ArticleThe Journal of cell biology1991
Myosin functional domains encoded by alternative exons are expressed in specific thoracic muscles of Drosophila.
Article in The Journal of cell biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 63 citations in OpenAlex.
- Distinct impacts of human co-chaperone UNC45 paralogs on Drosophila muscle development and function.Journal of cell science · 2025Article
- Enhanced expression of the myogenic factor Myocyte enhancer factor-2 in imaginal disc myoblasts activates a partial, but incomplete, muscle development program.Developmental biology · 2024Article
- Review
- Transcriptomic and Functional Analyses of Phenotypic Plasticity in a Higher Termite,Frontiers in genetics · 2019Article
- Alternative relay and converter domains tune native muscle myosin isoform function in Drosophila.Journal of molecular biology · 2012Article
- Regulated functional alternative splicing in Drosophila.Nucleic acids research · 2012Review
- Mutating the converter-relay interface of Drosophila myosin perturbs ATPase activity, actin motility, myofibril stability and flight ability.Journal of molecular biology · 2010Article
- Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics.Biophysical journal · 2009Article
- Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles.Journal of molecular biology · 2008Article
- Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function.Journal of molecular biology · 2008Article
- A variable domain near the ATP-binding site in Drosophila muscle myosin is part of the communication pathway between the nucleotide and actin-binding sites.Journal of molecular biology · 2007Article
- Alternative S2 hinge regions of the myosin rod differentially affect muscle function, myofibril dimensions and myosin tail length.Journal of molecular biology · 2007Article
- Transcriptional regulation of the Drosophila melanogaster muscle myosin heavy-chain gene.Gene expression patterns : GEP · 2007Article
- An alternative domain near the ATP binding pocket of Drosophila myosin affects muscle fiber kinetics.Biophysical journal · 2006Article
- The iStem, a long-range RNA secondary structure element required for efficient exon inclusion in the Drosophila Dscam pre-mRNA.Molecular and cellular biology · 2005Article
- Stretchin-klp, a novel Drosophila indirect flight muscle protein, has both myosin dependent and independent isoforms.Journal of muscle research and cell motility · 2005Article
- Article
- Specific myosin heavy chain mutations suppress troponin I defects in Drosophila muscles.The Journal of cell biology · 1999Article
- The role of evolutionarily conserved sequences in alternative splicing at the 3' end of Drosophila melanogaster myosin heavy chain RNA.Genetics · 1999Article
- Transposable element insertions respecify alternative exon splicing in three Drosophila myosin heavy chain mutants.Genetics · 1998Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Drosophila 36B muscle myosin heavy chain (MHC) gene has five sets of alternatively spliced exons that encode functionally important domains of the MHC protein and provide a combinatorial potential for expression of as many as 480 MHC isoforms. In this study, in situ hybridization analysis has been used to examine the complexity and muscle specificity of MHC isoform expression in the fibrillar indirect flight muscle (IFM), the tubular direct flight muscles (DFM) and tubular tergal depressor of the trochanter muscle (TDT), and the visceral esophageal muscle in the adult thorax. Our results show that alternative splicing of the MHC gene transcripts is precisely regulated in these thoracic muscles, which express three MHC isoforms. Individual thoracic muscles each express transcripts of only one isoform, as detectable by in situ hybridization. An apparently novel fourth MHC isoform, with sequence homology to the rod but not to the head domain of the 36B MHC, is expressed in two direct flight muscles. These findings form a basis for transgenic experiments designed to analyze the muscle-specific functions of MHC domains encoded by alternative exons.
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