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Direct Interaction between Nrf2 and p21Cip1/WAF1 Upregulates the Nrf2-Mediated Antioxidant Response
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In response to oxidative stress, Nrf2 and p21(Cip1/WAF1) are both upregulated to protect cells from oxidative damage. Nrf2 is constantly ubiquitinated by a Keap1 dimer that interacts with a weak-binding (29)DLG motif and a strong-binding (79)ETGE motif in Nrf2, resulting in degradation of Nrf2. Modification of the redox-sensitive cysteine residues on Keap1 disrupts the Keap1-(29)DLG binding, leading to diminished Nrf2 ubiquitination and activation of the antioxidant response. However, the underlying mechanism by which p21 protects cells from oxidative damage remains unclear. Here we present molecular and genetic evidence suggesting that the antioxidant function of p21 is mediated through activation of Nrf2 by stabilizing the Nrf2 protein. The (154)KRR motif in p21 directly interacts with the (29)DLG and (79)ETGE motifs in Nrf2 and thus competes with Keap1 for Nrf2 binding, compromising ubiquitination of Nrf2. Furthermore, the physiological significance of our findings was demonstrated in vivo using p21-deficient mice.
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“The 154KRR156 motif within p21 directly binds to the DLG and ETGE motifs in Nrf2, thereby competing with Keap1 for Nrf2 binding [26]; but instead of Nrf2 degradation, p21-Nrf2 binding leads to Nrf2 stabilization and increased response to oxidative stress [26].”
From Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022) · cites this paper as [26]
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Itoh, K., Wakabayashi, N., Katoh, Y., Ishii, T., Igarashi, K., Engel, J. D., & Yamamoto, M. (1999) · Genes & Development · doi:10.1101/gad.13.1.76 · Cited by 3,634
Cell Survival Responses to Environmental Stresses Via the Keap1-Nrf2-ARE Pathway
Kensler, T. W., Wakabayashi, N., & Biswal, S. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.46.120604.141046 · Cited by 3,630
Kobayashi, A., Kang, M.-I., Okawa, H., Ohtsuji, M., Zenke, Y., Chiba, T., Igarashi, K., & Yamamoto, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.16.7130-7139.2004 · Cited by 2,224
Zhang, D. D., & Hannink, M. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.22.8137-8151.2003 · Cited by 1,480
Self-citationKeap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex
Zhang, D. D., Lo, S., Cross, J. V., Templeton, D. J., & Hannink, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.24.10941-10953.2004 · Cited by 1,284
Self-citationMcMahon, M., Itoh, K., Yamamoto, M., & Hayes, J. D. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300931200 · Cited by 1,141
Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway
Zhang, D. D. (2006) · Drug Metabolism Reviews · doi:10.1080/03602530600971974 · Cited by 1,105
Self-citationRamos-Gomez, M., Kwak, M.-K., Dolan, P. M., Itoh, K., Yamamoto, M., Talalay, P., & Kensler, T. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.051618798 · Cited by 1,102
Molecular Mechanisms Activating the Nrf2-Keap1 Pathway of Antioxidant Gene Regulation
Kobayashi, M., & Yamamoto, M. P. (2005) · Antioxidants and Redox Signaling · doi:10.1089/ars.2005.7.385 · Cited by 1,087
Wakabayashi, N., Dinkova-Kostova, A. T., Holtzclaw, W. D., Kang, M.-I., Kobayashi, A., Yamamoto, M., Kensler, T. W., & Talalay, P. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307301101 · Cited by 986
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Hu, Z.-L., Lin, Z.-Y., Ren, W.-S., Liu, B., Zhao, H., & Qin, Q. (2024) · International Journal of Ophthalmology · doi:10.18240/ijo.2024.07.21 · Cited by 9
