ArticleJournal of molecular biology2007
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.
Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Structure of the Inhibited Smooth Muscle Myosin and Its Implications on the Regulation of Insect Striated Muscle Myosin.Life (Basel, Switzerland) · 2025Review
- Nucleotide-free structures of KIF20A illuminate atypical mechanochemistry in this kinesin-6.Open biology · 2023Article
- Alpha and beta myosin isoforms and human atrial and ventricular contraction.Cellular and molecular life sciences : CMLS · 2021Review
- Identification of sequence changes in myosin II that adjust muscle contraction velocity.PLoS biology · 2021Article
- Alternative N-terminal regions ofThe Journal of biological chemistry · 2020Article
- 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
- Article
- Shared gene structures and clusters of mutually exclusive spliced exons within the metazoan muscle myosin heavy chain genes.PloS one · 2014Article
- The superfast human extraocular myosin is kinetically distinct from the fast skeletal IIa, IIb, and IId isoforms.The Journal of biological chemistry · 2013Article
- Conformational changes at the nucleotide site in the presence of bound ADP do not set the velocity of fast Drosophila myosins.Journal of muscle research and cell motility · 2013Article
- Erratum to: Identification of functional differences between recombinant human α and β cardiac myosin motors.Cellular and molecular life sciences : CMLS · 2012Article
- Identification of functional differences between recombinant human α and β cardiac myosin motors.Cellular and molecular life sciences : CMLS · 2012Article
- Transgenic expression and purification of myosin isoforms using the Drosophila melanogaster indirect flight muscle system.Methods (San Diego, Calif.) · 2012Article
- Two Drosophila myosin transducer mutants with distinct cardiomyopathies have divergent ADP and actin affinities.The Journal of biological chemistry · 2011Article
- Structural mechanism of the ATP-induced dissociation of rigor myosin from actin.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Role of insert-1 of myosin VI in modulating nucleotide affinity.The Journal of biological chemistry · 2011Article
- Alternative exon 9-encoded relay domains affect more than one communication pathway in the Drosophila myosin head.Journal of molecular biology · 2009Article
- Similarities and differences between frozen-hydrated, rigor acto-S1 complexes of insect flight and chicken skeletal muscles.Journal of molecular biology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Drosophila expresses several muscle myosin isoforms from a single gene by alternatively splicing six of the 19 exons. Here we investigate exon 7, which codes for a region in the upper 50 kDa domain near the nucleotide-binding pocket. This region is of interest because it is also the place where a large insert is found in myosin VI and where several cardiomyopathy mutations have been identified in human cardiac myosin. We expressed and purified chimeric muscle myosins from Drosophila, each varying at exon 7. Two chimeras exchanged the entire exon 7 domain between the indirect flight muscle (IFI, normally containing exon 7d) and embryonic body wall muscle (EMB, normally containing exon 7a) isoforms to create IFI-7a and EMB-7d. The second two chimeras replaced each half of the exon 7a domain in EMB with the corresponding portion of exon 7d to create EMB-7a/7d and EMB-7d/7a. Transient kinetic studies of the motor domain from these myosin isoforms revealed changes in several kinetic parameters between the IFI or EMB isoforms and the chimeras. Of significance were changes in nucleotide binding, which differed in the presence and absence of actin, consistent with a model in which the exon 7 domain is part of the communication pathway between the nucleotide and actin-binding sites. Homology models of the structures suggest how the exon 7 domain might modulate this pathway.
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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.