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CD8αα and ‐αβ isotypes are equally recruited to the immunological synapse through their ability to bind to MHC class I

Academic Article
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Overview

authors

  • Rybakin, V.
  • Clamme, J. P.
  • Ampudia, J.
  • Yachi, Pia
  • Gascoigne, Nicholas

publication date

  • December 2011

journal

  • EMBO Reports  Journal

abstract

  • Bimolecular fluorescence complementation was used to engineer CD8 molecules so that CD8αα and CD8αβ dimers can be independently visualized on the surface of a T cell during antigen recognition. Using this approach, we show that CD8αα is recruited to the immunological synapse almost as well as CD8αβ, but because the kinase Lck associates preferentially with CD8αβ in lipid rafts, CD8αα is the weaker co-receptor. During recognition of the strong CD8αα ligand H2-TL, CD8αα is preferentially recruited. Thus, recruitment of the two CD8 species correlates with their relative binding to the available ligands, rather than with the co-receptor functions of the CD8 species.

subject areas

  • Animals
  • Antigens, CD8
  • Fluorescence
  • Histocompatibility Antigens Class I
  • Immunological Synapses
  • Ligands
  • Membrane Glycoproteins
  • Mice
  • Protein Binding
  • Protein Isoforms
  • Receptors, Antigen, T-Cell
  • Recombinant Fusion Proteins
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Research

keywords

  • T-cell activation
  • bimolecular fluorescence complementation
  • co-receptor
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Identity

PubMed Central ID

  • PMC3245696

International Standard Serial Number (ISSN)

  • 1469-221X

Digital Object Identifier (DOI)

  • 10.1038/embor.2011.209

PubMed ID

  • 22081144
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Additional Document Info

start page

  • 1251

end page

  • 1256

volume

  • 12

issue

  • 12

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