Organization, chemistry, and assembly of the cytoskeletal apparatus of the intestinal brush border.

No abstract is available for this paper.

• Publication year

  1985

• Venue

  Annual Review of Cell Biology

• Publication date

  Unknown publication date

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1146/ANNUREV.CB.01.110185.001233PMID 3916317
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Development of the structural components of the brush border in absorptive cells of the chick intestine

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• Evidence for the association of villin with core filaments and rootlets of intestinal epithelial microvilli

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• Structural and functional properties of the non-muscle tropomyosins

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• Comparison of Ca++-regulated events in the intestinal brush border

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• Role of myosin in terminal web contraction in isolated intestinal epithelial brush borders

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• Membrane insertion of the microvillar 110-kDa protein of the enterocyte.

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• Biosynthesis of intestinal microvillar proteins

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• Studies on the spectrin-like protein from the intestinal brush border, TW 260/240, and characterization of its interaction with the cytoskeleton and actin

  1984cited by this paper
• The 110,000-dalton actin- and calmodulin-binding protein from intestinal brush border is a myosin-like ATPase.

  1984cited by this paper
• Identity of p36K phosphorylated upon Rous sarcoma virus transformation with a protein purified from brush borders; calcium‐dependent binding to non‐erythroid spectrin and F‐actin.

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• The brush border cytoskeleton is not static: in vivo turnover of proteins

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• Changes in the distribution of the 34-kdalton tyrosine kinase substrate during differentiation and maturation of chicken tissues

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• The microvillus 110K cytoskeletal protein is an integral membrane protein.

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• Phosphorylation controls brush border motility by regulating myosin structure and association with the cytoskeleton.

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• Characterization of the 110-kdalton actin-calmodulin-, and membrane- binding protein from microvilli of intestinal epithelial cells

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• Fodrin is the general spectrin-like protein found in most cells whereas spectrin and the TW protein have a restricted distribution.

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• Mechanism of brush border contractility studied by the quick-freeze, deep-etch method

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• Demonstration of three distinct calcium-binding sites in villin, a modulator of actin assembly.

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• Structural and functional relationship between the membrane and the cytoskeleton in brush border microvilli.

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• Reactivation of intestinal epithelial cell brush border motility: ATP- dependent contraction via a terminal web contractile ring

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• Organization of actin, myosin, and intermediate filaments in the brush border of intestinal epithelial cells

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• Organization of the cross-filaments in intestinal microvilli

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• Analysis of cytoskeletal proteins and Ca2+-dependent regulation of structure in intestinal brush borders from rachitic chicks.

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• The intracellular localization of the microvillus 110K protein, a component considered to be involved in side-on membrane attachment of F-actin.

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• Erythroid spectrin, brain fodrin, and intestinal brush border proteins (TW-260/240) are related molecules containing a common calmodulin-binding subunit bound to a variant cell type-specific subunit.

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