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Prepublished online as a Blood First Edition Paper on April 24, 2003; DOI 10.1182/blood-2003-01-0334.
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Blood, 15 August 2003, Vol. 102, No. 4, pp. 1155-1159
PERSPECTIVES
New insights into the structural basis of integrin activation
Jian-Ping Xiong,
Thilo Stehle,
Simon L. Goodman, and
M. Amin Arnaout
From the Renal Unit, Leukocyte Biology and Inflammation Program, Structural Biology Program, Massachusetts General Hospital, and Harvard Medical School, Charlestown, MA; Laboratory of Developmental Immunology, Massachusetts General Hospital and Harvard Medical School, Boston, MA; and Department of Oncology Research, Merck KGaA, Darmstadt, Germany.
Abstract
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 3 decades. In this perspective, we develop a new hypothesis for integrin activation based on recent crystallographic, electron microscopic, and biochemical studies.
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