Structure, assembly, and dynamics of actin filaments in situ and in vitro.
Actin, though highly conserved, exhibits a myriad of diverse functions, most of which ultimately depend on its intrinsic ability to rapidly assemble and disassemble filamentous structures. Many organisms synthesize multiple actin isoforms even within the same cell. Tissue-specific expression patterns and tight developmental regulation as well as a high conservation across species emphasize the functional importance of isoforms. The detailed knowledge of the structure, assembly, and dynamic behavior of actin provides important pieces in solving the puzzle of how the different isoforms can be so versatile despite their extremely high sequence identity.
Schoenenberger
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M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, CH-4506 Basel, Switzerland. Schoenenberg@ubaclu.unibas.ch
Steinmetz
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MO
Stoffler
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Mandinova
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A
Aebi
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U
D000199:Actins / Q000737:chemistry* / Q000502:physiology*; D000818:Animals; D001665:Binding Sites; D003599:Cytoskeleton / Q000737:chemistry*; D004023:Dictyostelium / Q000166:cytology; D049452:Green Fluorescent Proteins; D006801:Humans; D007202:Indicators and Reagents / Q000378:metabolism; D008164:Luminescent Proteins / Q000378:metabolism; D008854:Microscopy, Electron; D013329:Structure-Activity Relationship
D000199:Actins; D007202:Indicators and Reagents; D008164:Luminescent Proteins; D049452:Green Fluorescent Proteins