ArticleThe Journal of cell biology1996
Drosophila paramyosin/miniparamyosin gene products show a large diversity in quantity, localization, and isoform pattern: a possible role in muscle maturation and function.
Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 39 citations in OpenAlex.
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- Alternative S2 hinge regions of the myosin rod affect myofibrillar structure and myosin kinetics.Biophysical journal · 2009Article
- Aging enhances indirect flight muscle fiber performance yet decreases flight ability in Drosophila.Biophysical journal · 2008Article
- Passive stiffness in Drosophila indirect flight muscle reduced by disrupting paramyosin phosphorylation, but not by embryonic myosin S2 hinge substitution.Biophysical journal · 2006Article
- The structural role of high molecular weight tropomyosins in dipteran indirect flight muscle and the effect of phosphorylation.Journal of muscle research and cell motility · 2006Article
- Paramyosin phosphorylation site disruption affects indirect flight muscle stiffness and power generation in Drosophila melanogaster.Proceedings of the National Academy of Sciences of the United States of America · 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
- Two functionally identical modular enhancers in Drosophila troponin T gene establish the correct protein levels in different muscle types.Molecular biology of the cell · 2004Article
- Drosophila paramyosin is important for myoblast fusion and essential for myofibril formation.The Journal of cell biology · 2003Article
- Overexpression of miniparamyosin causes muscle dysfunction and age-dependant myofibril degeneration in the indirect flight muscles of Drosophila melanogaster.Journal of muscle research and cell motility · 2001Article
- Troponin-T is a calcium-binding protein in insect muscle: in vivo phosphorylation, muscle-specific isoforms and developmental profile in Drosophila melanogaster.Journal of muscle research and cell motility · 1998Article
- Immunocytochemical electron microscopic study and western blot analysis of myosin, paramyosin and miniparamyosin in the striated muscle of the fruit fly Drosophila melanogaster and in obliquely striated and smooth muscles of the earthworm Eisenia foetida.Journal of muscle research and cell motility · 1997Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
The Drosophila paramyosin/miniparamyosin gene expresses two products of different molecular weight transcriptionally regulated from two different promoters. Distinct muscle types also have different relative amounts of myosin, paramyosin, and miniparamyosin, reflecting differences in the organization of their thick filaments. Immunofluorescence and EM data indicate that miniparamyosin is mainly located in the M line and at both ends of the thick filaments in Drosophila indirect flight muscles, while paramyosin is present all along the thick filaments. In the tergal depressor of the trochanter muscle, both proteins are distributed all along the A band. In contrast, in the waterbug, Lethocerus, both paramyosin and miniparamyosin are distributed along the length of the indirect flight and leg muscle thick filaments. Two-dimensional and one-dimensional Western blot analyses have revealed that miniparamyosin has several isoforms, focusing over a very wide pH range, all of which are phosphorylated in vivo. The changes in isoform patterns of miniparamyosin and paramyosin indicate a direct or indirect involvement of these proteins in muscle function and flight. This wide spectrum of potential regulatory characteristics underlines the key importance of paramyosin/miniparamyosin and its complex isoform pattern in the organization of the invertebrate thick filament.
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