The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription factor that is activated by t-butyl hydroquinone but not by endoplasmic reticulum stressors

Yiguo Zhang, John M. Lucocq, John D. Hayes

    Research output: Contribution to journalArticle

    45 Citations (Scopus)

    Abstract

    In rat liver RL-34 cells, endogenous Nrf1 (nuclear factor-erythroid 2 p45 subunit-related factor 1) is localized in the ER (endoplasmic reticulum) where it exists as a glycosylated protein. Electron microscopy has demonstrated that. ectopic Nrf1 in COS-I cells is located in the ER and the NE (nuclear envelope). Subcellular fractionation, together with I membrane proteinase protection assay, revealed that Nrf1 is an integral membrane protein with both luminal anti cytoplasmic domains. The N-terminal 65 residues of Nrf1 direct its integration into the ER and NE membranes and tether it to a Triton X-100-resistant membrane microdomain that is associated with lipid rafts. The activity of Nrf1 was increased by the electrophile tBHQ (t-butyl hydroquinone) probably through an N-terminal domain-dependent process. We found that the NST (Asn/Ser/Thr-rich) domain, along with AD1 (acidic domain 1), contributes positively to the transactivation activity of full-length Nrf1. Furthermore, the NST domain contains seven putative-Asn-Xaa-Ser/Thr- glycosylation sites and, when glycosylation

    Original languageEnglish
    Pages (from-to)293-310
    Number of pages18
    JournalBiochemical Journal
    Volume418
    DOIs
    Publication statusPublished - 1 Mar 2009

    Keywords

    • detergent-resistant membrane
    • endoplasmic reticulum stress
    • glycosylation
    • nuclear factor-erythroid 2 p45 subunit-related factor 1 (Nrf1)
    • nuclear envelope
    • oxidative stress
    • transcriptional regulation
    • ANTIOXIDANT RESPONSE ELEMENT
    • LEUCINE-ZIPPER
    • TERT-BUTYLHYDROQUINONE
    • TRANSMEMBRANE DOMAIN
    • INDUCIBLE EXPRESSION
    • EMBRYONIC LETHALITY
    • MEMBRANE-PROTEINS
    • OXIDATIVE STRESS
    • CELL-SURVIVAL
    • FACTOR TCF11

    Cite this

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    title = "The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription factor that is activated by t-butyl hydroquinone but not by endoplasmic reticulum stressors",
    abstract = "In rat liver RL-34 cells, endogenous Nrf1 (nuclear factor-erythroid 2 p45 subunit-related factor 1) is localized in the ER (endoplasmic reticulum) where it exists as a glycosylated protein. Electron microscopy has demonstrated that. ectopic Nrf1 in COS-I cells is located in the ER and the NE (nuclear envelope). Subcellular fractionation, together with I membrane proteinase protection assay, revealed that Nrf1 is an integral membrane protein with both luminal anti cytoplasmic domains. The N-terminal 65 residues of Nrf1 direct its integration into the ER and NE membranes and tether it to a Triton X-100-resistant membrane microdomain that is associated with lipid rafts. The activity of Nrf1 was increased by the electrophile tBHQ (t-butyl hydroquinone) probably through an N-terminal domain-dependent process. We found that the NST (Asn/Ser/Thr-rich) domain, along with AD1 (acidic domain 1), contributes positively to the transactivation activity of full-length Nrf1. Furthermore, the NST domain contains seven putative-Asn-Xaa-Ser/Thr- glycosylation sites and, when glycosylation",
    keywords = "detergent-resistant membrane, endoplasmic reticulum stress, glycosylation, nuclear factor-erythroid 2 p45 subunit-related factor 1 (Nrf1), nuclear envelope, oxidative stress, transcriptional regulation, ANTIOXIDANT RESPONSE ELEMENT, LEUCINE-ZIPPER, TERT-BUTYLHYDROQUINONE, TRANSMEMBRANE DOMAIN, INDUCIBLE EXPRESSION, EMBRYONIC LETHALITY, MEMBRANE-PROTEINS, OXIDATIVE STRESS, CELL-SURVIVAL, FACTOR TCF11",
    author = "Yiguo Zhang and Lucocq, {John M.} and Hayes, {John D.}",
    note = "doi:10.1042/BJ20081575",
    year = "2009",
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    day = "1",
    doi = "10.1042/BJ20081575",
    language = "English",
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    pages = "293--310",
    journal = "Biochemical Journal",
    issn = "0264-6021",
    publisher = "Portland Press",

