Nanoscale architecture of integrin-based cell adhesions

Pakorn Kanchanawong, Gleb Shtengel, Ana M. Pasapera, Ericka B. Ramko, Michael W. Davidson (), Harald F. Hess () and Clare M. Waterman ()
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Pakorn Kanchanawong: National Heart Lung and Blood Institute, National Institutes of Health
Gleb Shtengel: Howard Hughes Medical Institute, Janelia Farm Research Campus
Ana M. Pasapera: National Heart Lung and Blood Institute, National Institutes of Health
Ericka B. Ramko: National High Magnetic Field Laboratory, The Florida State University
Michael W. Davidson: National High Magnetic Field Laboratory, The Florida State University
Harald F. Hess: Howard Hughes Medical Institute, Janelia Farm Research Campus
Clare M. Waterman: National Heart Lung and Blood Institute, National Institutes of Health

Nature, 2010, vol. 468, issue 7323, 580-584

Abstract: The architecture of focal adhesions The physical linkage between the extracellular matrix and the actin cytoskeleton of a cell is made by structures known as focal adhesions, acting through integrin receptors. They are of fundamental importance in human physiology because they mediate cell adhesion, mechanosensing and signalling for the control of cell growth and differentiation. The molecular architecture of focal adhesions has now been determined using three-dimensional super-resolution fluorescence microscopy to map protein organization at the nanoscale level. They are revealed as well-organized ultrastructures in which integrins and actin are separated by a 40-nanometre-long core consisting of partially overlapping protein-specific layers, spanned by talin tethers. The multilaminar architecture creates three or more separate compartments that mediate the interdependent functions of focal adhesions.

Date: 2010
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DOI: 10.1038/nature09621

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