ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals
ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecular chaperones. Upon ER stress, ATF6 translocates from the ER to the Golgi where it is processed to its active form. We have found that the ER chaperone BiP/GRP78 bi...
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| Veröffentlicht in: | Developmental cell 2002-07, Vol.3 (1), p.99-111 |
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| creator | Shen, Jingshi Chen, Xi Hendershot, Linda Prywes, Ron |
| description | ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecular chaperones. Upon ER stress, ATF6 translocates from the ER to the Golgi where it is processed to its active form. We have found that the ER chaperone BiP/GRP78 binds ATF6 and dissociates in response to ER stress. Loss of BiP binding correlates with the translocation of ATF6 to the Golgi, which was slowed in cells overexpressing BiP. Two Golgi localization signals (GLSs) were identified in ATF6. Removal of BiP binding sites from ATF6, while retaining a GLS, resulted in its constitutive translocation to the Golgi. These results suggest that BiP retains ATF6 in the ER by inhibiting its GLSs and that dissociation of BiP during ER stress allows ATF6 to be transported to the Golgi. |
| doi_str_mv | 10.1016/S1534-5807(02)00203-4 |
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Upon ER stress, ATF6 translocates from the ER to the Golgi where it is processed to its active form. We have found that the ER chaperone BiP/GRP78 binds ATF6 and dissociates in response to ER stress. Loss of BiP binding correlates with the translocation of ATF6 to the Golgi, which was slowed in cells overexpressing BiP. Two Golgi localization signals (GLSs) were identified in ATF6. Removal of BiP binding sites from ATF6, while retaining a GLS, resulted in its constitutive translocation to the Golgi. These results suggest that BiP retains ATF6 in the ER by inhibiting its GLSs and that dissociation of BiP during ER stress allows ATF6 to be transported to the Golgi.</description><identifier>ISSN: 1534-5807</identifier><identifier>EISSN: 1878-1551</identifier><identifier>DOI: 10.1016/S1534-5807(02)00203-4</identifier><identifier>PMID: 12110171</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>3T3 Cells ; Activating Transcription Factor 6 ; Animals ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; Cell Compartmentation - genetics ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Endoplasmic Reticulum - metabolism ; Endoplasmic Reticulum - ultrastructure ; Eukaryotic Cells - cytology ; Eukaryotic Cells - metabolism ; Gene Expression Regulation - physiology ; Golgi Apparatus - metabolism ; Golgi Apparatus - ultrastructure ; Heat-Shock Proteins ; HeLa Cells ; Humans ; Mice ; Molecular Chaperones - genetics ; Molecular Chaperones - metabolism ; Mutation - genetics ; Protein Binding - genetics ; Protein Folding ; Protein Structure, Tertiary - genetics ; Protein Transport - genetics ; Signal Transduction - genetics ; Stress, Physiological - genetics ; Stress, Physiological - metabolism ; Transcription Factors - genetics ; Transcription Factors - metabolism</subject><ispartof>Developmental cell, 2002-07, Vol.3 (1), p.99-111</ispartof><rights>2002 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c557t-4c9b53bc0b0e5aa0499ec29608262dcf004ddfea61470b92d2f59b427413d4a63</citedby><cites>FETCH-LOGICAL-c557t-4c9b53bc0b0e5aa0499ec29608262dcf004ddfea61470b92d2f59b427413d4a63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S1534-5807(02)00203-4$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>315,781,785,3551,27929,27930,46000</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12110171$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shen, Jingshi</creatorcontrib><creatorcontrib>Chen, Xi</creatorcontrib><creatorcontrib>Hendershot, Linda</creatorcontrib><creatorcontrib>Prywes, Ron</creatorcontrib><title>ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals</title><title>Developmental cell</title><addtitle>Dev Cell</addtitle><description>ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecular chaperones. Upon ER stress, ATF6 translocates from the ER to the Golgi where it is processed to its active form. We have found that the ER chaperone BiP/GRP78 binds ATF6 and dissociates in response to ER stress. Loss of BiP binding correlates with the translocation of ATF6 to the Golgi, which was slowed in cells overexpressing BiP. Two Golgi localization signals (GLSs) were identified in ATF6. Removal of BiP binding sites from ATF6, while retaining a GLS, resulted in its constitutive translocation to the Golgi. These results suggest that BiP retains ATF6 in the ER by inhibiting its GLSs and that dissociation of BiP during ER stress allows ATF6 to be transported to the Golgi.