LAUSR

Pellino-2 is an E3 ubiquitin ligase that mediates intracellular signaling in innate immune pathways. Most studies of endogenous Pellino-2 have been performed in macrophages, but none in non-immune cells. Using yeast two-hybrid screening and co-immunoprecipitation, we identified six novel interaction partners of Pellino-2, with various localizations: insulin receptor substrate 1(IRS-1), NIMA-related kinase 9 (NEK9), tumor necrosis factor receptor-associated factor 7 (TRAF7), cyclin-F, roundabout homolog 1 (ROBO-1), and dishevelled homolog 2 (DVL-2). Pellino-2 showed cytoplasmic localization in a wide range of non-immune cells under physiological potassium concentrations. Treatment with the potassium ionophore nigericin resulted in nuclear localization of Pellino-2, which was reversed by the potassium channel blocker TEA. Live cell imaging revealed intracellular migration of GFP-tagged Pellino-2. In summary, Pellino-2 interacts with proteins at different cellular locations, taking part in dynamic processes that change its intracellular localization.