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Keywords {🔍}

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Topics {✒️}

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WebPage:
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         headline:T cell specific adaptor protein (TSAd) promotes interaction of Nck with Lck and SLP-76 in T cells
         description:The Lck and Src binding adaptor protein TSAd (T cell specific adaptor) regulates actin polymerization in T cells and endothelial cells. The molecular details as to how TSAd regulates this process remain to be elucidated. To identify novel interaction partners for TSAd, we used a scoring matrix-assisted ligand algorithm (SMALI), and found that the Src homology 2 (SH2) domain of the actin regulator Non-catalytic region of tyrosine kinase adaptor protein (Nck) potentially binds to TSAd phosphorylated on Tyr280 (pTyr280) and pTyr305. These predictions were confirmed by peptide array analysis, showing direct binding of recombinant Nck SH2 to both pTyr280 and pTyr305 on TSAd. In addition, the SH3 domains of Nck interacted with the proline rich region (PRR) of TSAd. Pull-down and immunoprecipitation experiments further confirmed the Nck-TSAd interactions through Nck SH2 and SH3 domains. In line with this Nck and TSAd co-localized in Jurkat cells as assessed by confocal microscopy and imaging flow cytometry. Co-immunoprecipitation experiments in Jurkat TAg cells lacking TSAd revealed that TSAd promotes interaction of Nck with Lck and SLP-76, but not Vav1. TSAd expressing Jurkat cells contained more polymerized actin, an effect dependent on TSAd exon 7, which includes interactions sites for both Nck and Lck. TSAd binds to and co-localizes with Nck. Expression of TSAd increases both Nck-Lck and Nck-SLP-76 interaction in T cells. Recruitment of Lck and SLP-76 to Nck by TSAd could be one mechanism by which TSAd promotes actin polymerization in activated T cells.
         datePublished:2015-07-11T00:00:00Z
         dateModified:2015-07-11T00:00:00Z
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            SLP-76
            Cell Biology
            Protein-Ligand Interactions
            Receptors
            Cytokines and Growth Factors
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      headline:T cell specific adaptor protein (TSAd) promotes interaction of Nck with Lck and SLP-76 in T cells
      description:The Lck and Src binding adaptor protein TSAd (T cell specific adaptor) regulates actin polymerization in T cells and endothelial cells. The molecular details as to how TSAd regulates this process remain to be elucidated. To identify novel interaction partners for TSAd, we used a scoring matrix-assisted ligand algorithm (SMALI), and found that the Src homology 2 (SH2) domain of the actin regulator Non-catalytic region of tyrosine kinase adaptor protein (Nck) potentially binds to TSAd phosphorylated on Tyr280 (pTyr280) and pTyr305. These predictions were confirmed by peptide array analysis, showing direct binding of recombinant Nck SH2 to both pTyr280 and pTyr305 on TSAd. In addition, the SH3 domains of Nck interacted with the proline rich region (PRR) of TSAd. Pull-down and immunoprecipitation experiments further confirmed the Nck-TSAd interactions through Nck SH2 and SH3 domains. In line with this Nck and TSAd co-localized in Jurkat cells as assessed by confocal microscopy and imaging flow cytometry. Co-immunoprecipitation experiments in Jurkat TAg cells lacking TSAd revealed that TSAd promotes interaction of Nck with Lck and SLP-76, but not Vav1. TSAd expressing Jurkat cells contained more polymerized actin, an effect dependent on TSAd exon 7, which includes interactions sites for both Nck and Lck. TSAd binds to and co-localizes with Nck. Expression of TSAd increases both Nck-Lck and Nck-SLP-76 interaction in T cells. Recruitment of Lck and SLP-76 to Nck by TSAd could be one mechanism by which TSAd promotes actin polymerization in activated T cells.
      datePublished:2015-07-11T00:00:00Z
      dateModified:2015-07-11T00:00:00Z
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      pageEnd:14
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         TSAd
         T cell specific adaptor protein
         Nck
         Lck
         SH2 domain
         adaptor protein
         SH2D2A
         SLP-76
         Cell Biology
         Protein-Ligand Interactions
         Receptors
         Cytokines and Growth Factors
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            name:Vibeke Sundvold-Gjerstad
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            name:Stine Granum
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            address:
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      name:Vibeke Sundvold-Gjerstad
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            name:Institute of Basic Medical Sciences, University of Oslo
            address:
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               type:PostalAddress
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      name:Greger Abrahamsen
      affiliation:
            name:Institute of Basic Medical Sciences, University of Oslo
            address:
               name:Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
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      name:Laszlo Buday
      affiliation:
            name:Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences
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            address:
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               type:PostalAddress
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      email:[email protected]
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      name:Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
      name:Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
      name:Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
      name:Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
      name:Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
      name:Institute of Enzymology, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary
      name:Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway
      name:Institute of Basal Medical Sciences, University of Oslo, Blindern, Norway

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