ArticleJournal of muscle research and cell motility1988
Brush border myosin filament assembly and interaction with actin investigated with monoclonal antibodies.
Article in Journal of muscle research and cell motility, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- R40.76 binds to the α domain of ZO-1: role of ZO-1 (α+) in epithelial differentiation and mechano-sensing.Tissue barriers · 2019Article
- Role of the COOH-terminal nonhelical tailpiece in the assembly of a vertebrate nonmuscle myosin rod.The Journal of cell biology · 1992Article
- Parallel modulation of brush border myosin conformation and enzyme activity induced by monoclonal antibodies.The Journal of cell biology · 1989Article
- Modulation of cellular morphology and locomotory activity by antibodies against myosin.The Journal of cell biology · 1988Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Monoclonal antibodies binding to epitopes in the rod portion of brush border myosin were used to study the mechanism of filament assembly and its role in myosin interaction with actin. The antibodies and their Fab fragments had specific effects on the size of the filaments assembled in vitro. Two antibodies (BM3 and BM4), directed against the tip of the myosin tail, completely inhibited myosin filament assembly. The other antibodies (BM1, BM2 and BM5), binding to other sites along the myosin rod, only partially blocked filament growth, and short filaments could be assembled. Thiophosphorylated brush border myosin filaments appeared slightly more stable to the effects of the antibodies than those composed of dephosphorylated myosin. Only one (BM3) of the antibodies which completely inhibited the assembly of new filaments was capable of disassembling preformed myosin filaments. The other antibody, BM4, partially disassembled filaments, leaving approximately 0.2-microns long 'cores', suggesting that polymerization in this myosin occurs by a biphasic mechanism, i.e. the formation of a stable nucleus of antiparallely packed molecules, followed by elongation. The antibodies BM1 and BM2 bound to myosin filaments generating a regular transverse pattern with a approximately 14-nm periodicity, and had little effect on the stability of these preformed filaments. Inhibition of filament formation and solubilization of the myosin by the antibodies appeared to be associated with inhibition of myosin interaction with actin, as measured by the actin-activated MgATPase activity. In the presence of the antibodies which completely inhibit filament assembly, we observed a decrease to approximately 20% (BM4-Fab) and to approximately 50% (BM3) of the control actin-activated myosin MgATPase activity, and this activity was kinetically different from that of the soluble myosin S1 fragment, suggesting that the rod has a profound effect on the kinetics of actomyosin interaction.
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