ArticleJournal of muscle research and cell motility1986
Kinetics of actin monomer exchange at the slow growing ends of actin filaments and their relation to the elongation of filaments shortened by gelsolin.
Article in Journal of muscle research and cell motility, 1986. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 39 citations in OpenAlex.
- Gelsolin binds to polyphosphoinositide-free lipid vesicles and simultaneously to actin microfilaments.The Biochemical journal · 2005Article
- Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein.The Journal of cell biology · 1992Article
- Mechanisms of actin rearrangements mediating platelet activation.The Journal of cell biology · 1992Article
- Regulation of water flow by actin-binding protein-induced actin gelatin.Biophysical journal · 1992Article
- Domain structure in actin-binding proteins: expression and functional characterization of truncated severin.The Journal of cell biology · 1991Article
- Gel electrophoresis of native gelsolin and gelsolin-actin complexes.Journal of muscle research and cell motility · 1990Article
- Dictyostelium discoideum plasma membranes contain an actin-nucleating activity that requires ponticulin, an integral membrane glycoprotein.The Journal of cell biology · 1990Article
- Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis.The Journal of cell biology · 1989Article
- Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments.The Journal of cell biology · 1988Article
- Circulating actin-gelsolin complexes following oleic acid-induced lung injury.The American journal of pathology · 1988Article
- Antigenic probes locate a serum-gelsolin-interaction site on the C-terminal part of actin.The Biochemical journal · 1987Article
- Reversible binding of actin to gelsolin and profilin in human platelet extracts.The Journal of cell biology · 1987Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The kinetics of actin monomer exchange with the slow growing pointed ends of actin filaments have been determined by measuring rates of monomer addition to or loss from filaments with their fast-growing barbed ends blocked by the protein gelsolin. Direct measurements of filament length by electron microscopy confirmed that each gelsolin acts as a nucleus for an actin filament. The rate constants ascertained are k- = 0.03 s-1; k+ = 0.06 microM-1 s-1 at 23 degrees C and k- = 0.11 s-1; k+ = 0.09 microM-1 s-1 at 37 degrees C. They are approximately independent of pH from 7.0 to 8.0 at both temperatures. These rates are far slower than those reported on the basis of some electron microscopic studies of filaments assembled on to actin bundles. The rate constants also predict a higher critical monomer concentration for the pointed end at 37 degrees C than at room temperature, consistent with direct measurements of this quantity. The relative slowness of the monomer exchange at the pointed end suggests that actin filaments with blocked barbed ends are relatively stable. The rate of redistribution of actin monomers from filaments stabilized at their barbed ends by gelsolin-calcium complex to longer filaments was measured following removal of Ca2+, which decreases the capacity of gelsolin to nucleate filaments. The elongation occurs at a rate consistent with the measured rates of monomer exchange and is quantitatively described by Hill's model for filament elongation by random exchange of monomers from one end.
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