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Cell biology

Adhesion articulated

Nature volume 432, pages 27–28 (2004)Cite this article

A new structure of the ‘head’ region of an integrin protein explains the remarkable vertical extension that enables these molecules to rise to the task of mediating cell adhesion.

If they are to survive and move, cells must be able to stick to their surroundings. Integrin proteins enable a bidirectional control of cell adhesiveness, by dynamically coupling the matrix of molecules found outside the cell to the cell's internal ‘skeleton’. All 24 members of the integrin family have two subunits, one from the α-subfamily and one from the β-subfamily; each subunit is composed of large extracellular and short intracellular regions. Integrins work by conveying shape changes through these subunits — from the intracellular domains, through the cell membrane, to the extracellular region, and vice versa1,2. As adhesion needs to be strictly controlled to avoid inappropriate cell aggregation or migration, integrins require a highly responsive structure that can exist in low-affinity (inactive), high-affinity (primed) or ligand-bound (activated) states.

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Figure 1: Integrin activation states.
Figure 2: The complex between a macromolecular ligand and the integrin head domains.

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Authors and Affiliations

  1. the Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester, M13 9PT, UK

    A. Paul Mould & Martin J. Humphries

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  1. A. Paul Mould
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  2. Martin J. Humphries
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Mould, A., Humphries, M. Adhesion articulated. Nature 432, 27–28 (2004). https://doi.org/10.1038/432027a

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