Redox state associated with antitumor and immunomodulatory peptides in cancer
Cruz‐Gregorio, A., Aranda‐Rivera, A. K., Sciutto, E., Fragoso, G., & Pedraza‐Chaverrí, J. (2022) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2022.109414 · Cited by 9
Dhaibar, H. A., Kamberov, L., Carroll, N., Amatya, S., Cosic, D. D., Gómez, O., Vital, S. A., Sivandzade, F., Bhalerao, A., Mancuso, S., et al. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241310994 · Cited by 10
Gorska‐Arcisz, M., Popęda, M., Braun, M., Piasecka, D., Nowak, J. I., Kitowska, K., Stasiłojć, G., Okrój, M., Romańska, H., & Sądej, R. (2024) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-024-00586-6 · Cited by 9
Liu, Q., Mier, J. W., & Panka, D. J. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-115 · Cited by 9
RetractedChen, X., Wang, K., Cederbaum, A. I., & Lu, Y. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.03.021 · Cited by 9
Wang, L., Lewis, T. A., Zhang, Y., Khodier, C., Magesh, S., Chen, L., Inoyama, D., Chen, Y., Zhen, J., Hu, L., et al. (2013) · Europe PMC (PubMed Central) · Cited by 9
Nrf2 in human cancers: biological significance and therapeutic potential
Tian, Y. (2024) · American Journal of Cancer Research · doi:10.62347/lzvo6743 · Cited by 9
Lin, Y., Ku, C., Wuputra, K., Wu, D., & Yokoyama, K. K. (2024) · Cells · doi:10.3390/cells13191648 · Cited by 8
Feng, T., Xu, X., Wang, X., Tang, W., & Lu, Y. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07233-0 · Cited by 8
Self-citationKhalil, M., & Tsao, M. (2025) · Cancers · doi:10.3390/cancers17132199 · Cited by 9
The emerging role of hypoxia and environmental factors in inflammatory bowel disease
Villareal, L., & Xue, X. (2024) · Toxicological Sciences · doi:10.1093/toxsci/kfae004 · Cited by 9
Chen, J., Su, S., Pickar‐Oliver, A., Chiarella, A. M., Hahn, Q., Goldfarb, D., Cloer, E. W., Small, G. W., Sivashankar, S., Ramsden, D. A., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae761 · Cited by 8
Cho, J., Kim, Y. W., Choi, B. Y., & Keum, Y. (2014) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2014.08.007 · Cited by 8
Pinto, B., Melo, T. M., Flister, K. F. T., França, L. M., Moreira, V. R., Kajihara, D., Mendes, N. O., Pereira, S. R. F., Laurindo, F. R. M., & Paes, A. M. D. A. (2022) · Antioxidants · doi:10.3390/antiox11071395 · Cited by 8
Bidzińska, J., Pietro, L. D., Naghshineh, E., Pandini, C., Doria, F., Zaffaroni, N., Gandellini, P., Neidle, S., & Folini, M. (2025) · Cell Death and Disease · doi:10.1038/s41419-025-07908-2 · Cited by 8
Ruan, Y., Cai, Z., Kang, Z., Liang, J., Tian, H., Yu, Q., Zhang, Q., & Lin, W. (2024) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.23808 · Cited by 7
Niture, S. K., Gnatt, A. L., & Jaiswal, A. K. (2013) · Journal of Cell Science · doi:10.1242/jcs.133819 · Cited by 7
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Ko, F., Isoda, F., & Mobbs, C. V. (2014) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2014.0031 · Cited by 7
Vernazza, S., Dellacasa, E., Tirendi, S., Pastorino, L., & Bassi, A. M. (2021) · Nanomaterials · doi:10.3390/nano11061365 · Cited by 7
Allyl-isothiocyanate against colorectal cancer via the mutual dependent regulation of p21 and Nrf2
Ren, X., Zhang, G., Ling, X., Zhang, L., Tian, Y., Zhu, G., Wang, P., Leavenworth, J. W., Luo, L., & Li, F. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176016 · Cited by 8
Kim, J., Choi, S. H., Lee, E., Kang, Y. J., & Kim, H. (2012) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2012.09.012 · Cited by 7
Possible involvement of granulocyte oxidative burst in Nrf2 signaling in cancer.
