title: Actin dynamics: old friends with new stories.
abstract: Actin dynamics, or the rapid turnover of actin filaments, play a central role in numerous cellular processes. A large and diverse cast of characters, accessory proteins known as actin-binding proteins, modulate actin dynamics. They do this by binding to the monomer pool, interacting with the side and ends of filaments, creating breaks along a filament, and generating new filaments de novo. Recent biochemical and single-filament imaging analyses of several conserved classes of plant actin-binding proteins reveal unusual and unexpected properties. Examples that are highlighted in this review include: an abundant monomer-binding protein that catalyzes nucleotide exchange; a barbed-end capping protein that is dissociated from filament ends by the signaling lipid, phosphatidic acid; a villin-like bundling protein that lacks all Ca(2+)-regulated activities; and a formin family member that is non-processive and is sufficient to generate actin filament bundles. These and other stories motivate a careful description of the properties of plant proteins in vitro as a prelude to greater insight into the molecular mechanism(s) underlying the regulation of actin dynamics in vivo.
authors.affiliation: Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-2064, USA. laurent@bilbo.bio.prudue.edu
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Staiger
authors.forename: Laurent
authors.initials: L
authors.lastname: Blanchoin
mesh_terms: D000199:Actins / Q000378:metabolism*; D008840:Microfilament Proteins / Q000378:metabolism*; D010940:Plant Proteins / Q000378:metabolism*; D010944:Plants / Q000378:metabolism
chemical_list: D000199:Actins; D008840:Microfilament Proteins; D010940:Plant Proteins