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- W2294569968 abstract "A mounting body of evidence has shown the importance of βArrestin1 in the nucleus, however the mechanism of how βArrestin1 enters the nucleus to mediate its functions is not known. Despite a high homology between the two members of the βarrestin family, they do not localize to the same subcellular compartments. βarrestin1 can be seen ubiquitously throughout the cell while βarrestin2 is excluded from the nucleus by a functional NES in its C terminus. While no nuclear import signal has been identified in either βarrestin, it has been noted that an intact N-terminal domain is required for nuclear localization of both members. To explore this further, we visualized the localization of full-length βarrestin1 as well as N-terminal domain truncation and deletion mutants. Based on the results, a seven-residue candidate nuclear localization sequence was found in βarrestin1. Mutation of these residues led to a loss of βarrestin1 nuclear localization by inhibiting its binding to the nuclear import machinery. Functionally, expression of wild type βArrestin1 is able to enhance the transcriptional activity of NF-κB following bradykinin stimulation and the nuclear localization of βArrestin1 is critical for this effect. Loss of nuclear localization of βArrestin1 led to an inhibition of NF-κB mediated gene transcription by affecting the post-translational modification profile of p65/RelA following bradykinin stimulation, which led to a decrease in effective promoter binding. In conclusion, this study identifies structural determinants for the nuclear localization of βArrestin1, and demonstrates its role in regulating NF-κB activation." @default.
- W2294569968 created "2016-06-24" @default.
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- W2294569968 date "2010-04-01" @default.
- W2294569968 modified "2023-10-16" @default.
- W2294569968 title "Identification of the Nuclear Localization Sequence in Beta Arrestin1: functional inplications in NF‐(kappa)B activation" @default.
- W2294569968 doi "https://doi.org/10.1096/fasebj.24.1_supplement.586.5" @default.
- W2294569968 hasPublicationYear "2010" @default.
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