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dc.contributor.authorCristea, Ileana
dc.contributor.authorBruland, Ove
dc.contributor.authorRødahl, Eyvind
dc.contributor.authorBredrup, Cecilie
dc.description.abstractPellino-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.en_US
dc.rightsNavngivelse-Ikkekommersiell 4.0 Internasjonal*
dc.titlePellino-2 in nonimmune cells: novel interaction partners and intracellular localizationen_US
dc.typeJournal articleen_US
dc.typePeer reviewed
dc.rights.holderCopyright 2021 The Authorsen_US
dc.source.journalFEBS Lettersen_US
dc.identifier.citationFEBS Letters. 2021en_US

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Navngivelse-Ikkekommersiell 4.0 Internasjonal
Except where otherwise noted, this item's license is described as Navngivelse-Ikkekommersiell 4.0 Internasjonal