Inhibition of actin filament depolymerization by the Dictyostelium 30,000-D actin-bundling protein

We have studied the effect of the Dictyostelium discoideum 30,000-D actin-bundling protein on the assembly and disassembly of pyrenyl-labeled actin in vitro. The results indicate that the protein is a potent inhibitor of the rate of actin depolymerization. The inhibition is rapid, dose dependent, an...

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Bibliographic Details
Published in:The Journal of cell biology 1992-11, Vol.119 (3), p.559-567
Main Authors: Zigmond, S.H. (University of Pennsylvania, Philadelphia, PA), Furukawa, R, Fechheimer, M
Format: Article
Language:English
Subjects:
Actins
Actins - metabolism
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Calcium-Binding Proteins - isolation & purification
Calcium-Binding Proteins - metabolism
Carrier proteins
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Cell Biology
Cell motility
Cellular biology
Contractile proteins
Depolymerization
Dictyostelium - metabolism
Fluorescence
Fundamental and applied biological sciences. Psychology
Gelsolin
GLOBULINAS
GLOBULINE
Holoproteins
INHIBICION
INHIBITION
Kinetics
Life Sciences & Biomedicine
Macromolecular Substances
Microfilament proteins
Microfilament Proteins - isolation & purification
Microfilament Proteins - metabolism
Microfilaments
MIXOMICETES
Molecular Weight
Monomers
MYXOMYCETES
Nucleation
Polymerization
PROTEINAS
PROTEINAS VEGETALES
PROTEINE
PROTEINE VEGETALE
Proteins
REACCIONES QUIMICAS
REACTION CHIMIQUE
Science & Technology
Time Factors
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Description
Summary:We have studied the effect of the Dictyostelium discoideum 30,000-D actin-bundling protein on the assembly and disassembly of pyrenyl-labeled actin in vitro. The results indicate that the protein is a potent inhibitor of the rate of actin depolymerization. The inhibition is rapid, dose dependent, and is observed at both ends of the filament. There is little effect of 30-kD protein on the initial rate of elongation from F-actin seeds or on the spontaneous nucleation of actin polymerization. We could detect little or no effect on the critical concentration. The novel feature of these results is that the filament ends are free for assembly but are significantly impaired in disassembly with little change in the critical concentration at steady state. The effects appear to be largely independent of the cross-linking of actin filaments by the 30-kD protein. Actin cross-linking proteins may not only cross-link actin filaments, but may also differentially protect filaments in cells from disassembly and promote the formation of localized filament arrays with enhanced stability
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.119.3.559