Evidence map›Paper›PMID 12426371›Full record

ArticleThe EMBO journal2002

Dynamic interaction of CD2 with the GYF and the SH3 domain of compartmentalized effector molecules.

Christian Freund, Ronald Kühne, Hailin Yang, Sunghyouk Park, Ellis L Reinherz, Gerhard Wagner

Open access · greenAbstract readComparative Study
In one paragraph

Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
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  12. Article
  13. CD2 Immunobiology.Frontiers in immunology · 2020
    Review
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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 3 institutions in 2 countries.

Christian FreundProtein Engineering Group and Molecular Modeling Group, Forschungsinstitut für Molekulare Pharmakologie and Freie Universität Berlin, Robert-Rössle-Strasse 10, D-13125 Berlin, Germany. freund@fmp-berlin.de
Ronald Kühne
Hailin Yang
Sunghyouk Park
Ellis L Reinherz
Gerhard Wagner
Dana-Farber Cancer Institute · USFreie Universität Berlin · DEHarvard University · US

Funding

T CELL SPECIFIC TRANSCRIPTION COMPLEXESP01GM047467 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1992 to 2017
$28.6M
STRUCTURE BASIS OF IMMUNE-CELL SURFACE RECEPTOR FUNCTIONR01AI037581 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 1996 to 2021
$6.7M
T CELL ANTIGEN RECOGNITIONR37AI019807 · NIAID · DANA-FARBER CANCER INSTITUTE · PI REINHERZ, ELLIS L · 1999 to 2008
$4.4M
WATER IN BACTERIORHODOPSIN, POLYCARBONATE &ORGANIC SOLVENTS: NMRP41RR000995 · NCRR · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI BALEJA, JAMES D · 1985 to 2002
$3.5M
T Cell Antigen RecognitionR01AI019807 · NIAID · DANA-FARBER CANCER INSTITUTE · PI REINHERZ, ELLIS L · 1985 to 2010
$1.3M
T Cell Antigen RecognitionR56AI019807 · NIAID · DANA-FARBER CANCER INST · PI REINHERZ, ELLIS L · 2012 to 2012
$430k
NCRR NIH HHS RR 00995NIAID NIH HHS AI 19807NIAID NIH HHS AI 37581NIAID NIH HHS R01 AI019807NIAID NIH HHS R01 AI037581NIAID NIH HHS R37 AI019807NIAID NIH HHS R56 AI019807NIGMS NIH HHS GM 47467NIGMS NIH HHS P01 GM047467
6 · The paper itself

Abstract

Intracellular protein interaction domains are essential for eukaryotic signaling. In T cells, the CD2BP2 adaptor binds two membrane-proximal proline-rich motifs in the CD2 cytoplasmic tail via its GYF domain, thereby regulating interleukin-2 production. Here we present the structure of the GYF domain in complex with a CD2 tail peptide. Unlike SH3 domains, which use two surface pockets to accommodate proline residues of ligands, the GYF domain employs phylogenetically conserved hydrophobic residues to create a single interaction surface. NMR analysis shows that the Fyn but not the Lck tyrosine kinase SH3 domain competes with CD2BP2 GYF-domain binding to the same CD2 proline-rich sequence in vitro. To test the in vivo significance of this competition, we used co-immunoprecipitation experiments and found that CD2BP2 is the ligand of the membrane-proximal proline-rich tandem repeat of CD2 in detergent-soluble membrane compartments, but is replaced by Fyn SH3 after CD2 is translocated into lipid rafts upon CD2 ectodomain clustering. This unveils the mechanism of a switch of CD2 function due to an extracellular mitogenic signal.

Indexed as

Protein Interaction MappingAdaptor Proteins, Signal TransducingAmino Acid MotifsAmino Acid SequenceBinding, CompetitiveBinding SitesCarrier ProteinsCD2 AntigensCell DivisionHumansHydrophobic and Hydrophilic InteractionsLigandsLymphocyte ActivationLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane MicrodomainsModels, MolecularAdaptor Proteins, Signal TransducingCarrier ProteinsCD2 AntigensCD2BP2 protein, humanFYN protein, humanLigandsLymphocyte Specific Protein Tyrosine Kinase p56(lck)ProlineProto-Oncogene ProteinsProto-Oncogene Proteins c-fyn

Identifiers

PMID12426371
PMCPMC137194
OpenAlexW2171019231

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.