Signal transduction by CD28 costimulatory receptor on T cells: B7-1 and B7-2 regulation of tyrosine kinase adaptor molecules

Jacques A. Nunès (Lead / Corresponding author), Alemseged Truneh, Daniel Olive, Doreen A. Cantrell

    Research output: Contribution to journalArticle

    68 Citations (Scopus)

    Abstract

    This study compares the biochemical responses in T cells activated with the CD28 ligands B7-1 and B7-2. The patterns of tyrosine phosphorylation induced in T cells by these two CD28 ligands are identical, but clearly different from the tyrosine phosphorylation induced by the T cell receptor (TCR). The TCR regulates protein complexes mediated by the adapter Grb2 both in vivo and in vitro. In contrast, there is no apparent regulation of in vivo Grb2 complexes in response to B7-1 or B7-2. Rather, B7-1 and B7-2 both induce tyrosine phosphorylation of a different adapter protein, p62. The regulation of p62 is a unique CD28 response that is not shared with the TCR. These data indicate that B7-1 and B7-2 induce identical tyrosine kinase signal transduction pathways. The data show also that the TCR and CD28 couple to different adapter proteins, which could explain the divergence of TCR and CD28 signal transduction pathways during T cell activation.

    Original languageEnglish
    Pages (from-to)1591-1598
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume271
    Issue number3
    DOIs
    Publication statusPublished - 19 Jan 1996

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