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  • Cathepsin X cleavage of the ß2 integrin regulates talin-binding and LFA-1 affinity in T cells
    Jevnikar, Zala ...
    T cell migration, essential for immune surveillance and response, is mediated by the integrin LFA-1. CatX, a cysteine carboxypeptidase, is involved in the regulation of T cell migration by ... interaction with LFA-1. We show that sequential cleavage of C-terminal amino acids from the ?2 cytoplasmic tail of LFA-1, by CatX, enhances binding of the adaptor protein talin to LFA-1 and triggers formation of the latter's high-affinity form. As shown by SPR analysis of peptides constituting the truncated ?2 tail, the cleavage of three C-terminal amino acids by CatX resulted in a 1.6-fold increase of talin binding. Removal of one more amino acid resulted in a 2.5-fold increase over the intact tail. CatX cleavage increased talin-binding affinity to the MD but not the MP talin-binding site on the ?2 tail. This was shown by molecular modeling of the ?2 tail/talin F3 complex to be a result of conformational changes affecting primarily the distal-binding site. Analysis of LFA-1 by conformation-specific mAb showed that CatX modulates LFA-1 affinity, promoting formation of high-affinity from intermediate-affinity LFA-1 but not the initial activation of LFA-1 from a bent to extended form. CatX post-translational modifications may thus represent a mechanism of LFA-1 fine-tuning that enables the trafficking of T cells
    Vir: Journal of leukocyte biology. - ISSN 0741-5400 (Vol. 90, no. 1, 2011, str. 99-109)
    Vrsta gradiva - članek, sestavni del
    Leto - 2011
    Jezik - angleški
    COBISS.SI-ID - 2988913

    Povezava(-e):

    http://www.jleukbio.org/content/early/2011/03/31/jlb.1110622.abstract
    DOI

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