Keap1 Is a Redox-Regulated Substrate Adaptor Protein for a Cul3-Dependent Ubiquitin Ligase Complex

By Donna D. Zhang, Shih-Ching Lo, J. Cross, D. Templeton, Mark Hannink. Molecular and Cellular Biology, 2004

1,258 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/c58a00f0530a404a49b50b83df633106c7fcf2ee

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Citations in the corpus

ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis (2007, background): “…the pathway and the nRF2-cognate adaptor of a cullin-3 (Cul3)–ring-box-1 (RBX1) ubiquitin-ligase complex that marks nRF2 for proteosomal degradation 91–94 Chemical inducers, by modifying KeaP1, decrease ubiquitylation and proteosomal degradation of nRF2 and promote its nuclear accumulation 95,96 .”
Alpha-lipoic acid as a dietary supplement: Molecular mechanisms and therapeutic potential (2009, background): “LA, acting as a pro-oxidant, may increase Nrf2-dependent transcriptional activity by forming lipoyl-cysteinyl mixed disulfides on Keap1 [81], the protein that sequesters Nrf2 and bridges it to ubiquitin ligases [82].”
Nrf2 and Oxidative Stress: A General Overview of Mechanisms and Implications in Human Disease (2022, background): “Keap1 [49] belongs to the BTB-Kelch family of proteins which includes about 50 members, all of which assemble with the Cul3 E3 ubiquitin ligase and RING box protein-1 (Rbx1) to form the Cullin-RING E3 ubiquitin ligases (CRLs) involved in the ubiquitination of BTB-Kelch proteins, such as Keap1 [51,66”
Activation of Nrf2-antioxidant signaling attenuates NF-κB-inflammatory response and elicits apoptosis (2008, background): “[5] Zhang DD, Lo SC, Cross JV, Templeton DJ, Hannink M.”
Transcriptional Regulation by Nrf2 (2017, background): “Under unstressed conditions, Nrf2 is constantly targeted for proteasomal degradation by the Keap1/Cul3 E3 ubiquitin ligase complex (37, 60, 80, 192).”
Mechanistic Studies of the Nrf2-Keap1 Signaling Pathway (2006, background): “…clear evidence that Keap1 does not just passively sequester Nrf2 in the cytoplasm to block Nrf2 nuclear translocation, as originally proposed, but actively targets Nrf2 for ubiquitination and proteasomal degradation by functioning as a component of an E3 ubiquitin ligase (Zhang et al., 2004).”
Direct interaction between Nrf2 and p21(Cip1/WAF1) upregulates the Nrf2-mediated antioxidant response. (2009, background): “It is believed that the Keap1 homodimer binds both the (29)DLG and (79)ETGE motifs in Nrf2 to align the seven ubiquitin-accepting lysine residues between these motifs into a conformation suitable for ubiquitin conjugation (McMahon et al., 2006; Tong et al., 2006, 2007; Zhang et al., 2004).”