ArticleJournal of molecular biology2008
Alternative relay domains of Drosophila melanogaster myosin differentially affect ATPase activity, in vitro motility, myofibril structure and muscle function.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 28 citations in OpenAlex.
- Drosophila myosin function and muscle structure are modulated by isoform-specific amino acid residues of the relay domain.Biochemical and biophysical research communications · 2026Article
- Structure of the Inhibited Smooth Muscle Myosin and Its Implications on the Regulation of Insect Striated Muscle Myosin.Life (Basel, Switzerland) · 2025Review
- Article
- Myosin Transducer Inter-Strand Communication Is Critical for Normal ATPase Activity and Myofibril Structure.Biology · 2022Article
- X-ray Crystallographic and Molecular Dynamic Analyses of Drosophila melanogaster Embryonic Muscle Myosin Define Domains Responsible for Isoform-Specific Properties.Journal of molecular biology · 2020Article
- Reductions in ATPase activity, actin sliding velocity, and myofibril stability yield muscle dysfunction in Drosophila models of myosin-based Freeman-Sheldon syndrome.Molecular biology of the cell · 2019Article
- Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- ADisease models & mechanisms · 2017Article
- The Drosophila indirect flight muscle myosin heavy chain isoform is insufficient to transform the jump muscle into a highly stretch-activated muscle type.American journal of physiology. Cell physiology · 2017Article
- A Restrictive Cardiomyopathy Mutation in an Invariant Proline at the Myosin Head/Rod Junction Enhances Head Flexibility and Function, Yielding Muscle Defects in Drosophila.Journal of molecular biology · 2016Article
- The Relay/Converter Interface Influences Hydrolysis of ATP by Skeletal Muscle Myosin II.The Journal of biological chemistry · 2016Article
- A Failure to Communicate: MYOSIN RESIDUES INVOLVED IN HYPERTROPHIC CARDIOMYOPATHY AFFECT INTER-DOMAIN INTERACTION.The Journal of biological chemistry · 2015Article
- Mapping interactions between myosin relay and converter domains that power muscle function.The Journal of biological chemistry · 2014Article
- Alternative relay and converter domains tune native muscle myosin isoform function in Drosophila.Journal of molecular biology · 2012Article
- Transgenic expression and purification of myosin isoforms using the Drosophila melanogaster indirect flight muscle system.Methods (San Diego, Calif.) · 2012Article
- The influence of myosin converter and relay domains on cross-bridge kinetics of Drosophila indirect flight muscle.Biophysical journal · 2010Article
- Mutating the converter-relay interface of Drosophila myosin perturbs ATPase activity, actin motility, myofibril stability and flight ability.Journal of molecular biology · 2010Article
- Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head.Journal of molecular biology · 2009Article
- Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics.Biophysical journal · 2009Article
- Alternative versions of the myosin relay domain differentially respond to load to influence Drosophila muscle kinetics.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The relay domain of myosin is hypothesized to function as a communication pathway between the nucleotide-binding site, actin-binding site and the converter domain. In Drosophila melanogaster, a single myosin heavy chain gene encodes three alternative relay domains. Exon 9a encodes the indirect flight muscle isoform (IFI) relay domain, whereas exon 9b encodes one of the embryonic body wall isoform (EMB) relay domains. To gain a better understanding of the function of the relay domain and the differences imparted by the IFI and the EMB versions, we constructed two transgenic Drosophila lines expressing chimeric myosin heavy chains in indirect flight muscles lacking endogenous myosin. One expresses the IFI relay domain in the EMB backbone (EMB-9a), while the second expresses the EMB relay domain in the IFI backbone (IFI-9b). Our studies reveal that the EMB relay domain is functionally equivalent to the IFI relay domain when it is substituted into IFI. Essentially no differences in ATPase activity, actin-sliding velocity, flight ability at room temperature or muscle structure are observed in IFI-9b compared to native IFI. However, when the EMB relay domain is replaced with the IFI relay domain, we find a 50% reduction in actin-activated ATPase activity, a significant increase in actin affinity, abolition of actin sliding, defects in myofibril assembly and rapid degeneration of muscle structure compared to EMB. We hypothesize that altered relay domain conformational changes in EMB-9a impair intramolecular communication with the EMB-specific converter domain. This decreases transition rates involving strongly bound actomyosin states, leading to a reduced ATPase rate and loss of actin motility.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.