Palladin Can Compensate for Arp2/3 Complex Defects and Structurally Organizes Actin-Rich Structures Generated during Listeria monocytogenes Infections
Aaron S Dhanda, A Wayne Vogl, Carol A Otey, Moriah R Beck, and Julian A Guttman Palladin Can Compensate for Arp2/3 Complex Defects and Structurally Organizes Actin-Rich Structures Generated during Listeria monocytogenes Infections FASEB J April 2017 31:741.2
The actin cytoskeleton is co-opted by the invasive and motile bacteria Listeria monocytogenes (Listeria) for their entry, intracellular motility and dissemination from one cell to another. Once inside host cells, these bacteria are propelled by bacterially-generated, Arp2/3-based, actin-rich structures called comet tails. The host protein palladin is a crucial actin crosslinker of motile actin-based structures generated during eukaryotic cell motility. Recently, palladin has been shown to nucleate branched actin filament arrays in vitro. Whether this new actin-nucleating role of palladin is involved in powering cell motility remains unknown.