The Open Cell Development & Biology Journal
2008, 1 : 17-23Published online 2008 June 17. DOI: 10.2174/1874085500801010017
Publisher ID: TOCBJ-1-17
RESEARCH ARTICLE
Identification of Proteins Interacting with Dysferlin Using the Tandem Affinity Purification Method
2 Case Western Reserve University, Department of Neurology, Cleveland, USA
3 University of Basel, Biozentrum, Basel, Switzerland
* Address correspondence to this author at the the F. Hoffmann-La Roche, Roche Center for Medical Genomics, Basel, Switzerland; Tel: +41-61-688 25 13; Fax: +41-61-688 14 48; E-mail: maziar.assadi@roche.com
ABSTRACT
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.