EurekaMag
+ Translate
+ Most Popular
Advantages and disadvantages of bordeaux mixture and of lime-sulphur used on apples in the growing season
Observations on the Umaria marine bed
10 years of hearing conservation in the Royal Air Force
Chocolate crumb - dairy ingredient for milk chocolate
Effect of daily gelatin ingestion on human scalp hair
Comparison of rice bran and maize bran as feeds for growing and fattening pigs
The composition of pampas-grass (Cortaderia argentea.)
The Accraian Series:
The mechanism of the Liebermann-Burchard reaction of sterols and triterpenes and their esters
Cerebrovascular Doppler ultrasound studies (cv-Doppler)
Toria: PT-303 - first national variety
Hair growth promoting activity of tridax procumbens
Productivity of Pekin x Khaki Campbell ducks
A stable cytosolic expression of VH antibody fragment directed against PVY NIa protein in transgenic potato plant confers partial protection against the virus
Solar treatment of wheat loose smut
Swimmers itch in the Lake of Garda
Bactofugation and the Bactotherm process
The effects of prefrontal lobotomy on aggressive behavior in dogs
Visual rating scales for screening whorl-stage corn for resistance to fall armyworm
Breakdown of seamounts at the trench axis, viewed from gravity anomaly
Kooken; pennsylvania's toughest cave
Recovery of new dinosaur and other fossils from the Early Cretaceous Arundel Clay facies (Potomac Group) of central Maryland, U.S.A
Zubor horny (Bison bonasus) v prirodnych podmienkach Slovensku
The extended Widal test in the diagnosis of fevers due to Salmonella infection
Hair of the american mastodon indicates an adaptation to a semi aquatic habitat

Role of the N- and C-terminal actin-binding domains of gelsolin in barbed filament end capping


Role of the N- and C-terminal actin-binding domains of gelsolin in barbed filament end capping



Biochemistry 30(38): 9327-9334



ISSN/ISBN: 0006-2960

PMID: 1654094

DOI: 10.1021/bi00102a027

Gelsolin is a bivalent Ca(2+)-modulated actin-binding protein that severs, nucleates, and caps filaments. In order to gain a better understanding of the capping mechanism we have studied N- and C-terminal gelsolin fragments, 14NT and 41CT, each of which contains a single functional actin-binding site. The very tight binding measured between gelsolin and the barbed filament end requires gelsolin to greatly decrease the dissociation rate constant of the terminal actin from this end. A mechanism that could account for the observed decrease in dissociation is one in which gelsolin links two actin monomers so that they dissociate more slowly as a dimer. This cannot be the only mechanism, however, since, as shown here, 14NT and 41CT, fragments with single actin-binding sites, decrease the dissociation rate of the capped terminal actin molecule. The observations suggest that these fragments induce a conformational change in the actin monomer that either increases the affinity or alters the kinetics of the terminal actin-actin bond. The available data argue for strengthening of the terminal actin-actin bond.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 018102872

Download citation: RISBibTeXText

Related references

Distinct roles of four gelsolin-like domains of Caenorhabditis elegans gelsolin-like protein-1 in actin filament severing, barbed end capping, and phosphoinositide binding. Biochemistry 49(20): 4349-4360, 2010

Coordinated regulation of platelet actin filament barbed ends by gelsolin and capping protein. Journal of Cell Biology 134(2): 389-399, 1996

Capping protein binding to S100B: implications for the tentacle model for capping the actin filament barbed end. Journal of Biological Chemistry 279(14): 14382-14390, 2004

Actin filament barbed-end capping activity in neutrophil lysates: the role of capping protein-beta 2. Molecular Biology of the Cell 6(12): 1659-1671, 1995

Mapping the functional domains of gcap39 a gelsolin like actin filament capping protein. Journal of Cell Biology 111(5 Part 2): 28A, 1990

Equilibrium constant for binding of an actin filament capping protein to the barbed end of actin filaments. Biochemistry 24(4): 1035-1040, 1985

Cooperativity in F-actin Binding of gelsolin at the barbed end affects the structure of the whole filament. Biophysical Journal 68(2 Part 2): A284, 1995

Control of actin filament dynamics at barbed ends by WH2 domains: from capping to permissive and processive assembly. Cytoskeleton 70(10): 540-549, 2013

Cooperativity in F-actin: binding of gelsolin at the barbed end affects structure and dynamics of the whole filament. Journal of Molecular Biology 260(5): 756-766, 1996

Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end. Journal of Biological Chemistry 281(41): 31021-31030, 2006

Two of the three actin-binding domains of gelsolin bind to the same subdomain of actin. Implications of capping and severing mechanisms. Febs Letters 280(1): 70-74, 1991

Vinculin is a dually regulated actin filament barbed end-capping and side-binding protein. Journal of Biological Chemistry 285(30): 23420-23432, 2010

Rate constant for capping of the barbed ends of actin filaments by the gelsolin-actin complex. European Journal of Biochemistry 155(2): 397-401, 1986

High concentrations of phosphatidylinositol-4,5-bisphosphate may promote actin filament growth by three potential mechanisms: inhibiting capping by neutrophil lysates, severing actin filaments and removing capping protein-beta2 from barbed ends. Biochimica et Biophysica Acta 1358(3): 261-278, 1997

Evidence for functional homology in the F-actin binding domains of gelsolin and a-actinin: implications for the requirements of severing and capping. The Journal of Cell Biology 119(4): 5-42, 1992