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Integrin Structure and Function

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Cell-Extracellular Matrix Interactions in Cancer

Abstract

Integrins are a large family of heterodimeric glycoprotein receptors first discovered over twenty years ago. They exist as two noncovalently bound a- and b- subunits that function as adhesion molecules and play key roles in many biological processes including actin cytoskeleton organization and transduction of intracellular signals regulating cellular functions. Integrins bind a variety of extracellular matrices including collagens and laminins. The phenotypes observed from the generation of integrin knockout mice have provided a wealth of information on the unique biological functions of specific integrin heterodimers. Structural data obtained from X-ray crystallography and nuclear magnetic resonance (NMR) have provided insight into the structural basis for integrin activation and subsequent transduction of bidirectional signals bidirectionally, important for controlling biological cellular functions.

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  1. Department of Medicine, Cancer Biology and Cell Biology, Vanderbilt Medical Center, Nashville, TN, 37232, USA

    Manakan Betsy Srichai & Roy Zent

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  1. Manakan Betsy Srichai
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  1. Vanderbilt University Medical Center, Department of Medicine, Nashville, 37232, U.S.A.

    Roy Zent

  2. Medical Center, Vanderbilt University, Nashville, 37232, U.S.A.

    Ambra Pozzi

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Srichai, M.B., Zent, R. (2010). Integrin Structure and Function. In: Zent, R., Pozzi, A. (eds) Cell-Extracellular Matrix Interactions in Cancer. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-0814-8_2

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