A gelsolin-related actin-severing protein with fully reversible actin-binding properties from the tail muscle of crayfish, Astacus leptodactylus
نویسندگان
چکیده
منابع مشابه
The actin filament-severing domain of plasma gelsolin
Gelsolin, a multifunctional actin-modulating protein, has two actin-binding sites which may interact cooperatively. Native gelsolin requires micromolar Ca2+ for optimal binding of actin to both sites, and for expression of its actin filament-severing function. Recent work has shown that an NH2-terminal chymotryptic 17-kD fragment of human plasma gelsolin contains one of the actin-binding sites,...
متن کاملOntogeny of osmoregulation in the crayfish Astacus leptodactylus.
Osmoregulation was studied during the postembryonic development of Astacus leptodactylus Eschscholtz 1823 in juvenile stages 1-8 and in adults. Juveniles hatch and later stages develop in freshwater or in moderately saline waters. The time of acclimation from freshwater to a saline medium increased from early juveniles to adults. At all stages, it was longer than in comparable stages of marine ...
متن کاملBinding of phosphate, aluminum fluoride, or beryllium fluoride to F-actin inhibits severing by gelsolin.
Actin exhibits ATPase activity of unknown function that increases when monomers polymerize into filaments. Differences in the kinetics of ATP hydrolysis and the release of the hydrolysis products ADP and inorganic phosphate suggest that phosphate-rich domains exist in newly polymerized filaments. We examined whether the enrichment of phosphate on filamentous ADP-actin might modulate the severin...
متن کاملFreshwater crayfish Astacus leptodactylus (Eschscholtz, 1823) accumulates and depurates copper.
Cu accumulation and depuration in various tissues of the crayfish Astacus leptodactylus was investigated. Adult specimens were exposed to 0.5, 2.5 and 5.0 mg Cu/L under static conditions for three weeks. At the end of the 3rd week the specimens were divided into three groups and left in dechlorinated water for either 1, 2 or 3 weeks for depuration. After 7, 14 and 21 days, four crayfish from ea...
متن کاملDirect observation of actin filament severing by gelsolin and binding by gCap39 and CapZ
Dynamic behavior of actin filaments in cells is the basis of many different cellular activities. Remodeling of the actin filament network involves polymerization and depolymerization of the filaments. Proteins that regulate these behaviors include proteins that sever and/or cap actin filaments. This report presents direct observation of severing of fluorescently-labeled actin filaments. Coversl...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1994
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1994.00727.x