Click
here to close Hello! We notice that
you are using Internet Explorer, which is not supported by Echinobase
and may cause the site to display incorrectly. We suggest using a
current version of Chrome,
FireFox,
or Safari.
J Muscle Res Cell Motil
1986 Apr 01;72:133-41. doi: 10.1007/bf01753414.
Show Gene links
Show Anatomy links
The effects of a 45 000 molecular weight protein from unfertilized sea urchin eggs and its 1:1 actin complex on actin filaments.
Coluccio LM
,
Sedlar PA
,
Bryan J
.
???displayArticle.abstract???
A 45 kDa actin-binding protein (SU45) has been isolated previously from egg extracts of the Hawaiian sea urchin Tripneustes gratilla by DEAE Sephacel, Sephadex G-75 and hydroxyapatite chromatography. Using pyrene-labelled rabbit skeletal muscle actin, we have found that when SU45 is added to actin in the presence of calcium and the salt concentration is increased, the initial rate of actin assembly is accelerated. Moreover, the final polymer concentration is reduced indicating that SU45 caps the preferred end of actin filaments shifting the critical concentration (Cc) to that of the nonpreferred end. Determination of the Cc as a function of the concentration of SU45 gave an apparent KD of 1 nM. Dilution of F-actin to below its Cc, into buffers containing SU45 and Ca2+ resulted in a sharp increase in the rate of depolymerization; reducing the Ca2+ concentration attenuated this effect. Incubation of SU45 with rabbit skeletal muscle G-actin yielded a 1:1 complex which held 45Ca2+ tightly with a dissociation half-time of 10.8 days. By kinetic analyses of assembly in the presence of the SU45-actin complex and dilution-induced disassembly of filaments precapped with complex, we have estimated both the association rate constant (4.0 X 10(4)M-1s-1) and the dissociation rate constant (0.05s-1) for the nonpreferred ends of actin filaments. Finally, dilution of F-actin to below its Cc, into complex in either Ca2+ or EGTA resulted in a much slower depolymerization consistent with a rapid capping of the preferred end by the SU45-actin complex.
Bonder,
Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament.
1983, Pubmed
Bonder,
Direct measurement of critical concentrations and assembly rate constants at the two ends of an actin filament.
1983,
Pubmed
Bonder,
Direct electron microscopic visualization of barbed end capping and filament cutting by intestinal microvillar 95-kdalton protein (villin): a new actin assembly assay using the Limulus acrosomal process.
1983,
Pubmed
Bretscher,
Villin is a major protein of the microvillus cytoskeleton which binds both G and F actin in a calcium-dependent manner.
1980,
Pubmed
Bryan,
Kinetic analysis of F-actin depolymerization in the presence of platelet gelsolin and gelsolin-actin complexes.
1985,
Pubmed
Bryan,
Actin-gelsolin interactions. Evidence for two actin-binding sites.
1984,
Pubmed
Coluccio,
Phalloidin enhances actin assembly by preventing monomer dissociation.
1984,
Pubmed
Cooper,
Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization.
1983,
Pubmed
Craig,
Regulation of actin polymerization by villin, a 95,000 dalton cytoskeletal component of intestinal brush borders.
1980,
Pubmed
Doi,
Actin polymerization. The effect of brevin on filament size and rate of polymerization.
1984,
Pubmed
Giffard,
Ca2+-dependent binding of severin to actin: a one-to-one complex is formed.
1984,
Pubmed
Glenney,
F actin assembly modulated by villin: Ca++-dependent nucleation and capping of the barbed end.
1981,
Pubmed
Glenney,
Calcium control of microfilaments: uncoupling of the F-actin-severing and -bundling activity of villin by limited proteolysis in vitro.
1981,
Pubmed
Hasegawa,
Fragmin: a calcium ion sensitive regulatory factor on the formation of actin filaments.
1980,
Pubmed
Hosoya,
A 45,000-mol-wt protein-actin complex from unfertilized sea urchin egg affects assembly properties of actin.
1984,
Pubmed
,
Echinobase
Kane,
Actin polymerization and interaction with other proteins in temperature-induced gelation of sea urchin egg extracts.
1976,
Pubmed
,
Echinobase
Kane,
Preparation and purification of polymerized actin from sea urchin egg extracts.
1975,
Pubmed
,
Echinobase
Karr,
Mechanism of microtubule depolymerization. Correlation of rapid induced disassembly experiments with a kinetic model for endwise depolymerization.
1980,
Pubmed
Korn,
Actin polymerization and its regulation by proteins from nonmuscle cells.
1982,
Pubmed
Kouyama,
Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin.
1981,
Pubmed
Kristofferson,
Dynamics of linear protein polymer disassembly.
1980,
Pubmed
Kurth,
Purification and characterization of a gelsolin-actin complex from human platelets. Evidence for Ca2+-insensitive functions.
1983,
Pubmed
Kurth,
Platelet activation induces the formation of a stable gelsolin-actin complex from monomeric gelsolin.
1984,
Pubmed
MacLean-Fletcher,
Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-association.
1980,
Pubmed
Mooseker,
Regulation of microvillus structure: calcium-dependent solation and cross-linking of actin filaments in the microvilli of intestinal epithelial cells.
1980,
Pubmed
Pollard,
Direct measurement of actin polymerization rate constants by electron microscopy of actin filaments nucleated by isolated microvillus cores.
1981,
Pubmed
Spudich,
The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin.
1971,
Pubmed
Sugino,
Effect of fragmin on actin polymerization: evidence for enhancement of nucleation and capping of the barbed end.
1982,
Pubmed
Tobacman,
The kinetics of actin nucleation and polymerization.
1983,
Pubmed
Walsh,
Effect of villin on the kinetics of actin polymerization.
1984,
Pubmed
Wang,
Isolation of calcium-dependent platelet proteins that interact with actin.
1981,
Pubmed
Wang,
A 45,000-mol-wt protein from unfertilized sea urchin eggs severs actin filaments in a calcium-dependent manner and increases the steady-state concentration of nonfilamentous actin.
1984,
Pubmed
,
Echinobase
Wegner,
Head to tail polymerization of actin.
1976,
Pubmed
Yin,
Control of cytoplasmic actin gel-sol transformation by gelsolin, a calcium-dependent regulatory protein.
1979,
Pubmed
Yin,
Ca2+ control of actin filament length. Effects of macrophage gelsolin on actin polymerization.
1981,
Pubmed