ArticleThe Journal of cell biology1987
Subunit exchange between smooth muscle myosin filaments.
Article in The Journal of cell biology, 1987. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Self-assembly of smooth muscle myosin filaments: adaptation of filament length by telokin and Mg·ATP.European biophysics journal : EBJ · 2022Article
- Myosin II dynamics and cortical flow during contractile ring formation in Dictyostelium cells.The Journal of cell biology · 2001Article
- Actin-facilitated assembly of smooth muscle myosin induces formation of actomyosin fibrils.The Journal of cell biology · 1992Article
- Visualization of myosin exchange between synthetic thick filaments.Journal of muscle research and cell motility · 1991Article
- Cell-free incorporation of newly synthesized myosin subunits into thick myofilaments.Journal of muscle research and cell motility · 1991Article
- A nucleation--elongation mechanism for the self-assembly of side polar sheets of smooth muscle myosin.The EMBO journal · 1991Article
- Mammalian nonsarcomeric myosin regulatory light chains are encoded by two differentially regulated and linked genes.The Journal of cell biology · 1990Article
- Differential distribution of myosin isoforms among the myofibrils of individual developing muscle fibers.The Journal of cell biology · 1990Article
- Monoclonal antibodies detect and stabilize conformational states of smooth muscle myosin.The Journal of cell biology · 1989Article
- Temperature dependence of the release of ATP hydrolysis products from the 10S conformation of smooth muscle myosin.Journal of muscle research and cell motility · 1989Article
- Actin filaments mediate Dictyostelium myosin assembly in vitro.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- Myosin filaments isolated from skinned amphibian smooth muscle cells are side-polar.Journal of muscle research and cell motility · 1989Article
- Distribution of fast myosin heavy chain isoforms in thick filaments of developing chicken pectoral muscle.The Journal of cell biology · 1989Article
- The dynamic distribution of fluorescent analogues of actin and myosin in protrusions at the leading edge of migrating Swiss 3T3 fibroblasts.The Journal of cell biology · 1988Article
- Brush border myosin filament assembly and interaction with actin investigated with monoclonal antibodies.Journal of muscle research and cell motility · 1988Article
- Posttranslational incorporation of contractile proteins into myofibrils in a cell-free system.The Journal of cell biology · 1988Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Filaments formed from phosphorylated smooth muscle myosin are stable in the presence of MgATP, whereas dephosphorylated filaments are disassembled to a mixture of folded monomers and dimers. The stability of copolymers of phosphorylated and dephosphorylated myosin was, however, unknown. Gel filtration, sedimentation velocity, and pelleting assays were used to show that MgATP could dissociate dephosphorylated myosin from copolymers containing either rod and myosin or dephosphorylated and phosphorylated myosin. Copolymers were typically formed by dialyzing monomeric mixtures into filament-forming buffer but, unexpectedly, could also be formed within minutes of mixing preformed rod and myosin minifilaments. This result suggested that molecules can rapidly and extensively exchange between filaments, presumably via the monomeric pool of myosin in equilibrium with polymer. An exchange of molecules between filaments was demonstrated directly by electron microscopy using gold-labeled streptavidin or antibody to detect the exchanged species. By this approach it was shown that smooth muscle myosin filaments, like other macromolecular assemblies, are dynamic structures that can readily alter their composition in response to changing solvent conditions. Moreover, because folded monomeric myosin is unable to polymerize, these experiments suggest a mechanism for the disassembly of the filament by MgATP.
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