Journal
JOURNAL OF CELL SCIENCE
Volume 126, Issue 15, Pages 3314-3323Publisher
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.122366
Keywords
Drosophila Abba/Thin; Sarcomeres; Z-discs; M-lines; TRIM32; Skeletal muscle
Categories
Funding
- Muscular Dystrophy Association [3597]
- Deutsche Forschungemeinschaft [NG 92/1-1]
- Fakulatsfrauenpreis from the University of Erlangen-Nurnberg
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Organized sarcomeric striations are an evolutionarily conserved hallmark of functional skeletal muscles. Here, we demonstrate that the Drosophila Abba protein, a member of the TRIM/RBCC superfamily, has a pivotal regulatory role in maintaining proper sarcomeric cytoarchitecture during development and muscle usage. abba mutant embryos initially form muscles, but F-actin and Myosin striations become progressively disrupted when the muscles undergo growth and endure increased contractile forces during larval development. Abnormal Myosin aggregates and myofiber atrophy are also notable in the abba mutants. The larval defects result in compromised muscle function, and hence important morphogenetic events do not occur properly during pupation, leading to lethality. Abba is localized at larval Z-discs, and genetic evidence indicates that abba interacts with alpha-actinin, kettin/D-titin and mlp84B, genes that encode important Z-disc proteins for stable myofibrillar organization and optimal muscle function. RNAi experiments and ultrastructural analysis reveal that Abba has an additional crucial role in sarcomere maintenance in adult muscles. Abba is required to ensure the integrity and function of Z-discs and M-lines. Rescue experiments further show that Abba function is dependent upon its B-box/coiled-coil domain, NHL repeats and RING finger domain. The importance of these presumed protein-protein interactions and ubiquitin ligase-associated domains supports our hypothesis that Abba is needed for specific protein complex formation and stabilization at Z-discs and M-lines.
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