ArticleThe Journal of cell biology1982
Organization of the cross-filaments in intestinal microvilli.
Article in The Journal of cell biology, 1982. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 68 citations in OpenAlex.
- Molecular model of the microvillar cytoskeleton and organization of the brush border.PloS one · 2010Article
- Fluid and Solute Transport in Bone: Flow-Induced Mechanotransduction.Annual review of fluid mechanics · 2009Article
- Mechanotransduction and strain amplification in osteocyte cell processes.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Structural and functional lesions in brush border of human polarized intestinal Caco-2/TC7 cells infected by members of the Afa/Dr diffusely adhering family of Escherichia coli.Infection and immunity · 2000Article
- Molecular motors are differentially distributed on Golgi membranes from polarized epithelial cells.The Journal of cell biology · 1994Article
- Localization of brush border cytoskeletal proteins in gastric oxynticopeptic cells from the bullfrog Rana catesbeiana.Cell and tissue research · 1994Article
- 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
- Role of microtubules in polarized delivery of apical membrane proteins to the brush border of the intestinal epithelium.The Journal of cell biology · 1989Article
- Reassociation of microvillar core proteins: making a microvillar core in vitro.The Journal of cell biology · 1989Article
- 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
- The 110-kD protein-calmodulin complex of the intestinal microvillus is an actin-activated MgATPase.The Journal of cell biology · 1987Article
- Changes in villin synthesis and subcellular distribution during intestinal differentiation of HT29-18 clones.The Journal of cell biology · 1987Article
- A possible mechanism of morphometric changes in dendritic spines induced by stimulation.Cellular and molecular neurobiology · 1985Review
- Microvillus 110K-calmodulin: effects of nucleotides on isolated cytoskeletons and the interaction of the purified complex with F-actin.The Journal of cell biology · 1985Article
- Brush border cytoskeleton and integration of cellular functions.The Journal of cell biology · 1984Review
- The brush border cytoskeleton is not static: in vivo turnover of proteins.The Journal of cell biology · 1984Article
- Studies on the spectrin-like protein from the intestinal brush border, TW 260/240, and characterization of its interaction with the cytoskeleton and actin.The Journal of cell biology · 1984Article
- Characterization of the 110-kdalton actin-calmodulin-, and membrane-binding protein from microvilli of intestinal epithelial cells.The Journal of cell biology · 1983Article
- Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells.The Journal of cell biology · 1983Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
We studied the arrangement of the cross-filaments in intestinal microvilli to understand how microfilaments interact with the membrane. Observations on thin-sectioned or negatively stained microvilli with the electron microscope demonstrate that the cross-filaments on the core bundle lie opposite to one another and are spaced 32.5 nm apart. In sections grazing through the membranes, the cross-filaments appear as transverse stripes in a barber-polelike arrangement. The cross-filaments point away from the microvillus tip. This subfragments S1 or HMM. The cross filaments are associated not only with the microfilaments but also with electron-dense patches on the inside surface of the membrane. These results suggest the cross-filaments are arranged as a double helix around the core bundle. Furthermore, the cross-filaments can serve as in situ markers for microvillar polarity. Lastly, the cross-filaments interact not only with specific portions on the actin filaments but also with dense patches on the membrane. These observations are summarized in a model of the microvillus cytoskeleton.
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Registered trials
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.