Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism
Cells are equipped with a number of transcriptional factors that safeguard against various environmental insults. Proteasomal protein degradation plays an important role in the Keap1-Nrf2 cytoprotection system, with molecular machinery similar to that for other environmental defense systems such as...
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| Veröffentlicht in: | Biological chemistry 2006-10, Vol.387 (10/11), p.1311-1320 |
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| container_issue | 10/11 |
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| container_title | Biological chemistry |
| container_volume | 387 |
| creator | Tong, Kit I. Kobayashi, Akira Katsuoka, Fumiki Yamamoto, Masayuki |
| description | Cells are equipped with a number of transcriptional factors that safeguard against various environmental insults. Proteasomal protein degradation plays an important role in the Keap1-Nrf2 cytoprotection system, with molecular machinery similar to that for other environmental defense systems such as inflammatory and hypoxic responses. While Nrf2 protein stabilization is known to be redox-sensitive, the transcription factors NF-κB and HIF-1α for inflammatory and hypoxic responses, respectively, are also influenced by the cellular redox conditions. In this review we present the recently proposed two-site substrate recognition model of the Keap1-Nrf2 system, which regulates the cellular responses against oxidative and xenobiotic stresses. The implications of two destructive motifs in Nrf2, the ETGE and DLG motifs, which appear to function as a hinge and latch attenuating Keap1 activity in different redox states, are discussed. |
| doi_str_mv | 10.1515/BC.2006.164 |
| format | Article |
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Proteasomal protein degradation plays an important role in the Keap1-Nrf2 cytoprotection system, with molecular machinery similar to that for other environmental defense systems such as inflammatory and hypoxic responses. While Nrf2 protein stabilization is known to be redox-sensitive, the transcription factors NF-κB and HIF-1α for inflammatory and hypoxic responses, respectively, are also influenced by the cellular redox conditions. In this review we present the recently proposed two-site substrate recognition model of the Keap1-Nrf2 system, which regulates the cellular responses against oxidative and xenobiotic stresses. The implications of two destructive motifs in Nrf2, the ETGE and DLG motifs, which appear to function as a hinge and latch attenuating Keap1 activity in different redox states, are discussed.</description><identifier>ISSN: 1431-6730</identifier><identifier>EISSN: 1437-4315</identifier><identifier>DOI: 10.1515/BC.2006.164</identifier><identifier>PMID: 17081101</identifier><language>eng</language><publisher>Germany: Walter de Gruyter</publisher><subject>Animals ; CUL3-BTB E3 ligase ; DLG motif ; ETGE motif ; Humans ; Intracellular Signaling Peptides and Proteins - metabolism ; Keap1 ; Models, Biological ; NF-E2-Related Factor 2 - metabolism ; Nrf2 ; oxidative stress sensor ; Proteasome Endopeptidase Complex - metabolism ; Protein Binding ; Substrate Specificity</subject><ispartof>Biological chemistry, 2006-10, Vol.387 (10/11), p.1311-1320</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c391t-4efcd0d383300c951c9593569fc3bfabcd85ec0f46dd70f3f50e8c7ebbc450df3</citedby><cites>FETCH-LOGICAL-c391t-4efcd0d383300c951c9593569fc3bfabcd85ec0f46dd70f3f50e8c7ebbc450df3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17081101$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tong, Kit I.</creatorcontrib><creatorcontrib>Kobayashi, Akira</creatorcontrib><creatorcontrib>Katsuoka, Fumiki</creatorcontrib><creatorcontrib>Yamamoto, Masayuki</creatorcontrib><title>Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism</title><title>Biological chemistry</title><addtitle>Biological Chemistry</addtitle><description>Cells are equipped with a number of transcriptional factors that safeguard against various environmental insults. Proteasomal protein degradation plays an important role in the Keap1-Nrf2 cytoprotection system, with molecular machinery similar to that for other environmental defense systems such as inflammatory and hypoxic responses. While Nrf2 protein stabilization is known to be redox-sensitive, the transcription factors NF-κB and HIF-1α for inflammatory and hypoxic responses, respectively, are also influenced by the cellular redox conditions. In this review we present the recently proposed two-site substrate recognition model of the Keap1-Nrf2 system, which regulates the cellular responses against oxidative and xenobiotic stresses. The implications of two destructive motifs in Nrf2, the ETGE and DLG motifs, which appear to function as a hinge and latch attenuating Keap1 activity in different redox states, are discussed.