Distinct Regulation of Internal Ribosome Entry Site-mediated Translation following Cellular Stress Is Mediated by Apoptotic Fragments of eIF4G Translation Initiation Factor Family Members eIF4GI and p97/DAP5/NAT1
Many cellular stresses lead to the inhibition of protein synthesis. Despite this, some cellular mRNAs are selectively translated under these conditions. It was suggested that the presence of internal ribosome entry site (IRES) sequences in the 5′-untranslated regions allow these mRNAs to be actively...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2003-02, Vol.278 (6), p.3572-3579 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3579 |
|---|---|
| container_issue | 6 |
| container_start_page | 3572 |
| container_title | The Journal of biological chemistry |
| container_volume | 278 |
| creator | Nevins, Tara A. Harder, Zdena M. Korneluk, Robert G. Holčı́k, Martin |
| description | Many cellular stresses lead to the inhibition of protein synthesis. Despite this, some cellular mRNAs are selectively translated under these conditions. It was suggested that the presence of internal ribosome entry site (IRES) sequences in the 5′-untranslated regions allow these mRNAs to be actively translated despite the overall cessation of protein synthesis. Here we tested the hypothesis that the IRES elements of genes that are involved in the control of cell survival are distinctly regulated by cellular stresses. We show that the transient conditions of cellular stress favor the translation of pro-survival IRES, while the severe apoptotic conditions support translation of pro-death IRES elements. Furthermore, activation of pro-death IRES during the etoposide-induced apoptosis is caspase-dependent and correlates with the expression of apoptotic fragments of two members of the eIF4G translation initiation factor family, p97/DAP5/NAT1 and eIF4GI. Our results suggest that the regulation of IRES translation during stress contributes to the fine-tuning of cell fate. |
| doi_str_mv | 10.1074/jbc.M206781200 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_18652110</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925819307604</els_id><sourcerecordid>18652110</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3980-c26089b9d272e2b46167fb25743e44f2ecad650fb6e00d45b8bf1361e5aff6473</originalsourceid><addsrcrecordid>eNp1kU9v0zAYxiMEYmVw5YgsDtzS2k7sJMeqW0ekDdBWJG6W7bxpPSV2sV2mfs99oHlK0cQBX14ffs_z_nmy7CPBc4KrcnGv9PyGYl7VhGL8KpsRXBd5wciv19kMY0ryhrL6LHsXwj1Or2zI2-yM0JLVlLBZ9nhhQjRWR3QL28Mgo3EWuR61NoK3ckC3RrngRkCXNvojujMR8hE6IyN0aOOlDSdR74bBPRi7RSsYhmTl0V30EAJqA7r5q1BHtNy7fXTRaLT2cjuCjeG5I7Tr8uofx9aaaKbvWurofCqjGY7JbVTgwyRpkbQd2jfV4mL5gy2-LTfkffaml0OAD6d6nv1cX25WX_Pr71ftanmd66Kpca4px3Wjmo5WFKgqOeFVryirygLKsqegZccZ7hUHjLuSqVr1pOAEmOx7XlbFefZl8t179_sAIYrRBJ22lxbcIQhSc0YJwQmcT6D2LgQPvdh7M0p_FASL5xxFylG85JgEn07OB5Wu_YKfgkvA5wnYme3uwXgQyji9g1HQqhZcFKyiCaonCNIR_hjwImgDVqcwPOgoOmf-N8ATI-65JA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18652110</pqid></control><display><type>article</type><title>Distinct Regulation of Internal Ribosome Entry Site-mediated Translation following Cellular Stress Is Mediated by Apoptotic Fragments of eIF4G Translation Initiation Factor Family Members eIF4GI and p97/DAP5/NAT1</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Alma/SFX Local Collection</source><creator>Nevins, Tara A. ; Harder, Zdena M. ; Korneluk, Robert G. ; Holčı́k, Martin</creator><creatorcontrib>Nevins, Tara A. ; Harder, Zdena M. ; Korneluk, Robert G. ; Holčı́k, Martin</creatorcontrib><description>Many cellular stresses lead to the inhibition of protein synthesis. Despite this, some cellular mRNAs are selectively translated under these conditions. It was suggested that the presence of internal ribosome entry site (IRES) sequences in the 5′-untranslated regions allow these mRNAs to be actively translated despite the overall cessation of protein synthesis. Here we tested the hypothesis that the IRES elements of genes that are involved in the control of cell survival are distinctly regulated by cellular stresses. We show that the transient conditions of cellular stress favor the translation of pro-survival IRES, while the severe apoptotic conditions support translation of pro-death IRES elements. Furthermore, activation of pro-death IRES during the etoposide-induced apoptosis is caspase-dependent and correlates with the expression of apoptotic fragments of two members of the eIF4G translation initiation factor family, p97/DAP5/NAT1 and eIF4GI. Our results suggest that the regulation of IRES translation during stress contributes to the fine-tuning of cell fate.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M206781200</identifier><identifier>PMID: 12458215</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Apoptosis ; Cell Line ; Etoposide - pharmacology ; Eukaryotic Initiation Factor-4G ; Humans ; Oxidative Stress ; Peptide Fragments - physiology ; Peptide Initiation Factors - physiology ; Protein Biosynthesis - drug effects ; Protein Biosynthesis - physiology ; Ribosomes - metabolism ; RNA, Messenger - genetics</subject><ispartof>The Journal of biological chemistry, 2003-02, Vol.278 (6), p.3572-3579</ispartof><rights>2003 © 2003 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3980-c26089b9d272e2b46167fb25743e44f2ecad650fb6e00d45b8bf1361e5aff6473</citedby><cites>FETCH-LOGICAL-c3980-c26089b9d272e2b46167fb25743e44f2ecad650fb6e00d45b8bf1361e5aff6473</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12458215$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nevins, Tara A.