Protein machines and self assembly in muscle organization

✍ Scribed by José M. Barral; Henry F. Epstein

• Publisher: John Wiley and Sons
• Year: 1999
• Tongue: English
• Weight: 251 KB
• Volume: 21
• Category: Article
• ISSN: 0265-9247
• DOI: 10.1002/(sici)1521-1878(199910)21:10<813::aid-bies3>3.0.co;2-0

✦ Synopsis

The remarkable order of striated muscle is the result of a complex series of protein interactions at different levels of organization. Within muscle, the thick filament and its major protein myosin are classical examples of functioning protein machines. Our understanding of the structure and assembly of thick filaments and their organization into the regular arrays of the A-band has recently been enhanced by the application of biochemical, genetic, and structural approaches. Detailed studies of the thick filament backbone have shown that the myosins are organized into a tubular structure. Additional protein machines and specific myosin rod sequences have been identified that play significant roles in thick filament structure, assembly, and organization. These include intrinsic filament components, cross-linking molecules of the M-band and constituents of the membranecytoskeleton system. Muscle organization is directed by the multistep actions of protein machines that take advantage of well-established self-assembly relationships.