The DOI matches its Crossref record; 8 of the 8 references it cites were found in a registry or an index.
The Carboxy-Terminal Neh3 Domain of Nrf2 Is Required for Transcriptional Activation
Open accessAbstract
Nrf2 is a transcription factor critical for the maintenance of cellular redox homeostasis. We have previously found that Nrf2 is a labile protein, and its activation in cells under stress involves mechanisms leading to its stabilization. As a modular protein, Nrf2 possesses distinct transactivation and DNA binding domains essential for its transcriptional activity. In this study, we found that the C-terminal "Neh3" domain of Nrf2 is also important for its activity. Deletion of the last 16 amino acids of the protein completely abolishes its ability to activate both reporter and endogenous gene expression. Using site-directed mutagenesis, we have identified a stretch of amino acids within this region that are essential for its activity and that are found to be conserved across species and among other members of the CNC-bZIP family. Importantly, deletion of the final 16 amino acids of Nrf2 does not influence its dimerizing capability, DNA binding activity, or subcellular localization, although it does increase the half-life of the protein. In addition, this region was found to be important for interaction with CHD6 (a chromo-ATPase/helicase DNA binding protein) in a yeast two-hybrid screen. RNA interference-mediated knockdown of CHD6 reduced both the basal and tert-butylhydroquinone-inducible expression of NQO1, a prototypical Nrf2 target gene. These data suggest that the Neh3 domain may act as a transactivation domain and that it is possibly involved in interaction with components of the transcriptional apparatus to affect its transcriptional activity.
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“Since Nrf2 is expressed constitutively and its steady-state level appears to be maintained in part by a Keap1-dependent degradation process (12, 18, 36), we sought to determine whether Nrf2CT 16 can still be regulated by Keap1.”
BackgroundInfluentialNguyen, T., Sherratt, P. J., Huang, H.-C., Yang, C. S., & Pickett, C. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207293200 · Cited by 615
Self-citationTargeted disruption of Nrf2 causes regenerative immune-mediated hemolytic anemia
Lee, J.-M., Chan, K., Kan, Y. W., & Johnson, J. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0403620101 · Cited by 120
Cited by
The KEAP1-NRF2 system: a thiol-based sensor-effector apparatus for maintaining redox homeostasis
Yamamoto, M., Kensler, T. W., & Motohashi, H. (2018) · Physiological Reviews · doi:10.1152/physrev.00023.2017 · Cited by 1,968
NRF2, a Transcription Factor for Stress Response and Beyond
He, F., Ru, X., & Wen, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134777 · Cited by 1,820
Nrf2 signaling pathway: pivotal roles in inflammation
Ahmed, S. M. U., Luo, L., Namani, A., Wang, X. J., & Tang, X. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.11.005 · Cited by 1,794
Linker, R. A., Lee, D.-H., Ryan, S., van Dam, A. M., Conrad, R., Bista, P., Zeng, W., Hronowsky, X., Buko, A., Chollate, S., et al. (2011) · Brain · doi:10.1093/brain/awq386 · Cited by 1,155
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease
Ngo, V., & Duennwald, M. L. (2022) · Antioxidants · doi:10.3390/antiox11122345 · Cited by 1,130
Metadata
- Authors
- Nioi, P., Nguyen, T., Sherratt, P. J., & Pickett, C. B.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 2005-12-01
- Volume
- 25
- Issue
- 24
- Pages
- 10895-10906
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- OpenAlex
- W1999872962
- Cited by
- 381
- References
- 8
- FWCI
- 1.27
- Type
- journal article
- Language
- en
- Open access
- green
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- Nioi, P., Nguyen, T., Sherratt, P. J., & Pickett, C. B. (2005). The Carboxy-Terminal Neh3 Domain of Nrf2 Is Required for Transcriptional Activation. Molecular and Cellular Biology. https://doi.org/10.1128/mcb.25.24.10895-10906.2005
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