Identification of Proteins Interacting with Dysferlin Using the Tandem Affinity Purification Method
Maziar Assadi*, 1, Thomas Schindler1, Bernd Muller1, John D Porter 2, Markus A Ruegg3, Hanno Langen 1
1 F. Hoffmann-La Roche, Roche Center for Medical Genomics, Basel, Switzerland
2 Case Western Reserve University, Department of Neurology, Cleveland, USA
3 University of Basel, Biozentrum, Basel, Switzerland
Mutations of DYSF, the gene encoding dysferlin, cause two types of muscular dystrophies: limb-girdle muscular dystrophy type 2B and Miyoshi myopathy. Recent work suggests a role of dysferlin in membrane repair and demonstrates that defective membrane repair is a novel mechanism of muscle degeneration. We used the tandem affinity purification method for the purification of proteins interacting with dysferlin. Three interacting partners were identified by this method (striatin, adaptin alpha, utrophin) and were confirmed by co-immunoprecipitations. All three proteins play a role in vesicle trafficking. Knowing the interacting partners of dysferlin will help to understand how muscle cells repair tears in the sarcolemma and will give a deeper insight into this very important cell function. At the same time the identified proteins could serve as potential candidates for other muscular dystrophies and muscle-related diseases with unknown aetiology.
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