PML-Nuclear Bodies Regulate the Stability of the Fusion Protein Dendra2-Nrf2 in the Nucleus
Author(s) -
Andrea Flores Burroughs,
Sylvia Eluhu,
Diva S. Whalen,
J. Shawn Goodwin,
Amos M. Sakwe,
Ifeanyi Arinze
Publication year - 2018
Publication title -
cellular physiology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.486
H-Index - 87
eISSN - 1421-9778
pISSN - 1015-8987
DOI - 10.1159/000490033
Subject(s) - ubiquitin ligase , microbiology and biotechnology , nucleus , cytoplasm , nuclear export signal , nuclear transport , transcription factor , proteasome , chemistry , ubiquitin , cell nucleus , nuclear localization sequence , biochemistry , biology , gene
Nuclear factor erythroid 2-related factor 2 (Nrf2) is a basic leucine-zipper transcription factor essential for cellular responses to oxidative stress. Degradation of Nrf2 in the cytoplasm, mediated by Keap1-Cullin3/RING box1 (Cul3-Rbx1) E3 ubiquitin ligase and the proteasome, is considered the primary pathway controlling the cellular abundance of Nrf2. Although the nucleus has been implicated in the degradation of Nrf2, little information is available on how this compartment participates in degrading Nrf2.
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