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doi: 10.1242/10.1242/jcs.00157
Commentary |
Wellcome Trust/Cancer Research UK Institute and Dept of Anatomy, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QR, UK
* Author for correspondence (e-mail: n.brown{at}welc.cam.ac.uk)
Recent studies have characterised a family of giant cytoskeletal crosslinkers encoded by the short stop gene in Drosophila and the dystonin/BPAG1 and MACF1 genes in mammals. We refer to the products of these genes as spectraplakins to highlight the fact that they share features with both the spectrin and plakin superfamilies. These genes produce a variety of large proteins, up to almost 9000 residues long, which can potentially extend 0.4 µm across a cell. Spectraplakins can interact with all three elements of the cytoskeleton: actin, microtubules and intermediate filaments. The analysis of mutant phenotypes in BPAG1 in mouse and short stop in Drosophila demonstrates that spectraplakins have diverse roles. These include linking the plasma membrane and the cytoskeleton, linking together different elements of the cytoskeleton and organising membrane domains.
Key words: Spectrin, Plakin, Cytoskeleton, Adhesion
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