14-3-3 proteins bind both filamin and alphaLbeta2 integrin in activated T cells

Susanna M. Nurmi, Carl G. Gahmberg, Susanna C. Fagerholm

    Research output: Contribution to journalArticlepeer-review

    17 Citations (Scopus)

    Abstract

    Engagement of the T cell receptor (TCR) initiates intracellular signaling cascades that result in T cell activation, differentiation, acquisition of effector functions, or apoptosis. The signals from the TCR are coupled to distal signaling pathways by adapter proteins leading to dramatic changes in the cytoskeleton, transcription, and activation of integrins, which mediate adhesion. LFA-1 (leukocyte function-associated antigen-1) integrin (Lß2 or CD11a/CD18) plays an important role in adhesion, for example, by linking extracellular ligands to the actin cytoskeleton. The intracellular tails of integrins contain several phosphorylation sites, making them candidate-binding partners for 14-3-3 proteins, which are adaptor proteins that bind to phosphorylated ligands. In a screen for 14-3-3 binding partners in T cells, we identified both ß2 integrins and filamin. The integrin ß2 chain binds to 14-3-3 proteins through phosphorylated Thr758 after TCR ligation and this association regulates integrin-mediated cell spreading, which is necessary for adhesion. Here, we show that filamin associates with 14-3-3 proteins in activated T cells. 14-3-3 association with T cell membrane and cytoskeleton proteins after cell stimulation may mediate numerous T cell functions.
    Original languageEnglish
    Pages (from-to)318-325
    Number of pages8
    JournalAnnals of the New York Academy of Sciences
    Volume1090
    Issue number1
    DOIs
    Publication statusPublished - Dec 2006

    Keywords

    • Integrin
    • 14-3-3 protein
    • Phosphorylation
    • LFA-1
    • T cell

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