Effects of villin on the polymerization and subunit exchange of actin
β Scribed by Wang, Yu-Li ;Bonder, Edward M. ;Mooseker, Mark S. ;Taylor, D. Lansing
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1983
- Weight
- 879 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0271-6585
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The G-F transformation of actin was studied in terms of a n interaction between different counterions and actin niacroion by means of electrometric measurements. Due to the polyelectrolyte structure of the actin molecule, the electrostatic interactions must play a predominant role. In this sense the
Villin, a calcium-regu-dted actin-binding protein, modulates the structure and assembly of actin filaments in vitro. It is organized into three domains, the first two of which are homologous. Villin is mainly produced in epithelial cells that develop a brush border and which are responsible for nutr
To discriminate between the influences of a motoneuron and muscle activity on the conformation of actin filaments, the extrinsic polarized fluorescence [of rhodamine-phalloidin and N-(iodoacetylamine)-1-naphthylamine-5-sulfonic acid attached to F-actin] was measured in "ghost" fibers from intact rat