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EMBO Rep. 2015 Feb;16(2):178-91. doi: 10.15252/embr.201439791. Epub 2014 Dec 22.

The RNA-binding protein Arrest (Bruno) regulates alternative splicing to enable myofibril maturation in Drosophila flight muscle.

Author information

1
Max Planck Institute of Biochemistry, Martinsried, Germany.
2
Max Planck Institute of Cell Biology and Genetics, Dresden, Germany.
3
Research Institute of Molecular Pathology (IMP) Vienna Biocenter (VBC), Vienna, Austria.
4
Max Planck Institute of Biochemistry, Martinsried, Germany schnorrer@biochem.mpg.de.

Abstract

In Drosophila, fibrillar flight muscles (IFMs) 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 IFMs. 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.

KEYWORDS:

Arrest; Drosophila; alternative splicing; flight muscle; myofibril

PMID:
25532219
PMCID:
PMC4328745
DOI:
10.15252/embr.201439791
[Indexed for MEDLINE]
Free PMC Article
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