Résumé :
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The dystonin gene encodes several tissue selective BPAG1 protein isoforms, issued from alternative splicing. In skeletal muscle, the main isoform is BPAG1-b, a 830kDa protein that presents the hallmarks of both spectrin and plakin families. The precise functions of BPAG1-b are so far unknown, nevertheless the analysis of dt mice (Dst null) have underlined the importance of this protein for the maintenance of skeletal muscle tissue integrity. In order to better understand its functions, we have initiated co-immunoprecipitation, pull-down and yeast two-hybrid assays that aim at identifying BPAG1-b interacting partners in muscle. Further analyses are underway to validate the potential partners identified in these screens.
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