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By Gunter Nitschke

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Three-dimensional structural determinations of fibronectin and integrin antibody studies suggest a two-point recognition process for binding, with the a subunit potentially binding the Arg in the synergy sequence and the b subunit binding the Arg-Gly-Asp sequence (1820). It seems likely that this kind of multipoint, cooperative binding mechanism will be seen in other integrinsit provides a simple, effective mechanism for binding ligands directly with considerable specificity in order to trigger ligand-specific integrin signaling.

Over the past decade, it has become clear that integrins play central roles not only in adhesion and cell migration, but also in the regulation of growth, gene expression, and differentiation. Concepts of integrins have evolved from considering these receptors as simple cell surface binding moieties for extracellular adhesion molecules to the realization that they also serve complex roles as activators or modulators of signal transduction. As summarized in Fig. 1, integrins can stimulate a surprising range of signal transduction pathways.

1). Integrins have a characteristic globular head domain that binds to ligands, long legs that hold the head a substantial distance above the plasma membrane, transmembrane domains, and short cytoplasmic tails (roughly 1000 From: Signaling Networks and Cell Cycle Control: The Molecular Basis of Cancer and Other Diseases Edited by: J. S.  1.  Integrin affinity and ability to bind to specific target ligands can be modulated by cytoplasmic processes that result in inside-out signaling that affects binding by the head domain.

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