sarcomere formation occurs by the assembly of multiple latent protein complexes肌节组装形成发生的多个潜在的蛋白复合物.pdfVIP

Sarcomere Formation Occurs by the Assembly of Multiple Latent Protein Complexes Yanning Rui1.*, Jianwu Bai1.¤, Norbert Perrimon1,2* 1 Department of Genetics, Harvard Medical School, Boston, Massachusetts, United States of America, 2 Howard Hughes Medical Institute, Harvard Medical School, Boston, Massachusetts, United States of America Abstract The stereotyped striation of myofibrils is a conserved feature of muscle organization that is critical to its function. Although most components that constitute the basic myofibrils are well-characterized biochemically and are conserved across the animal kingdom, the mechanisms leading to the precise assembly of sarcomeres, the basic units of myofibrils, are poorly understood. To gain insights into this process, we investigated the functional relationships of sarcomeric protein complexes. Specifically, we systematically analyzed, using either RNAi in primary muscle cells or available genetic mutations, the organization of myofibrils in Drosophila muscles that lack one or more sarcomeric proteins. Our study reveals that the thin and thick filaments are mutually dependent on each other for striation. Further, the tension sensor complex comprised of zipper/Zasp/a-actinin is involved in stabilizing the sarcomere but not in its initial formation. Finally, integrins appear essential for the interdigitation of thin and thick filaments that occurs prior to striation. Thus, sarcomere formation occurs by the coordinated assembly of multiple latent protein complexes, as opposed to sequential assembly. Citation: Rui Y, Bai J, Perrimon N (2010) Sarcomere Formation Occurs by the Assembly of Multiple Latent Protein Complexes. PLoS Genet 6(11): e1001208. doi:10.1371/journal.pgen.1001208 Editor: Gregory S. Barsh, Stanford University, United States of America Received January 12, 2010; Accepted October 15,