Pellino‐2 in nonimmune cells: novel interaction partners and intracellular localization
Autor: | Ove Bruland, Ingvild Aukrust, Ileana M. Cristea, Cecilie Bredrup, Eyvind Rødahl |
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Rok vydání: | 2021 |
Předmět: |
Nigericin
Ubiquitin-Protein Ligases Active Transport Cell Nucleus Biophysics Biochemistry chemistry.chemical_compound Structural Biology Two-Hybrid System Techniques Genetics medicine Humans Protein Interaction Maps Molecular Biology Cells Cultured Cell Nucleus Innate immune system biology Chemistry Kinase Nuclear Proteins Potassium channel blocker Cell Biology Fibroblasts Cell biology Ubiquitin ligase HEK293 Cells biology.protein Tumor necrosis factor alpha Nuclear localization sequence Intracellular Protein Binding medicine.drug |
Zdroj: | FEBS Letters |
ISSN: | 1873-3468 0014-5793 |
Popis: | 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. publishedVersion |
Databáze: | OpenAIRE |
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