Review

Nature Reviews Molecular Cell Biology 11, 23-36 (January 2010) | doi:10.1038/nrm2821

Regulation of cell signalling by uPAR

Harvey W. Smith1 & Chris J. Marshall2  About the authors

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Urokinase-type plasminogen activator receptor (uPAR) expression is elevated during inflammation and tissue remodelling and in many human cancers, in which it frequently indicates poor prognosis. uPAR regulates proteolysis by binding the extracellular protease urokinase-type plasminogen activator (uPA; also known as urokinase) and also activates many intracellular signalling pathways. Coordination of extracellular matrix (ECM) proteolysis and cell signalling by uPAR underlies its important function in cell migration, proliferation and survival and makes it an attractive therapeutic target in cancer and inflammatory diseases. uPAR lacks transmembrane and intracellular domains and so requires transmembrane co-receptors for signalling. Integrins are essential uPAR signalling co-receptors and a second uPAR ligand, the ECM protein vitronectin, is also crucial for this process.

Author affiliations

  1. Goodman Cancer Centre, Room 507, McGill University 1160 Pine Ave., West Montreal, Quebec, H3A 1A3, Canada.
    Email: harvey.smith2@mcgill.ca
  2. Cancer Research UK Centre for Cell and Molecular Biology, Institute of Cancer Research, 237 Fulham Road, London, SW3 6JB, United Kingdom.
    Email: chris.marshall@icr.ac.uk

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