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Cell adhesion

How integrins are activated

Nature volume 390, pages 15–17 (1997)Cite this article

The integrins are a family of adhesion receptors that are involved in a diverse array of cellular processes including cell migration and growth1,2. They adhere to various extracellular matrix proteins and their affinity for these ligands is altered (in response to cellular signals) by conformational changes in their ligand-binding sites3,4. The α and β chains of integrin heterodimers are each composed of an extracellular region, a transmembrane segment and a small cytoplasmic domain. Integrin activation is required for cell adhesion but the molecular mechanisms involved are unclear. A paper by Fenczik et al.5 on page 81of this issue reports that CD98, an early marker of T-cell activation, is an important regulator of integrin-mediated cell adhesion.

In previous studies, these investigators established that a limiting cellular factor is critical for adhesion involving integrins3. They engineered Chinese hamster ovary cells to produce a chimaeric protein composed of the extracellular and transmembrane portions of αIIbβ3integrin and the intracellular domain of α6Aβ1integrin3,4. This chimaeric protein is constitutively active, and is capable of binding ligands and transducing signals through the cytoplasmic domain. Fenczik and colleagues next engineered these cells to express another chimaeric protein (Tac-β1), composed of the cytoplasmic region of β1integrin and the extracellular domain of the Tac subunit of the interleukin-2 receptor. The doubly transfected cells exhibited a dominant and concentration-dependent suppression of integrin activation, and they were no longer capable of adhesion, spreading or migration.

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  1. the Department of Molecular Oncology, Genentech Inc., 460 Pt San Bruno Blvd, South San Francisco, California, 94080, USA

    Laurence A. Lasky

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  1. Laurence A. Lasky
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Lasky, L. How integrins are activated. Nature 390, 15–17 (1997). https://doi.org/10.1038/36204

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