Actin-Destabilizing Factors Disrupt Filaments by Means of a Time Reversal of Polymerization

Actin, one of the most highly conserved and abundant eukaryotic proteins, is constantly being polymerized and depolymerized within cells as part of cellular motility, tissue formation and repair, and embryonic development. Many proteins exist that bind to monomeric or filamentous (F) forms of actin...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2004-12, Vol.101 (51), p.17664-17668
Hauptverfasser:	Orlova, Albina, Shvetsov, Alexander, Galkin, Vitold E., Kudryashov, Dmitry S., Rubenstein, Peter A., Egelman, Edward H., Reisler, Emil, DeRosier, David J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Actin Cytoskeleton - chemistry Actin Cytoskeleton - genetics Actin Cytoskeleton - metabolism Actin Cytoskeleton - ultrastructure Actin Depolymerizing Factors Actins Analysis Animals Biochemistry Biological Sciences Biopolymers - antagonists & inhibitors Biopolymers - chemistry Biopolymers - metabolism Cellular biology Copolymers Cytoskeleton Destrin Disulfides Kinetics Microfilament Proteins - metabolism Microfilament Proteins - pharmacology Microfilaments Microscopy, Electron Models, Molecular Polymerization Protein Binding - drug effects Protein Conformation - drug effects Protein subunits Protein Subunits - antagonists & inhibitors Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Protein-Tyrosine Kinases - metabolism Proteins Rabbits Rhodamines Scanning electron microscopy Time Factors Yeasts
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