The biochemical and mass spectrometric profiling of the dystrophin complexome from skeletal muscle

摘要: The development of advanced mass spectrometric methodology has decisively enhanced the analytical capabilities for studies into composition and dynamics multi-subunit protein complexes their associated components. Large-scale complexome profiling is an approach that combines systematic isolation enrichment assemblies with sophisticated spectrometry-based identification methods. In skeletal muscles, membrane cytoskeletal dystrophin 427 kDa forms tight interactions a variety sarcolemmal, cytosolic extracellular proteins, which in turn associate key components matrix intracellular cytoskeleton. A major function this enormous assembly including dystroglycans, sarcoglycans, syntrophins, dystrobrevins, sarcospan, laminin cortical actin, postulated to stabilize muscle fibres during physical tensions continuous excitation-contraction-relaxation cycles. This article reviews evidence from recent proteomic have focused on characterization dystrophin-glycoprotein complex its central role establishment cytoskeleton-sarcolemma-matrisome axis. Proteomic findings suggest close linkage core species, tubulin, vimentin, desmin, annexin, proteoglycans collagens. Since almost complete absence underlying cause X-linked muscular dystrophy, more detailed understanding composition, structure plasticity may considerable biomedical implications.