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Prepublished online as a Blood First Edition Paper on April 24, 2003; DOI 10.1182/blood-2003-01-0334.
Submitted February 19, 2003
Accepted April 9, 2003
New insights into the structural basis of integrin activation
Jian-Ping Xiong, Thilo Stehle, Simon L Goodman, and M Amin Arnaout*
Department of Medicine, Massachusetts General Hospital, Charlestown, MA, USA; Department of Medicine, Massachusetts General Hospital, Charlestown, MA, USA
Department of Oncology Research, Merck KGaA, Darmstadt, Germany
Department of Medicine, Massachusetts General Hospital, Charlestown, MA, USA
* Corresponding author; email: arnaout{at}receptor.mgh.harvard.edu.
Integrins are cell adhesion receptors that communicate biochemical and mechanical signals in a bidirectional manner across the plasma membrane and thus influence most cellular functions. Intracellular signals switch integrins into a ligand-competent state as a result of elicited conformational changes in the integrin ectodomain. Binding of extracellular ligands induces in turn structural changes that convey distinct signals to the cell interior. The structural basis of this bidirectional signaling has been the focus of intensive study for the past three decades. In this perspective, we develop a new hypothesis for integrin activation based on recent crystallographic, electron microscopy and biochemical studies.
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