ArticleMolecular biology of the cell1992
A Dictyostelium myosin II lacking a proximal 58-kDa portion of the tail is functional in vitro and in vivo.
Article in Molecular biology of the cell, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 40 citations in OpenAlex.
- Actomyosin based contraction: one mechanokinetic model from single molecules to muscle?Journal of muscle research and cell motility · 2016Article
- Role of Turnover in Active Stress Generation in a Filament Network.Physical review letters · 2016Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Temperature dependence of myosin-II tail fragment assembly.Journal of muscle research and cell motility · 2008Article
- Biological, biochemical, and kinetic effects of mutations of the cardiomyopathy loop of Dictyostelium myosin II: importance of ALA400.The Journal of biological chemistry · 2005Article
- Dictyostelium and Acanthamoeba myosin II assembly domains go to the cleavage furrow of Dictyostelium myosin II-null cells.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- A structural model for phosphorylation control of Dictyostelium myosin II thick filament assembly.The Journal of cell biology · 1999Article
- X-ray diffraction studies on thermally induced tension generation in rigor muscle.Journal of muscle research and cell motility · 1996Article
- Structure-function studies of the myosin motor domain: importance of the 50-kDa cleft.Molecular biology of the cell · 1996Article
- Expression of light meromyosin in Dictyostelium blocks normal myosin II function.The Journal of cell biology · 1995Article
- A novel positive selection for identifying cold-sensitive myosin II mutants in Dictyostelium.Genetics · 1995Article
- Kinetic characterization of a cytoplasmic myosin motor domain expressed in Dictyostelium discoideum.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
We used molecular genetic approaches to delete 521 amino acid residues from the proximal portion of the Dictyostelium myosin II tail. The deletion encompasses approximately 40% of the tail, including the S2-LMM junction, a region that in muscle myosin II has been proposed to be important for contraction. The functions of the mutant myosin II are indistinguishable from the wild-type myosin II in our in vitro assays. It binds to actin in a typical rigor configuration in the absence of ATP and it forms filaments in a normal salt-dependent manner. In an in vitro motility assay, both monomeric and filamentous forms of the mutant myosin II translocate actin filaments at 2.4 microns/s at 30 degrees C, similar to that of wild-type myosin II. The mutant myosin II is also functional in vivo. Cells expressing the mutant myosin II in place of the native myosin II perform myosin II-dependent activities such as cytokinesis and formation of fruiting bodies, albeit inefficiently. Growth of the mutant cells in suspension gives rise to many large multinucleated cells, demonstrating that cytokinesis often fails. The majority of the fruiting bodies are also morphologically abnormal. These results demonstrate that this region of the myosin II tail is not required for motile activities but its presence is necessary for optimum function in vivo.
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