In vitro expressed dystrophin fragments do not associate with each other.

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 Lett

journal_title

FEBS letters

authors

Chan Y,Kunkel LM

doi

10.1016/s0014-5793(97)00454-7

subject

Has Abstract

pub_date

1997-06-30 00:00:00

pages

153-9

issue

2-3

eissn

0014-5793

issn

1873-3468

pii

S0014579397004547

journal_volume

410

pub_type

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