To understand how complex machines perform their functions, it is essential to map out the ‘blueprints’ of how their internal components are organized. Focal adhesions (FAs) are complex mechanobiological structures involved in a plethora of cell biological processes. The application of super-resolution microscopy in concert with protein engineering offers one approach to unravel the complexity of how individual proteins are organized within FAs. In our recent application, the FA protein talin was found to form a direct structural and physical link between integrin and actin. Interestingly, engineered talin constructs with alternate lengths rescaled the FA nanostructure accordingly. This helped establish that talin could be analogous to the backbone of FAs, serving as the mechanosensitive master coordinator of FA structural organization.
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Cover Image
Cover Image
The image represents talin in focal adhesions. Talin is a mechanosensitive molecule that connects the integrin receptors in the cell membrane with the cytoskeleton. It is exposed to mechanical stretching, which induces the unfolding of its structure. This controls talin's interaction with other proteins, such as Deleted in Liver Cancer (DLC), which is a tumour suppressor and negative regulator of cell contractility. To learn more about this, please see the articles in this issue by Burridge (pages 673–675), Barnett and Kanchanawong (pages 677–680), and Popa and Berkovich (pages 687–699). The image was prepared by Magdalena von Essen, background picture: Vesa Hytönen.
Visualizing the ‘backbone’ of focal adhesions
Armando del Río Hernández, Samuel F. H. Barnett, Pakorn Kanchanawong; Visualizing the ‘backbone’ of focal adhesions. Emerg Top Life Sci 21 December 2018; 2 (5): 677–680. doi: https://doi.org/10.1042/ETLS20180167
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