Evidence map›Paper›PMID 20661443›Full record

ArticlePloS one2010

Adhesion and degranulation promoting adapter protein (ADAP) is a central hub for phosphotyrosine-mediated interactions in T cells.

Marc Sylvester, Stefanie Kliche, Sabine Lange, Sabine Geithner, Clementine Klemm, Andreas Schlosser, Arndt Grossmann, Ulrich Stelzl, Burkhart Schraven, Eberhard Krause and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

21 citing papers in PubMed, 40 citations in OpenAlex.

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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

11 authors at 5 institutions in 1 country.

Marc SylvesterProtein Engineering Group, Leibniz-Institut für Molekulare Pharmakologie (FMP), Berlin, Germany.
Stefanie Kliche
Sabine Lange
Sabine Geithner
Clementine Klemm
Andreas Schlosser
Arndt Grossmann
Ulrich Stelzl
Burkhart Schraven
Eberhard Krause
Christian Freund
Leibniz-Forschungsinstitut für Molekulare Pharmakologie · DEMax Planck Institute for Molecular Genetics · DEOtto-von-Guericke University Magdeburg · DECharité - Universitätsmedizin Berlin · DEFreie Universität Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TCR stimulation leads to an increase in cellular adhesion among other outcomes. The adhesion and degranulation promoting adapter protein (ADAP) is known to be rapidly phosphorylated after T cell stimulation and relays the TCR signal to adhesion molecules of the integrin family. While three tyrosine phosphorylation sites have been characterized biochemically, the binding capabilities and associated functions of several other potential phosphotyrosine motifs remain unclear. Here, we utilize in vitro phosphorylation and mass spectrometry to map novel phosphotyrosine sites in the C-terminal part of human ADAP (486-783). Individual tyrosines were then mutated to phenylalanine and their relevance for cellular adhesion and migration was tested experimentally. Functionally important tyrosine residues include two sites within the folded hSH3 domains of ADAP and two at the C-terminus. Furthermore, using a peptide pulldown approach in combination with stable isotope labeling in cell culture (SILAC) we identified SLP-76, PLCgamma, PIK3R1, Nck, CRK, Gads, and RasGAP as phospho-dependent binding partners of a central YDDV motif of ADAP. The phosphorylation-dependent interaction between ADAP and Nck was confirmed by yeast two-hybrid analysis, immunoprecipitation and binary pulldown experiments, indicating that ADAP directly links integrins to modulators of the cytoskeleton independent of SLP-76.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid MotifsCell AdhesionCell MovementHumansJurkat CellsOncogene ProteinsPhosphorylationPhosphotyrosineProtein BindingSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationT-LymphocytesTwo-Hybrid System TechniquesTyrosineAdaptor Proteins, Signal TransducingFYB1 protein, humanNck proteinOncogene ProteinsPhosphotyrosineTyrosine

Identifiers

PMID20661443
PMCPMC2908683
OpenAlexW2024267421

What OpenQuestion holds

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LicenceCC BY
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.