P marks the spot: site-specific integrin phosphorylation regulates molecular interactions

Susanna C. Fagerholm, Tiina J. Hilden, Carl G. Gahmberg

    Research output: Contribution to journalArticle

    41 Citations (Scopus)

    Abstract

    Integrins are heterodimeric adhesion receptors at the cell membrane that function as two-way signaling devices. The short intracellular tails of integrins are devoid of catalytic activity, but are nevertheless important for adhesion and signaling, presumably, through interactions with cytoplasmic molecules. Recently, the structure of the intracellular tails has been investigated using NMR, giving important new insight into how integrins might be regulated, but many questions remain unanswered. Signaling by many cell-surface receptors involves protein phosphorylation; over the past few years, phosphorylation of the integrin tails at specific sites has started to emerge as a dynamic mechanism that regulates molecular interactions between integrins and cytoplasmic molecules. This phosphorylation might give rise to signaling specificity and fine-tuning of the integrin-mediated responses.
    Original languageEnglish
    Pages (from-to)504-12
    Number of pages9
    JournalTrends in Biochemical Sciences
    Volume29
    Issue number9
    DOIs
    Publication statusPublished - Sep 2004

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