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Lookup NU author(s): Mafalda Cacciottolo, Dr Steven Laval, Emerita Professor Katherine Bushby
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Dysferlin (DYSF) is a type II transmembrane protein implicated in surface membrane repair of muscle. Mutations in dysferlin lead to Limb Girdle Muscular Dystrophy 2B (LGMD2B), Miyoshi Myopathy (MM), and Distal Myopathy with Anterior Tibialis onset (DMAT). The DYSF protein complex is not well understood, and only a few protein-binding partners have been identified thus far. To increase the set of interacting protein partners for DYSF we recovered a list of predicted interacting protein through a systems biology approach. The predictions are part of a "reverse-engineered" genome-wide human gene regulatory network obtained from experimental data by computational analysis. The reverse-engineering algorithm behind the analysis relates genes to each other based on changes in their expression patterns. DYSF and AHNAK were used to query the system and extract lists of potential interacting proteins. Among the 32 predictions the two genes share, we validated the physical interaction between DYSF protein with moesin (MSN) and polymerase I and transcript release factor (PTRF) in mouse heart lysate, thus identifying two novel Dysferlin-interacting proteins. Our strategy could be useful to clarify Dysferlin function in intracellular vesicles and its implication in muscle membrane resealing.
Author(s): Cacciottolo M, Belcastro V, Laval S, Bushby K, di Bernardo D, Nigro V
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Year: 2011
Volume: 286
Issue: 7
Pages: 5404-5413
Print publication date: 18/02/2011
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology
URL: http://dx.doi.org/10.1074/jbc.M110.173559
DOI: 10.1074/jbc.M110.173559
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