Jaganjac, M. (2010) · PubMed · Cited by 7
Atia, A., & Abdullah, A. (2014) · International Journal of PharmTech Research · Cited by 7
Yang, Q., Deng, H., Xia, H., Xu, M., Pan, G.-T., Mao, J., Tao, S., Yamanaka, K., & An, Y. (2019) · Free Radical Research · doi:10.1080/10715762.2019.1642472 · Cited by 6
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Currier, J. M., Cheng, W., Menéndez, D., Conolly, R. B., & Chorley, B. N. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155875 · Cited by 6
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Wächter, K., Gohde, B., Szabo, G. B., & Simm, A. (2022) · Nutrients · doi:10.3390/nu14224790 · Cited by 6
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Chen, C., Chen, M., Wen, T., Awasthi, P., Carrillo, N. D., Anderson, R. A., & Cryns, V. L. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.26.564194 · Cited by 6
Ozleyen, A., Kulabas, S. S., Novak, M. J., Cichoń, M., Heras, C. M. D. L., Honda, T., Doveston, R. G., Dinkova‐Kostova, A. T., Grochot‐Przeczek, A., & Tumer, T. B. (2026) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2026.110847 · Cited by 5
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Treindl, F., Zabinsky, E., Kling, S., Schwarz, M., Braeuning, A., & Templin, M. F. (2020) · Archives of Toxicology · doi:10.1007/s00204-020-02680-y · Cited by 5
Nguyen, P. T. T. ‐., Pagé‐Larivière, F., Williams, K. L., O’Brien, J. M., & Crump, D. (2021) · Environmental Toxicology and Chemistry · doi:10.1002/etc.5274 · Cited by 5
Luffarelli, R., Panarello, L., Quatrana, A., Tiano, F., Fortuni, S., Rufini, A., Malisan, F., Testi, R., & Condò, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241612687 · Cited by 5
Satoh, C. I. M. (2015) · Biochemistry & Pharmacology Open Access · doi:10.4172/2167-0501.1000157 · Cited by 5
Jeong, G., Oh, J., & Kim, J. (2019) · Journal of Medicinal Food · doi:10.1089/jmf.2018.4290 · Cited by 5
Lee, Y., Sun, Y., & Glickman, R. D. (2014) · Proteomes · doi:10.3390/proteomes2030399 · Cited by 5
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Malarz, K., Zioła, P., Zych, D., Rurka, P., & Mrozek‐Wilczkiewicz, A. (2024) · Scientific Reports · doi:10.1038/s41598-024-77575-4 · Cited by 3
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Yu, X., Liu, Y., Pan, K., Sun, P., Li, J., Li, L., Chen, Q., & Sun, Z. (2022) · Archives of Oral Biology · doi:10.1016/j.archoralbio.2022.105447 · Cited by 3
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Bhattacharya, B., Chattrerjee, S., Berland, R., Pichugin, A., Gao, Y., Connor, J. H., Ivanov, A., Yan, B.-S., Kobzik, L., & Kramnik, I. (2017) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/238873 · Cited by 3
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Sang, Y., Hou, S., Zhang, Z., Jiang, S., Yang, W., & Cheng, Q. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052401 · Cited by 2
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Kim, S. G., Lee, W. H., & Kim, Y. W. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_540
Mercurio, A. M. (2018) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.732521613.793545511
Maiuthed, A., Chanvorachote, P., Schneider-Stock, R., & Eichler, J. (2018) · doi:10.58837/chula.the.2018.436
Metadata
- Authors
- Chen, W., Sun, Z., Wang, X.-J., Jiang, T., Huang, Z., Fang, D., & Zhang, D. D.
- Affiliations
- University of Arizona (US)
- University of Missouri (US)
- Corresponding author
- Zhang, Donna D.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-06
- Volume
- 34
- Issue
- 6
- Pages
- 663-673
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC2714804
- OpenAlex
- W2080155284
- Cited by
- 638
- References
- 36
- Citations by year
- 2026: 24 · 2025: 15 · 2024: 50 · 2023: 31 · 2022: 43 · 2021: 51 · 2020: 48 · 2019: 52 · 2018: 48 · 2017: 35 · 2016: 44 · 2015: 29 · 2014: 40 · 2013: 38 · 2012: 34
- FWCI
- 11.93
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1543 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- American Cancer Society (ES006694, RSG-07-154)
- National Institute of Environmental Health Sciences (ES015010)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- Nrf2, p21, Keap1, oxidative stress, antioxidant response, protein stabilization, ubiquitination, protein-protein interaction
- MeSH terms
- Animals, Antioxidants, Binding Sites, Male, Up-Regulation, Oxidative Stress, Amino Acid Motifs, Cyclin-Dependent Kinase Inhibitor p21, NF-E2-Related Factor 2, Mice, Ubiquitination
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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