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We are analyzing https://link.springer.com/article/10.1186/1478-811x-7-1.

Title:
Nck adapter proteins: functional versatility in T cells | Cell Communication and Signaling
Description:
Nck is a ubiquitously expressed adapter protein that is almost exclusively built of one SH2 domain and three SH3 domains. The two isoproteins of Nck are functionally redundant in many aspects and differ in only few amino acids that are mostly located in the linker regions between the interaction modules. Nck proteins connect receptor and non-receptor tyrosine kinases to the machinery of actin reorganisation. Thereby, Nck regulates activation-dependent processes during cell polarisation and migration and plays a crucial role in the signal transduction of a variety of receptors including for instance PDGF-, HGF-, VEGF- and Ephrin receptors. In most cases, the SH2 domain mediates binding to the phosphorylated receptor or associated phosphoproteins, while SH3 domain interactions lead to the formation of larger protein complexes. In T lymphocytes, Nck plays a pivotal role in the T cell receptor (TCR)-induced reorganisation of the actin cytoskeleton and the formation of the immunological synapse. However, in this context, two different mechanisms and adapter complexes are discussed. In the first scenario, dependent on an activation-induced conformational change in the CD3ε subunits, a direct binding of Nck to components of the TCR/CD3 complex was shown. In the second scenario, Nck is recruited to the TCR complex via phosphorylated Slp76, another central constituent of the membrane proximal activation complex. Over the past years, a large number of putative Nck interactors have been identified in different cellular systems that point to diverse additional functions of the adapter protein, e.g. in the control of gene expression and proliferation.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Education
  • Science
  • Telecommunications

Content Management System {📝}

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Custom-built

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What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
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How Does Link.springer.com Make Money? {💸}

We find it hard to spot revenue streams.

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Keywords {🔍}

nck, pubmed, article, google, scholar, cas, cell, protein, activation, cells, biol, domain, receptor, binding, kinase, proteins, signaling, central, factor, phosphorylation, interaction, cdε, tcr, adapter, domains, chem, complex, tyrosine, actin, pak, slp, family, wasp, interactions, partners, mol, adaptor, growth, interacts, immunol, expression, src, role, cytoskeleton, recruitment, sap, jbc, kinases, cellular, function,

Topics {✒️}

wiskott-aldrich syndrome protein c-jun nh2-terminal kinase c-jun n-terminal kinase t-cell receptor-mediated activation wild-type double-positive cells jennifer pieper & ottmar janssen platelet-derived growth factor superantigen-pulsed b-lcl tek/tie2 receptor signals pak/pix/git complex translocates article download pdf ebv-transformed b-lcl alexafluor546-conjugated secondary reagents p21-activated kinase-binding proteins pak-interacting exchange factor type-2-transmembrane protein belonging t-cell receptor independent ubiquitin ligase c-cbl cell receptor-induced apoptosis disease-causing sap mutants mesoderm-derived embryonic structures ch/tools/sim-prot syk-type kinase zap70 insulin receptor-related receptor ras-related gtpase ral cd4+cd8+ thymocytes influenced extended proline-rich stretch threshold-dependent cell polarity full size image serine-threonine kinase pak1 ras-dependent gene expression immature cd4+cd8+ thymocytes cd3ε-null background developed numerous protein-protein interactions low-avidity tcr signaling activated receptor-tyrosine kinases mutated proline-rich sequence immature cd4+cd8+ cells phospho-tyrosine residue py751 growth factor-1 receptor n-terminal sh3 domain wasp-wave protein network tcr-induced tyrosine phosphorylation slap/cd3ε prs-dependent degradation hepatocyte growth factor regulated activation-dependent reorganization small rho-gtpase cdc42 bokoch gm preselection cd4+cd8+ thymocytes nuclear nck-interacting proteins

Questions {❓}

  • Pitcher LA, van Oers NS: T-cell receptor signal transmission: who gives an ITAM?

