ArticleThe Journal of cell biology1989
Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 59 citations in OpenAlex.
- Molecular model of the microvillar cytoskeleton and organization of the brush border.PloS one · 2010Article
- A role for myosin-1A in the localization of a brush border disaccharidase.The Journal of cell biology · 2004Article
- Brush border myosin-I truncated in the motor domain impairs the distribution and the function of endocytic compartments in an hepatoma cell line.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Calmodulin in rat enterocyte: an immunogold electron-microscope study.Cell and tissue research · 1994Article
- Localization of brush border cytoskeletal proteins in gastric oxynticopeptic cells from the bullfrog Rana catesbeiana.Cell and tissue research · 1994Article
- Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry.The Journal of cell biology · 1993Article
- Measuring orientation of actin filaments within a cell: orientation of actin in intestinal microvilli.Biophysical journal · 1993Article
- Relative distribution of actin, myosin I, and myosin II during the wound healing response of fibroblasts.The Journal of cell biology · 1993Article
- Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes of the myosin I family.The Journal of cell biology · 1993Article
- Identification, characterization and cloning of myr 1, a mammalian myosin-I.The Journal of cell biology · 1993Article
- Golgi-derived vesicles from developing epithelial cells bind actin filaments and possess myosin-I as a cytoplasmically oriented peripheral membrane protein.The Journal of cell biology · 1993Article
- Concentration of an integral membrane protein, CD43 (leukosialin, sialophorin), in the cleavage furrow through the interaction of its cytoplasmic domain with actin-based cytoskeletons.The Journal of cell biology · 1993Article
- How Listeria exploits host cell actin to form its own cytoskeleton. I. Formation of a tail and how that tail might be involved in movement.The Journal of cell biology · 1992Article
- Localization of capping protein in chicken epithelial cells by immunofluorescence and biochemical fractionation.The Journal of cell biology · 1992Article
- Purification and characterization of a mammalian myosin I.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting.The Journal of cell biology · 1992Article
- A sialoglycoprotein complex linked to the microvillus cytoskeleton acts as a receptor for pilus (AF/R1) mediated adhesion of enteropathogenic Escherichia coli (RDEC-1) in rabbit small intestine.The Journal of cell biology · 1991Article
- Binding of brush border myosin I to phospholipid vesicles.The Journal of cell biology · 1990Article
- Calmodulin dissociation regulates brush border myosin I (110-kD-calmodulin) mechanochemical activity in vitro.The Journal of cell biology · 1990Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The actin bundle within each microvillus of the intestinal brush border (BB) is tethered laterally to the membrane by bridges composed of BB myosin I. Avian BB myosin I, formerly termed 110K-calmodulin, consists of a heavy chain with an apparent Mr of 110 kD and three to four molecules of calmodulin "light chains." Recent studies have shown that this complex shares many properties with myosin including mechanochemical activity. In this report, the isolation and characterization of a membrane fraction enriched in bound BB myosin I is described. This membrane fraction, termed microvillar membrane disks, was purified from ATP extracts of nonionic detergent-treated microvilli prepared from avian intestinal BBs. Ultrastructural analysis revealed that these membranes are flat, disk-shaped sheets with protrusions which are identical in morphology to purified BB myosin I. The disks exhibit actin-activated Mg-ATPase activity and bind and cross-link actin filaments in an ATP-dependent fashion. The mechanochemical activity of the membrane disks was assessed using the Nitella bead movement assay (Sheetz, M. P., and J. A. Spudich. 1983. Nature [Lond.]. 303:31-35). These preparations were shown to be free of significant contamination by conventional BB myosin. Latex beads coated with microvillar membrane disks move in a myosin-like fashion along Nitella actin cables at rates of 12-60 nm/s (average rate of 33 nm/s); unlike purified BB myosin I, the movement of membrane disk-coated beads was most reproducibly observed in buffers containing low Ca2+.
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