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We began analyzing https://www.tandfonline.com/doi/full/10.1128/MCB.24.16.7130-7139.2004, but it redirected us to https://www.tandfonline.com/doi/full/10.1128/MCB.24.16.7130-7139.2004. The analysis below is for the second page.

Title[redir]:
Oxidative Stress Sensor Keap1 Functions as an Adaptor for Cul3-Based E3 Ligase To Regulate Proteasomal Degradation of Nrf2: Molecular and Cellular Biology: Vol 24 , No 16 - Get Access
Description:
Biological responses to toxic environmental stresses are regulated by several coordinated functions of cellular factors, providing animals with a means of cellular protection. The cellular factors ...

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Keywords {🔍}

access, keap, journals, article, nrf, taylor, francis, online, open, group, page, search, issue, pdf, browse, studies, sciences, science, journal, cart, stress, ligase, degradation, content, environment, technology, health, information, add, oxidative, functions, adaptor, culbased, found, log, purchase, close, menu, select, books, bioscience, education, social, sports, publish, find, register, molecular, cellular, biology,

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cul3-based e3 ligase recruit ubiquitin-proteasome factors downloaded article pdf twitter page taylor francis group downloaded article pdfs antioxidant stress proteins e3 ligase complex oxidative stress journal search calls institution access receive personalised research published online journals browse journals books cart home moon-il kang cul3-roc1 complex provide solid evidence reported mammalian substrate tania o'connor science domain function analyses n-terminal region regulate proteasomal degradation keap1 functions 839 crossref citations date register nrf2 akira kobayashi journals a article https proteasome system technology sports search publish intervening-region keap1 associates makoto kobayashi education institution log health information rapid degradation taylor nrf2 degradation leisure tourism hiromi okawa makiko ohtsuji yukari zenke

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            name:Oxidative Stress Sensor Keap1 Functions ....
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      articleSection:Transcriptional Regulation
      name:Oxidative Stress Sensor Keap1 Functions as an Adaptor for Cul3-Based E3 Ligase To Regulate Proteasomal Degradation of Nrf2
      headline:Oxidative Stress Sensor Keap1 Functions as an Adaptor for Cul3-Based E3 Ligase To Regulate Proteasomal Degradation of Nrf2
      abstract:Transcription factor Nrf2 is a major regulator of genes encoding phase 2 detoxifying enzymes and antioxidant stress proteins in response to electrophilic agents and oxidative stress. In the absence of such stimuli, Nrf2 is inactive owing to its cytoplasmic retention by Keap1 and rapid degradation through the proteasome system. We examined the contribution of Keap1 to the rapid turnover of Nrf2 (half-life of less than 20 min) and found that a direct association between Keap1 and Nrf2 is required for Nrf2 degradation. In a series of domain function analyses of Keap1, we found that both the BTB and intervening-region (IVR) domains are crucial for Nrf2 degradation, implying that these two domains act to recruit ubiquitin-proteasome factors. Indeed, Cullin 3 (Cul3), a subunit of the E3 ligase complex, was found to interact specifically with Keap1 in vivo. Keap1 associates with the N-terminal region of Cul3 through the IVR domain and promotes the ubiquitination of Nrf2 in cooperation with the Cul3-Roc1 complex. These results thus provide solid evidence that Keap1 functions as an adaptor of Cul3-based E3 ligase. To our knowledge, Nrf2 and Keap1 are the first reported mammalian substrate and adaptor, respectively, of the Cul3-based E3 ligase system.
      description:Transcription factor Nrf2 is a major regulator of genes encoding phase 2 detoxifying enzymes and antioxidant stress proteins in response to electrophilic agents and oxidative stress. In the absence of such stimuli, Nrf2 is inactive owing to its cytoplasmic retention by Keap1 and rapid degradation through the proteasome system. We examined the contribution of Keap1 to the rapid turnover of Nrf2 (half-life of less than 20 min) and found that a direct association between Keap1 and Nrf2 is required for Nrf2 degradation. In a series of domain function analyses of Keap1, we found that both the BTB and intervening-region (IVR) domains are crucial for Nrf2 degradation, implying that these two domains act to recruit ubiquitin-proteasome factors. Indeed, Cullin 3 (Cul3), a subunit of the E3 ligase complex, was found to interact specifically with Keap1 in vivo. Keap1 associates with the N-terminal region of Cul3 through the IVR domain and promotes the ubiquitination of Nrf2 in cooperation with the Cul3-Roc1 complex. These results thus provide solid evidence that Keap1 functions as an adaptor of Cul3-based E3 ligase. To our knowledge, Nrf2 and Keap1 are the first reported mammalian substrate and adaptor, respectively, of the Cul3-based E3 ligase system.
      author:
            type:Person
            name:Akira Kobayashi
            type:Person
            name:Moon-Il Kang
            type:Person
            name:Hiromi Okawa
            type:Person
            name:Makiko Ohtsuji
            type:Person
            name:Yukari Zenke
            type:Person
            name:Tomoki Chiba
            type:Person
            name:Kazuhiko Igarashi
            type:Person
            name:Masayuki Yamamoto
      pageStart:7130
      pageEnd:7139
      datePublished:2023-03-27
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      name:Moon-Il Kang
      name:Hiromi Okawa
      name:Makiko Ohtsuji
      name:Yukari Zenke
      name:Tomoki Chiba
      name:Kazuhiko Igarashi
      name:Masayuki Yamamoto
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