AI Article Synopsis
- The study identified six new partners that interact with Pellino-2, some of which are involved in various cellular functions and are located in different parts of the cell.
- Pellino-2 normally resides in the cytoplasm of nonimmune cells but can move to the nucleus in response to changes in potassium levels, demonstrating its dynamic movement and importance in cellular processes.
Article Abstract
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.
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| http://dx.doi.org/10.1002/1873-3468.14212 | DOI Listing |
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