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The RNA ‐binding protein Arrest (Bruno) regulates alternative splicing to enable myofibril maturation in Drosophila flight muscle
Author(s) -
Spletter Maria L,
Barz Christiane,
Yeroslaviz Assa,
Schönbauer Cornelia,
Ferreira Irene R S,
Sarov Mihail,
Gerlach Daniel,
Stark Alexander,
Habermann Bianca H,
Schnorrer Frank
Publication year - 2015
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201439791
Subject(s) - microbiology and biotechnology , rna binding protein , drosophila (subgenus) , rna splicing , myofibril , biology , insect flight , rna , chemistry , genetics , biochemistry , physics , wing , gene , thermodynamics
In Drosophila , fibrillar flight muscles ( IFM s) enable flight, while tubular muscles mediate other body movements. Here, we use RNA ‐sequencing and isoform‐specific reporters to show that spalt major ( salm ) determines fibrillar muscle physiology by regulating transcription and alternative splicing of a large set of sarcomeric proteins. We identify the RNA ‐binding protein Arrest (Aret, Bruno) as downstream of salm . Aret shuttles between the cytoplasm and nuclei and is essential for myofibril maturation and sarcomere growth of IFM s. Molecularly, Aret regulates IFM ‐specific splicing of various salm ‐dependent sarcomeric targets, including Stretchin and wupA (TnI), and thus maintains muscle fiber integrity. As Aret and its sarcomeric targets are evolutionarily conserved, similar principles may regulate mammalian muscle morphogenesis.