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    TY - JOUR

    T1 - The Nrf1 CNC/bZIP protein is a nuclear envelope-bound transcription factor that is activated by t-butyl hydroquinone but not by endoplasmic reticulum stressors

    AU - Zhang, Yiguo

    AU - Lucocq, John M.

    AU - Hayes, John D.

    N1 - doi:10.1042/BJ20081575

    PY - 2009/3/1

    Y1 - 2009/3/1

    N2 - In rat liver RL-34 cells, endogenous Nrf1 (nuclear factor-erythroid 2 p45 subunit-related factor 1) is localized in the ER (endoplasmic reticulum) where it exists as a glycosylated protein. Electron microscopy has demonstrated that. ectopic Nrf1 in COS-I cells is located in the ER and the NE (nuclear envelope). Subcellular fractionation, together with I membrane proteinase protection assay, revealed that Nrf1 is an integral membrane protein with both luminal anti cytoplasmic domains. The N-terminal 65 residues of Nrf1 direct its integration into the ER and NE membranes and tether it to a Triton X-100-resistant membrane microdomain that is associated with lipid rafts. The activity of Nrf1 was increased by the electrophile tBHQ (t-butyl hydroquinone) probably through an N-terminal domain-dependent process. We found that the NST (Asn/Ser/Thr-rich) domain, along with AD1 (acidic domain 1), contributes positively to the transactivation activity of full-length Nrf1. Furthermore, the NST domain contains seven putative-Asn-Xaa-Ser/Thr- glycosylation sites and, when glycosylation

    AB - In rat liver RL-34 cells, endogenous Nrf1 (nuclear factor-erythroid 2 p45 subunit-related factor 1) is localized in the ER (endoplasmic reticulum) where it exists as a glycosylated protein. Electron microscopy has demonstrated that. ectopic Nrf1 in COS-I cells is located in the ER and the NE (nuclear envelope). Subcellular fractionation, together with I membrane proteinase protection assay, revealed that Nrf1 is an integral membrane protein with both luminal anti cytoplasmic domains. The N-terminal 65 residues of Nrf1 direct its integration into the ER and NE membranes and tether it to a Triton X-100-resistant membrane microdomain that is associated with lipid rafts. The activity of Nrf1 was increased by the electrophile tBHQ (t-butyl hydroquinone) probably through an N-terminal domain-dependent process. We found that the NST (Asn/Ser/Thr-rich) domain, along with AD1 (acidic domain 1), contributes positively to the transactivation activity of full-length Nrf1. Furthermore, the NST domain contains seven putative-Asn-Xaa-Ser/Thr- glycosylation sites and, when glycosylation

    KW - detergent-resistant membrane

    KW - endoplasmic reticulum stress

    KW - glycosylation

    KW - nuclear factor-erythroid 2 p45 subunit-related factor 1 (Nrf1)

    KW - nuclear envelope

    KW - oxidative stress

    KW - transcriptional regulation

    KW - ANTIOXIDANT RESPONSE ELEMENT

    KW - LEUCINE-ZIPPER

    KW - TERT-BUTYLHYDROQUINONE

    KW - TRANSMEMBRANE DOMAIN

    KW - INDUCIBLE EXPRESSION

    KW - EMBRYONIC LETHALITY

    KW - MEMBRANE-PROTEINS

    KW - OXIDATIVE STRESS

    KW - CELL-SURVIVAL

    KW - FACTOR TCF11

    U2 - 10.1042/BJ20081575

    DO - 10.1042/BJ20081575

    M3 - Article

    VL - 418

    SP - 293

    EP - 310

    JO - Biochemical Journal

    JF - Biochemical Journal

    SN - 0264-6021

    ER -