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Nck adapter proteins: functional versatility in T cells
         description:Nck is a ubiquitously expressed adapter protein that is almost exclusively built of one SH2 domain and three SH3 domains. The two isoproteins of Nck are functionally redundant in many aspects and differ in only few amino acids that are mostly located in the linker regions between the interaction modules. Nck proteins connect receptor and non-receptor tyrosine kinases to the machinery of actin reorganisation. Thereby, Nck regulates activation-dependent processes during cell polarisation and migration and plays a crucial role in the signal transduction of a variety of receptors including for instance PDGF-, HGF-, VEGF- and Ephrin receptors. In most cases, the SH2 domain mediates binding to the phosphorylated receptor or associated phosphoproteins, while SH3 domain interactions lead to the formation of larger protein complexes. In T lymphocytes, Nck plays a pivotal role in the T cell receptor (TCR)-induced reorganisation of the actin cytoskeleton and the formation of the immunological synapse. However, in this context, two different mechanisms and adapter complexes are discussed. In the first scenario, dependent on an activation-induced conformational change in the CD3ε subunits, a direct binding of Nck to components of the TCR/CD3 complex was shown. In the second scenario, Nck is recruited to the TCR complex via phosphorylated Slp76, another central constituent of the membrane proximal activation complex. Over the past years, a large number of putative Nck interactors have been identified in different cellular systems that point to diverse additional functions of the adapter protein, e.g. in the control of gene expression and proliferation.
         datePublished:2009-02-02T00:00:00Z
         dateModified:2009-02-02T00:00:00Z
         pageStart:1
         pageEnd:13
         license:http://creativecommons.org/licenses/by/2.0
         sameAs:https://doi.org/10.1186/1478-811X-7-1
         keywords:
            Immunological Synapse
            Weak Antigen
            WASP Interact Protein
            ITAM Phosphorylation
            Cell Biology
            Protein-Ligand Interactions
            Receptors
            Cytokines and Growth Factors
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            name:BioMed Central
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               name:Marcus Lettau
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               name:Jennifer Pieper
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ScholarlyArticle:
      headline:Nck adapter proteins: functional versatility in T cells
      description:Nck is a ubiquitously expressed adapter protein that is almost exclusively built of one SH2 domain and three SH3 domains. The two isoproteins of Nck are functionally redundant in many aspects and differ in only few amino acids that are mostly located in the linker regions between the interaction modules. Nck proteins connect receptor and non-receptor tyrosine kinases to the machinery of actin reorganisation. Thereby, Nck regulates activation-dependent processes during cell polarisation and migration and plays a crucial role in the signal transduction of a variety of receptors including for instance PDGF-, HGF-, VEGF- and Ephrin receptors. In most cases, the SH2 domain mediates binding to the phosphorylated receptor or associated phosphoproteins, while SH3 domain interactions lead to the formation of larger protein complexes. In T lymphocytes, Nck plays a pivotal role in the T cell receptor (TCR)-induced reorganisation of the actin cytoskeleton and the formation of the immunological synapse. However, in this context, two different mechanisms and adapter complexes are discussed. In the first scenario, dependent on an activation-induced conformational change in the CD3ε subunits, a direct binding of Nck to components of the TCR/CD3 complex was shown. In the second scenario, Nck is recruited to the TCR complex via phosphorylated Slp76, another central constituent of the membrane proximal activation complex. Over the past years, a large number of putative Nck interactors have been identified in different cellular systems that point to diverse additional functions of the adapter protein, e.g. in the control of gene expression and proliferation.
      datePublished:2009-02-02T00:00:00Z
      dateModified:2009-02-02T00:00:00Z
      pageStart:1
      pageEnd:13
      license:http://creativecommons.org/licenses/by/2.0
      sameAs:https://doi.org/10.1186/1478-811X-7-1
      keywords:
         Immunological Synapse
         Weak Antigen
         WASP Interact Protein
         ITAM Phosphorylation
         Cell Biology
         Protein-Ligand Interactions
         Receptors
         Cytokines and Growth Factors
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1186%2F1478-811X-7-1/MediaObjects/12964_2008_Article_49_Fig1_HTML.jpg
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                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
            name:Jennifer Pieper
            affiliation:
                  name:University Hospital Schleswig-Holstein Campus Kiel
                  address:
                     name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Ottmar Janssen
            affiliation:
                  name:University Hospital Schleswig-Holstein Campus Kiel
                  address:
                     name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
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      address:
         name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
         type:PostalAddress
      name:University Hospital Schleswig-Holstein Campus Kiel
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      affiliation:
            name:University Hospital Schleswig-Holstein Campus Kiel
            address:
               name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
               type:PostalAddress
            type:Organization
      email:[email protected]
      name:Jennifer Pieper
      affiliation:
            name:University Hospital Schleswig-Holstein Campus Kiel
            address:
               name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
               type:PostalAddress
            type:Organization
      name:Ottmar Janssen
      affiliation:
            name:University Hospital Schleswig-Holstein Campus Kiel
            address:
               name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
      name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany
      name:Institute of Immunology, Molecular Immunology, University Hospital Schleswig-Holstein Campus Kiel, Kiel, Germany

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