Journal
COMPREHENSIVE PHYSIOLOGY
Volume 5, Issue 3, Pages 1223-1239Publisher
WILEY
DOI: 10.1002/cphy.c140048
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Funding
- NCATS NIH HHS [UL1 TR000430] Funding Source: Medline
- NHLBI NIH HHS [R01 HL061322] Funding Source: Medline
- NIAMS NIH HHS [U54 AR052646] Funding Source: Medline
- NINDS NIH HHS [P01 NS072027] Funding Source: Medline
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The dystrophin complex stabilizes the plasma membrane of striated muscle cells. Loss of function mutations in the genes encoding dystrophin, or the associated proteins, trigger instability of the plasma membrane, and myofiber loss. Mutations in dystrophin have been extensively cataloged, providing remarkable structure-function correlation between predicted protein structure and clinical outcomes. These data have highlighted dystrophin regions necessary for in vivo function and fueled the design of viral vectors and now, exon skipping approaches for use in dystrophin restoration therapies. However, dystrophin restoration is likely more complex, owing to the role of the dystrophin complex as a broad cytoskeletal integrator. This review will focus on dystrophin restoration, with emphasis on the regions of dystrophin essential for interacting with its associated proteins and discuss the structural implications of these approaches. (C) 2015 American Physiological Society.
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