Regulation of integrin function through conformational complexity: Not simply a knee-jerk reaction?

A. Paul Mould, Martin J. Humphries

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Such diverse biological processes as the maintenance of tissue architecture and the regulation of cell migration are controlled through dynamic changes in integrin receptor conformation. Early analyses of the mechanisms of shape change by integrins led to the definition of three inter-convertible conformational states: inactive, primed and ligand-occupied. Recent advances reviewed in this article have now shown that the integrin molecule contains a number of flexible joints and connections, leading to a broad spectrum of possible conformational states. This conformational complexity is likely to permit fine-tuning of integrin function through regulation of ligand-binding affinity and intracellular signalling.
    Original languageEnglish
    Pages (from-to)544-551
    Number of pages7
    JournalCurrent opinion in cell biology
    Volume16
    Issue number5
    DOIs
    Publication statusPublished - Oct 2004

    Keywords

    • adjacent to MIDAS
    • ADMIDAS
    • electron microscopy
    • EM
    • fluorescence resonance energy transfer
    • FRET
    • ligand-associated metal binding site
    • LIMBS
    • mAb
    • metal-ion-dependent adhesion site
    • MIDAS
    • monoclonal antibody

    Fingerprint

    Dive into the research topics of 'Regulation of integrin function through conformational complexity: Not simply a knee-jerk reaction?'. Together they form a unique fingerprint.

    Cite this