Abstract:
:Dystrophin, a component of the muscle membrane cytoskeleton, is the protein altered in Duchenne Muscular Dystrophy (DMD) and Becker Muscular Dystrophy (BMD). Dystrophin shares significant homology with other cytoskeletal proteins, such as alpha-actinin and spectrin. On the basis of its sequence similarity with alpha-actinin and spectrin, dystrophin has been proposed to function as dimer. However, the existence of both dimers and monomers have been observed by electron microscopy. To address this apparent discrepancy, we expressed dystrophin fragments composed of different domains in an in vitro translation system. The expressed fragments were tested for their ability to interact with each other and full-length dystrophin by both immunoprecipitation and blot overlay assays. These assays were successfully used to demonstrate the dimerization of alpha-actinin and spectrin, yet failed to detect any interaction between dystrophin fragments. Although these in vitro results do not prove that dystrophin is not a dimer in vivo, they do indicate that this interaction is not like that of the alpha-actinin and spectrin.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Chan Y,Kunkel LMdoi
10.1016/s0014-5793(97)00454-7subject
Has Abstractpub_date
1997-06-30 00:00:00pages
153-9issue
2-3eissn
0014-5793issn
1873-3468pii
S0014579397004547journal_volume
410pub_type
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