Key result
Review summarizes structure-function relationships among actin-binding proteins regulating actin cytoskeleton assembly.
Why the study?
Malfunction of cytoskeletal proteins causes various human diseases, and understanding regulation of actin cytoskeleton dynamics is critical for cellular activities.
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Design
Review of actin-binding proteins regulating cytoskeleton assembly
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Consolidates actin-binding protein insights; leaves open validation in cardiovascular cell models.
The dynamic remolding of the actin cytoskeleton is a critical part of most cellular activities, and malfunction of cytoskeletal proteins results in various human diseases. The transition between two forms of actin, monomeric or G-actin and filamentous or F-actin, is tightly regulated in time and space by a large number of signaling, scaffolding and actin-binding proteins (ABPs). New ABPs are constantly being discovered in the post-genomic era. Most of these proteins are modular, integrating actin binding, protein-protein interaction, membrane-binding, and signaling domains. In response to extracellular signals, often mediated by Rho family GTPases, ABPs control different steps of actin cytoskeleton assembly, including filament nucleation, elongation, severing, capping, and depolymerization. This review summarizes structure-function relationships among ABPs in the regulation of actin cytoskeleton assembly.
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Lee et al. (2010) reported a review. This review summarizes structure-function relationships among actin-binding proteins in the regulation of actin cytoskeleton assembly.
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