Specific effects of individual C2 domains on recovery of voltage-induced SR calcium release after osmotic shock in muscle fibers from dysferlin-null mice

Abstract

Our earlier studies used osmotic shock injury (OSI) to show that dysferlin modulates the coupling of excitation to Ca2+ release in skeletal myofibers (Lukyanenko et al., 2017). As the C2A domain plays an important role in Ca2+ signaling, we expressed it in dysferlin-null A/J mouse FDB myofibers to assess its ability to support normal Ca2+ signaling. cDNAs encoding C2 domains with N-terminal Venus (Venus-C2A, -C2A-C2A, -C2A-C2A-C2A-C2A, -C2A-C2B, -C2C, and -C2E) with or without mutations (pathogenic: W52R, V67D; polymorphisms: V68L; A84V), and with or without dysferlin's C-terminal transmembrane domain (TM), were electroporated into A/J FDB muscles.