute · USHôpital Necker-Enfants Malades · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SAP is an intracellular adaptor molecule composed almost exclusively of an SH2 domain. It is mutated in patients with X-linked lymphoproliferative disease, a human immunodeficiency. Several immune abnormalities were also identified in SAP-deficient mice. By way of its SH2 domain, SAP interacts with tyrosine-based motifs in the cytoplasmic domain of SLAM family receptors. SAP promotes SLAM family receptor-induced protein tyrosine phosphorylation, due to its capacity to recruit the Src-related kinase FynT. This unusual property relies on the existence of a second binding surface in the SAP SH2 domain, centered on arginine 78 of SAP, that binds directly to the FynT SH3 domain. Herein, we wanted to further understand the mechanisms controlling the interaction between SLAM-SAP and FynT. Our experiments showed that, unlike conventional associations mediated by SH3 domains, the interaction of the FynT SH3 domain with SLAM-SAP was strictly inducible. It was absolutely dependent on engagement of SLAM by extracellular ligands. We obtained evidence that this inducibility was not due to increased binding of SLAM to SAP following SLAM engagement. Furthermore, it could occur independently of any appreciable SLAM-dependent biochemical signal. In fact, our data indicated that the induced association of the FynT SH3 domain with SLAM-SAP was triggered by a change in the conformation of SLAM-associated SAP caused by SLAM engagement. Together, these data elucidate further the events initiating SLAM-SAP signaling in immune cells. Moreover, they identify a strictly inducible interaction mediated by an SH3 domain.

Indexed as

src Homology DomainsAdaptor Proteins, Signal TransducingAnimalsAntigens, CDCell LineGlycoproteinsHumansImmunoglobulinsIntracellular Signaling Peptides and ProteinsMiceMice, KnockoutMultiprotein ComplexesProtein BindingProto-Oncogene Proteins c-fynReceptors, Cell SurfaceRecombinant ProteinsAdaptor Proteins, Signal TransducingAntigens, CDGlycoproteinsImmunoglobulinsIntracellular Signaling Peptides and ProteinsMultiprotein ComplexesProto-Oncogene Proteins c-fynReceptors, Cell SurfaceRecombinant ProteinsSignaling Lymphocytic Activation Molecule Family Member 1Tyrosine

Identifiers

PMID16847311
PMCPMC1592776
OpenAlexW2104182629

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.