ArticleThe Journal of cell biology1987
Calcium-regulated cooperative binding of the microvillar 110K-calmodulin complex to F-actin: formation of decorated 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 20 papers.
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Who cites it
20 citing papers in PubMed, 75 citations in OpenAlex.
- Mammalian class I myosin, Myo1b, is monomeric and cross-links actin filaments as determined by hydrodynamic studies and electron microscopy.Biophysical journal · 2005Article
- Regulatory implications of a novel mode of interaction of calmodulin with a double IQ-motif target sequence from murine dilute myosin V.Protein science : a publication of the Protein Society · 2002Article
- Rat myr 4 defines a novel subclass of myosin I: identification, distribution, localization, and mapping of calmodulin-binding sites with differential calcium sensitivity.The Journal of cell biology · 1994Article
- Calcium-calmodulin and regulation of brush border myosin-I MgATPase and mechanochemistry.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
- 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
- The role of myosin I and II in cell motility.Cancer metastasis reviews · 1992Review
- Purification and characterization of a mammalian myosin I.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- 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
- Partial deduced sequence of the 110-kD-calmodulin complex of the avian intestinal microvillus shows that this mechanoenzyme is a member of the myosin I family.The Journal of cell biology · 1989Article
- Plasma membrane association of Acanthamoeba myosin I.The Journal of cell biology · 1989Article
- Characterization of intestinal microvillar membrane disks: detergent-resistant membrane sheets enriched in associated brush border myosin I (110K-calmodulin).The Journal of cell biology · 1989Article
- The 110-kD protein-calmodulin complex of the intestinal microvillus (brush border myosin I) is a mechanoenzyme.The Journal of cell biology · 1989Article
- Reassociation of microvillar core proteins: making a microvillar core in vitro.The Journal of cell biology · 1989Article
- Modulation of cellular morphology and locomotory activity by antibodies against myosin.The Journal of cell biology · 1988Article
- Structural and immunological characterization of the myosin-like 110-kD subunit of the intestinal microvillar 110K-calmodulin complex: evidence for discrete myosin head and calmodulin-binding domains.The Journal of cell biology · 1988Article
- Organization of the actin filament cytoskeleton in the intestinal brush border: a quantitative and qualitative immunoelectron microscope study.The Journal of cell biology · 1988Article
- Mapping of the microvillar 110K-calmodulin complex: calmodulin-associated or -free fragments of the 110-kD polypeptide bind F-actin and retain ATPase activity.The Journal of cell biology · 1988Article
- Genetic analysis of myosin assembly in Caenorhabditis elegans.Molecular neurobiologyReview
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Abstract
The 110K-calmodulin complex of intestinal microvilli is believed to be the link between the actin filaments comprising the core bundle and the surrounding cell membrane. Although not the first study describing a purification scheme for the 110K-calmodulin complex, a procedure for the isolation of stable 110K-calmodulin complex both pure and in high yield is presented; moreover, isolation is without loss of the associated calmodulin molecules since a previously determined ratio in isolated microvillar cytoskeletons of calmodulin to 110-kD polypeptide of 3.3:1 is preserved. We have found that removal of calmodulin from the complex by the calmodulin antagonists W7 or W13 results in precipitation of the 110-kD polypeptide with calmodulin remaining in solution. The interaction of 110K-calmodulin with beef skeletal muscle F-actin has been examined. Cosedimentation assays of 110K-calmodulin samples incubated with F-actin show the amount of 110K-calmodulin associating with F-actin to be ATP, calcium, and protein concentration dependent; however, relatively salt independent. In calcium, approximately 30% of the calmodulin remains in the supernatant rather than cosedimenting with the 110-kD polypeptide and actin. Electron microscopy of actin filaments after incubation with 110K-calmodulin in either calcium- or EGTA-containing buffers show polarized filaments often laterally associated. Each individual actin filament is seen to exhibit an arrowhead appearance characteristic of actin filaments after their incubation with myosin fragments, heavy meromyosin and subfragment 1. In some cases projections having a 33-nm periodicity are observed. This formation of periodically spaced projections on actin filaments provides further compelling evidence that the 110K-calmodulin complex is the bridge between actin and the microvillar membrane.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.