</description><subject>Animals</subject><subject>CUL3-BTB E3 ligase</subject><subject>DLG motif</subject><subject>ETGE motif</subject><subject>Humans</subject><subject>Intracellular Signaling Peptides and Proteins - metabolism</subject><subject>Keap1</subject><subject>Models, Biological</subject><subject>NF-E2-Related Factor 2 - metabolism</subject><subject>Nrf2</subject><subject>oxidative stress sensor</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Protein Binding</subject><subject>Substrate Specificity</subject><issn>1431-6730</issn><issn>1437-4315</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1LAzEQhoMofp-8S05eZOuM2exuvWnxC4uiVBA8hGwysav7UZMt6r832qKHYV6YhxfmYWwPYYAS5dHZaHAMkA0wS1fYJqYiT1KBcvU3Y5LlAjbYVgivAFBAKtbZBuZQIAJusufJR5eEqice5mXovY7Jk-le2qqvupY3naWau87zfkr8hvQMk1vvjnn4Cj01J1zzadW-ENet5bXuzZQ3ZKa6rUKzw9acrgPtLvc2e7w4n4yukvHd5fXodJwYMcQ-SckZC1YUQgCYocQ4QyGzoTOidLo0tpBkwKWZtTk44SRQYXIqS5NKsE5ss4NF78x373MKvWqqYKiudUvdPKiswPg25BE8XIDGdyF4cmrmq0b7L4Wgflyqs5H6camiy0jvL2vnZUP2n13Ki0CyAKqo4vPvrv2bitJzqe4nqXqCMWbwcKPG4htUHX3_</recordid><startdate>20061001</startdate><enddate>20061001</enddate><creator>Tong, Kit I.</creator><creator>Kobayashi, Akira</creator><creator>Katsuoka, Fumiki</creator><creator>Yamamoto, Masayuki</creator><general>Walter de Gruyter</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20061001</creationdate><title>Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism</title><author>Tong, Kit I. ; Kobayashi, Akira ; Katsuoka, Fumiki ; Yamamoto, Masayuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c391t-4efcd0d383300c951c9593569fc3bfabcd85ec0f46dd70f3f50e8c7ebbc450df3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>CUL3-BTB E3 ligase</topic><topic>DLG motif</topic><topic>ETGE motif</topic><topic>Humans</topic><topic>Intracellular Signaling Peptides and Proteins - metabolism</topic><topic>Keap1</topic><topic>Models, Biological</topic><topic>NF-E2-Related Factor 2 - metabolism</topic><topic>Nrf2</topic><topic>oxidative stress sensor</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Protein Binding</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tong, Kit I.</creatorcontrib><creatorcontrib>Kobayashi, Akira</creatorcontrib><creatorcontrib>Katsuoka, Fumiki</creatorcontrib><creatorcontrib>Yamamoto, Masayuki</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tong, Kit I.</au><au>Kobayashi, Akira</au><au>Katsuoka, Fumiki</au><au>Yamamoto, Masayuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism</atitle><jtitle>Biological chemistry</jtitle><addtitle>Biological Chemistry</addtitle><date>2006-10-01</date><risdate>2006</risdate><volume>387</volume><issue>10/11</issue><spage>1311</spage><epage>1320</epage><pages>1311-1320</pages><issn>1431-6730</issn><eissn>1437-4315</eissn><abstract>Cells are equipped with a number of transcriptional factors that safeguard against various environmental insults. 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| fulltext | fulltext |
| identifier | ISSN: 1431-6730 |
| ispartof | Biological chemistry, 2006-10, Vol.387 (10/11), p.1311-1320 |
| issn | 1431-6730 1437-4315 |
| language | eng |
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| source | MEDLINE; De Gruyter数学期刊（与数学科学学院共建） |
| subjects | Animals CUL3-BTB E3 ligase DLG motif ETGE motif Humans Intracellular Signaling Peptides and Proteins - metabolism Keap1 Models, Biological NF-E2-Related Factor 2 - metabolism Nrf2 oxidative stress sensor Proteasome Endopeptidase Complex - metabolism Protein Binding Substrate Specificity |
| title | Two-site substrate recognition model for the Keap1-Nrf2 system: a hinge and latch mechanism |
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