</description><subject>3T3 Cells</subject><subject>Activating Transcription Factor 6</subject><subject>Animals</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Cell Compartmentation - genetics</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Endoplasmic Reticulum - metabolism</subject><subject>Endoplasmic Reticulum - ultrastructure</subject><subject>Eukaryotic Cells - cytology</subject><subject>Eukaryotic Cells - metabolism</subject><subject>Gene Expression Regulation - physiology</subject><subject>Golgi Apparatus - metabolism</subject><subject>Golgi Apparatus - ultrastructure</subject><subject>Heat-Shock Proteins</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Mice</subject><subject>Molecular Chaperones - genetics</subject><subject>Molecular Chaperones - metabolism</subject><subject>Mutation - genetics</subject><subject>Protein Binding - genetics</subject><subject>Protein Folding</subject><subject>Protein Structure, Tertiary - genetics</subject><subject>Protein Transport - genetics</subject><subject>Signal Transduction - genetics</subject><subject>Stress, Physiological - genetics</subject><subject>Stress, Physiological - metabolism</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - metabolism</subject><issn>1534-5807</issn><issn>1878-1551</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkctOwzAQRS0E4lH4BFBWCBahY8dOnBUqpS1IlUAtrC3HdipDGkOcIsHX4z4AsepqHjr3jjQXoVMMVxhw2p1iltCYccgugFwCEEhiuoMOMc94jBnDu6H_QQ7QkfcvEHSYwz46wAQHkwwfoq_BJJq2jfE-mpjZopKtdXXkyqj3NEyjsVOysl_rZfEZ3VrvnbK_0I197I4mjxkPXa1tPYtkraPnei7963IKyMhVM_vfaGpntaz8MdorQzEnm9pBz8PBU_8uHj-M7vu9cawYy9qYqrxgSaGgAMOkBJrnRpE8BU5SolUJQLUujUwxzaDIiSYlywtKMooTTWWadND52vetce8L41sxt16ZqpK1cQsvMpxDCjnfCmJOGSWcBJCtQdU47xtTirfGzmXzKTCIZTpilY5Yvl4AEat0BA26s82BRTE3-k-1iSMA12vAhH98WNMIr6ypldG2MaoV2tktJ74B9I2dxg</recordid><startdate>20020701</startdate><enddate>20020701</enddate><creator>Shen, Jingshi</creator><creator>Chen, Xi</creator><creator>Hendershot, Linda</creator><creator>Prywes, Ron</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>7X8</scope></search><sort><creationdate>20020701</creationdate><title>ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals</title><author>Shen, Jingshi ; Chen, Xi ; Hendershot, Linda ; Prywes, Ron</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c557t-4c9b53bc0b0e5aa0499ec29608262dcf004ddfea61470b92d2f59b427413d4a63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>3T3 Cells</topic><topic>Activating Transcription Factor 6</topic><topic>Animals</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Cell Compartmentation - genetics</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Endoplasmic Reticulum - metabolism</topic><topic>Endoplasmic Reticulum - ultrastructure</topic><topic>Eukaryotic Cells - cytology</topic><topic>Eukaryotic Cells - metabolism</topic><topic>Gene Expression Regulation - physiology</topic><topic>Golgi Apparatus - metabolism</topic><topic>Golgi Apparatus - ultrastructure</topic><topic>Heat-Shock Proteins</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Mice</topic><topic>Molecular Chaperones - genetics</topic><topic>Molecular Chaperones - metabolism</topic><topic>Mutation - genetics</topic><topic>Protein Binding - genetics</topic><topic>Protein Folding</topic><topic>Protein Structure, Tertiary - genetics</topic><topic>Protein Transport - genetics</topic><topic>Signal Transduction - genetics</topic><topic>Stress, Physiological - genetics</topic><topic>Stress, Physiological - metabolism</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shen, Jingshi</creatorcontrib><creatorcontrib>Chen, Xi</creatorcontrib><creatorcontrib>Hendershot, Linda</creatorcontrib><creatorcontrib>Prywes, Ron</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Developmental cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shen, Jingshi</au><au>Chen, Xi</au><au>Hendershot, Linda</au><au>Prywes, Ron</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals</atitle><jtitle>Developmental cell</jtitle><addtitle>Dev Cell</addtitle><date>2002-07-01</date><risdate>2002</risdate><volume>3</volume><issue>1</issue><spage>99</spage><epage>111</epage><pages>99-111</pages><issn>1534-5807</issn><eissn>1878-1551</eissn><abstract>ATF6 is an endoplasmic reticulum (ER) stress-regulated transmembrane transcription factor that activates the transcription of ER molecular chaperones. Upon ER stress, ATF6 translocates from the ER to the Golgi where it is processed to its active form. We have found that the ER chaperone BiP/GRP78 binds ATF6 and dissociates in response to ER stress. Loss of BiP binding correlates with the translocation of ATF6 to the Golgi, which was slowed in cells overexpressing BiP. Two Golgi localization signals (GLSs) were identified in ATF6. Removal of BiP binding sites from ATF6, while retaining a GLS, resulted in its constitutive translocation to the Golgi. These results suggest that BiP retains ATF6 in the ER by inhibiting its GLSs and that dissociation of BiP during ER stress allows ATF6 to be transported to the Golgi.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12110171</pmid><doi>10.1016/S1534-5807(02)00203-4</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Open Access: Cell Press Free Archives; EZB Electronic Journals Library |
| subjects | 3T3 Cells Activating Transcription Factor 6 Animals Carrier Proteins - genetics Carrier Proteins - metabolism Cell Compartmentation - genetics DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Endoplasmic Reticulum - metabolism Endoplasmic Reticulum - ultrastructure Eukaryotic Cells - cytology Eukaryotic Cells - metabolism Gene Expression Regulation - physiology Golgi Apparatus - metabolism Golgi Apparatus - ultrastructure Heat-Shock Proteins HeLa Cells Humans Mice Molecular Chaperones - genetics Molecular Chaperones - metabolism Mutation - genetics Protein Binding - genetics Protein Folding Protein Structure, Tertiary - genetics Protein Transport - genetics Signal Transduction - genetics Stress, Physiological - genetics Stress, Physiological - metabolism Transcription Factors - genetics Transcription Factors - metabolism |
| title | ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals |
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