Actin and actin-binding proteins in higher plants |
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Authors: | David W. McCurdy David R. Kovar Christopher J. Staiger |
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Affiliation: | (1) School of Biological and Chemical Sciences, University of Newcastle, 2308 Callaghan, NSW, Australia;(2) Department of Biological Sciences, Purdue University, West Lafayette, Indiana |
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Abstract: | Summary The actin cytoskeleton is a complex and dynamic structure that participates in diverse cellular events which contribute to plant morphogenesis and development. Plant actins and associated actin-binding proteins are encoded by large, differentially expressed gene families. The complexity of these gene families is thought to have been conserved to maintain a pool of protein isovariants with unique properties, thus providing a mechanistic basis for the observed diversity of plant actin functions. Plants contain actin-binding proteins which regulate the supramolecular organization and function of the actin cytoskeleton, including monomer-binding proteins (profilin), severing and dynamizing proteins (ADF/cofilin), and side-binding proteins (fimbrin, 135-ABP/villin, 115-ABP). Although significant progress in documenting the biochemical activities of many of these classes of proteins has been made, the precise roles of actin-binding proteins in vivo awaits clarification by detailed mutational analyses.Dedicated to Professor Brian E. S. Gunning on the occasion of his 65th birthday |
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Keywords: | Actin-bundling protein/villin Actin depolymerization factor/cofilin Cytoskeleton Fimbrin/plastin Plant cell morphogenesis Profilin |
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