Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization

Albina Orlova; Alexander Shvetsov; Vitold E Galkin; Dmitry S Kudryashov; Peter A Rubenstein; Edward H Egelman; Emil Reisler

doi:10.1073/pnas.0407525102

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Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization

Journal article

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Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization

Albina Orlova, Alexander Shvetsov, Vitold E Galkin, Dmitry S Kudryashov, Peter A Rubenstein, Edward H Egelman and Emil Reisler

Proceedings of the National Academy of Sciences - PNAS, Vol.101(51), pp.17664-17668

12/21/2004

DOI: 10.1073/pnas.0407525102

PMCID: PMC539747

PMID: 15591338

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Abstract

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 to regulate the polymerization state. It has become increasingly apparent that the ability of different proteins to bind to and regulate actin filament dynamics depends on the ability of the filament to exist in altered conformations. Yet, little is known about how these conformational changes occur at the molecular level. We have destabilized F-actin filaments by forming a disulfide that locks the “hydrophobic plug” to the body of the actin subunit or by altering the C terminus of actin with a tetramethylrhodamine label. We also examined F-actin filaments at short times after the initiation of polymerization. In all three cases, a substantial fraction of protomers can be found in a “tilted” state that also is induced by actin depolymerizing factor/cofilin proteins. These observations suggest that F-actin filaments are annealed over time into a stable filament and that actin-depolymerizing proteins can effect a time reversal of polymerization.

Biological Sciences

cytoskeleton

image analysis

Details

Title: Subtitle: Actin-destabilizing factors disrupt filaments by means of a time reversal of polymerization
Creators: Albina Orlova - Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733
Alexander Shvetsov - Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733
Vitold E Galkin - Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733
Dmitry S Kudryashov - Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733
Peter A Rubenstein - Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733
Edward H Egelman - Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733
Emil Reisler - Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733
Resource Type: Journal article
Publication Details: Proceedings of the National Academy of Sciences - PNAS, Vol.101(51), pp.17664-17668
DOI: 10.1073/pnas.0407525102
PMID: 15591338
PMCID: PMC539747
NLM abbreviation: Proc Natl Acad Sci U S A
ISSN: 0027-8424
eISSN: 1091-6490
Publisher: National Academy of Sciences
Language: English
Date published: 12/21/2004
Academic Unit: Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9984025288102771

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