Abstract
The actin cytoskeleton forms much of the structure needed for the intracellular motility of an assortment of microbes as well as entire cells. The co-factor to the ubiquitin conjugating enzyme Ube2N (Ube2V1) has been implicated in both cancer cell metastasis and lysine-63 ubiquitylation of β actin. As this protein complexes with Ube2N, we sought to investigate whether Ube2N itself was involved in actin-based events occurring during the Listeria monocytogenes infections as well as within motile whole cells. Through examination of L. monocytogenes actin clouds, comet tails and membrane protrusions as well as lamellipodia in migrating cells, we show that Ube2N is recruited to actin-rich structures. When pharmacologically inhibited we demonstrate that Ube2N is crucial for the function of actin-rich structures when associated with the plasma membrane.
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