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• W2051723944 abstract "Mutations in nebulin, a giant muscle protein with 185 actin-binding nebulin repeats, are the major cause of nemaline myopathy in humans. Nebulin sets actin thin filament length in sarcomeres, potentially by stabilizing thin filaments in the I-band, where nebulin and thin filaments coalign. However, the precise role of nebulin in setting thin filament length and its other functions in regulating power output are unknown. Here, we show that Lasp, the only member of the nebulin family in Drosophila melanogaster, acts at two distinct sites in the sarcomere and controls thin filament length with just two nebulin repeats. We found that Lasp localizes to the Z-disc edges to control I-band architecture and also localizes at the A-band, where it interacts with both actin and myosin to set proper filament spacing. Furthermore, introducing a single amino acid change into the two nebulin repeats of Lasp demonstrated different roles for each domain and established Lasp as a suitable system for studying nebulin repeat function." @default.
• W2051723944 created "2016-06-24" @default.
• W2051723944 creator A5020740298 @default.
• W2051723944 creator A5034400910 @default.
• W2051723944 date "2014-08-11" @default.
• W2051723944 modified "2023-10-07" @default.
• W2051723944 title "The nebulin repeat protein Lasp regulates I-band architecture and filament spacing in myofibrils" @default.
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• W2051723944 doi "https://doi.org/10.1083/jcb.201401094" @default.
• W2051723944 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4137052" @default.
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