Pellino-2 in nonimmune cells: novel interaction partners and intracellular localization.
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 nonimmune 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, ... NIMA-related kinase 9, tumor necrosis factor receptor-associated factor 7, cyclin-F, roundabout homolog 1, and disheveled homolog 2. Pellino-2 showed cytoplasmic localization in a wide range of nonimmune 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 tetraethylammonium. 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 influenced by potassium efflux.
Mesh Terms:
Active Transport, Cell Nucleus, Cell Nucleus, Cells, Cultured, Fibroblasts, HEK293 Cells, Humans, Nuclear Proteins, Protein Binding, Protein Interaction Maps, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases
Active Transport, Cell Nucleus, Cell Nucleus, Cells, Cultured, Fibroblasts, HEK293 Cells, Humans, Nuclear Proteins, Protein Binding, Protein Interaction Maps, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases
FEBS Lett
Date: Dec. 01, 2020
PubMed ID: 34674267
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