ECB-ART-31320
J Cell Biol
1991 Dec 01;1156:1611-20. doi: 10.1083/jcb.115.6.1611.
Characterization of actin filament severing by actophorin from Acanthamoeba castellanii.
Maciver SK
,
Zot HG
,
Pollard TD
.
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Actophorin is an abundant 15-kD actinbinding protein from Acanthamoeba that is thought to form a nonpolymerizable complex with
actin monomers and also to reduce the viscosity of polymerized
actin by severing filaments (Cooper et al., 1986. J. Biol. Chem. 261:477-485). Homologous proteins have been identified in sea urchin, chicken, and mammalian tissues. Chemical crosslinking produces a 1:1 covalent complex of
actin and actophorin. Actophorin and
profilin compete for crosslinking to
actin monomers. The influence of actophorin on the steady-state
actin polymer concentration gave a Kd of 0.2 microM for the complex of actophorin with
actin monomers. Several new lines of evidence, including assays for
actin filament ends by elongation rate and depolymerization rate, show that actophorin severs
actin filaments both at steady state and during spontaneous polymerization. This is confirmed by direct observation in the light microscope and by showing that the effects of actophorin on the low shear viscosity of polymerized
actin cannot be explained by monomer sequestration. The severing activity of actophorin is strongly inhibited by stoichiometric concentrations of phalloidin or millimolar concentrations of inorganic phosphate.
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1757465
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PMC2289216
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J Cell Biol
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[+]
Genes referenced:
coel1
LOC100887844
LOC100893907
LOC590297
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