Literature DB >> 6129657

Microfilament-membrane interaction: the brush border of intestinal epithelial cells as a model.

K Weber, J R Glenney.   

Abstract

The intestinal epithelium provides an excellent starting material for the isolation of natural microfilament organizations in amounts suitable for biochemical studies. The microvillus filament bundle core and the terminal web provide two distinct microfilament systems. We review the current knowledge of the filament bundle core and the attempts that have been made to reconstitute this structure from actin and its four major associated proteins. We show in addition that a high molecular mass actin-binding protein (TW-260/240) having spectrin-like properties is, next to myosin, the major associated protein of the terminal web retained in isolated brush borders. We summarize the biochemical and morphological evidence for the existence of a class of spectrin-related molecules in the cortical cytoplasm of many cell types. These findings may lead to a new understanding of membrane-microfilament interactions.

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Year:  1982        PMID: 6129657     DOI: 10.1098/rstb.1982.0127

Source DB:  PubMed          Journal:  Philos Trans R Soc Lond B Biol Sci        ISSN: 0962-8436            Impact factor:   6.237


  5 in total

1.  A novel terminal web-like structure in cortical lens fibers: architecture and functional assessment.

Authors:  Kristin J Al-Ghoul; Timothy P Lindquist; Spencer S Kirk; Sean T Donohue
Journal:  Anat Rec (Hoboken)       Date:  2010-11       Impact factor: 2.064

2.  Probing endocytosis from the enterocyte brush border using fluorescent lipophilic dyes: lipid sorting at the apical cell surface.

Authors:  E Michael Danielsen
Journal:  Histochem Cell Biol       Date:  2014-12-20       Impact factor: 4.304

3.  Villin--a marker of brush border differentiation and cellular origin in human renal cell carcinoma.

Authors:  H J Gröne; K Weber; U Helmchen; M Osborn
Journal:  Am J Pathol       Date:  1986-08       Impact factor: 4.307

4.  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.

Authors:  V Gerke; K Weber
Journal:  EMBO J       Date:  1984-01       Impact factor: 11.598

5.  The amino acid sequence of protein II and its phosphorylation site for protein kinase C; the domain structure Ca2+-modulated lipid binding proteins.

Authors:  K Weber; N Johnsson; U Plessmann; P N Van; H D Söling; C Ampe; J Vandekerckhove
Journal:  EMBO J       Date:  1987-06       Impact factor: 11.598

  5 in total

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