</creatorcontrib><creatorcontrib>Harder, Zdena M.</creatorcontrib><creatorcontrib>Korneluk, Robert G.</creatorcontrib><creatorcontrib>Holčı́k, Martin</creatorcontrib><title>Distinct Regulation of Internal Ribosome Entry Site-mediated Translation following Cellular Stress Is Mediated by Apoptotic Fragments of eIF4G Translation Initiation Factor Family Members eIF4GI and p97/DAP5/NAT1</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Many cellular stresses lead to the inhibition of protein synthesis. Despite this, some cellular mRNAs are selectively translated under these conditions. It was suggested that the presence of internal ribosome entry site (IRES) sequences in the 5′-untranslated regions allow these mRNAs to be actively translated despite the overall cessation of protein synthesis. Here we tested the hypothesis that the IRES elements of genes that are involved in the control of cell survival are distinctly regulated by cellular stresses. We show that the transient conditions of cellular stress favor the translation of pro-survival IRES, while the severe apoptotic conditions support translation of pro-death IRES elements. Furthermore, activation of pro-death IRES during the etoposide-induced apoptosis is caspase-dependent and correlates with the expression of apoptotic fragments of two members of the eIF4G translation initiation factor family, p97/DAP5/NAT1 and eIF4GI. Our results suggest that the regulation of IRES translation during stress contributes to the fine-tuning of cell fate.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Cell Line</subject><subject>Etoposide - pharmacology</subject><subject>Eukaryotic Initiation Factor-4G</subject><subject>Humans</subject><subject>Oxidative Stress</subject><subject>Peptide Fragments - physiology</subject><subject>Peptide Initiation Factors - physiology</subject><subject>Protein Biosynthesis - drug effects</subject><subject>Protein Biosynthesis - physiology</subject><subject>Ribosomes - metabolism</subject><subject>RNA, Messenger - genetics</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU9v0zAYxiMEYmVw5YgsDtzS2k7sJMeqW0ekDdBWJG6W7bxpPSV2sV2mfs99oHlK0cQBX14ffs_z_nmy7CPBc4KrcnGv9PyGYl7VhGL8KpsRXBd5wciv19kMY0ryhrL6LHsXwj1Or2zI2-yM0JLVlLBZ9nhhQjRWR3QL28Mgo3EWuR61NoK3ckC3RrngRkCXNvojujMR8hE6IyN0aOOlDSdR74bBPRi7RSsYhmTl0V30EAJqA7r5q1BHtNy7fXTRaLT2cjuCjeG5I7Tr8uofx9aaaKbvWurofCqjGY7JbVTgwyRpkbQd2jfV4mL5gy2-LTfkffaml0OAD6d6nv1cX25WX_Pr71ftanmd66Kpca4px3Wjmo5WFKgqOeFVryirygLKsqegZccZ7hUHjLuSqVr1pOAEmOx7XlbFefZl8t179_sAIYrRBJ22lxbcIQhSc0YJwQmcT6D2LgQPvdh7M0p_FASL5xxFylG85JgEn07OB5Wu_YKfgkvA5wnYme3uwXgQyji9g1HQqhZcFKyiCaonCNIR_hjwImgDVqcwPOgoOmf-N8ATI-65JA</recordid><startdate>20030207</startdate><enddate>20030207</enddate><creator>Nevins, Tara A.</creator><creator>Harder, Zdena M.</creator><creator>Korneluk, Robert G.</creator><creator>Holčı́k, Martin</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</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></search><sort><creationdate>20030207</creationdate><title>Distinct Regulation of Internal Ribosome Entry Site-mediated Translation following Cellular Stress Is Mediated by Apoptotic Fragments of eIF4G Translation Initiation Factor Family Members eIF4GI and p97/DAP5/NAT1</title><author>Nevins, Tara A. ; Harder, Zdena M. ; Korneluk, Robert G. ; Holčı́k, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3980-c26089b9d272e2b46167fb25743e44f2ecad650fb6e00d45b8bf1361e5aff6473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Cell Line</topic><topic>Etoposide - pharmacology</topic><topic>Eukaryotic Initiation Factor-4G</topic><topic>Humans</topic><topic>Oxidative Stress</topic><topic>Peptide Fragments - physiology</topic><topic>Peptide Initiation Factors - physiology</topic><topic>Protein Biosynthesis - drug effects</topic><topic>Protein Biosynthesis - physiology</topic><topic>Ribosomes - metabolism</topic><topic>RNA, Messenger - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nevins, Tara A.</creatorcontrib><creatorcontrib>Harder, Zdena M.</creatorcontrib><creatorcontrib>Korneluk, Robert G.</creatorcontrib><creatorcontrib>Holčı́k, Martin</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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nevins, Tara A.</au><au>Harder, Zdena M.</au><au>Korneluk, Robert G.</au><au>Holčı́k, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distinct Regulation of Internal Ribosome Entry Site-mediated Translation following Cellular Stress Is Mediated by Apoptotic Fragments of eIF4G Translation Initiation Factor Family Members eIF4GI and p97/DAP5/NAT1</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2003-02-07</date><risdate>2003</risdate><volume>278</volume><issue>6</issue><spage>3572</spage><epage>3579</epage><pages>3572-3579</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Many cellular stresses lead to the inhibition of protein synthesis. Despite this, some cellular mRNAs are selectively translated under these conditions. It was suggested that the presence of internal ribosome entry site (IRES) sequences in the 5′-untranslated regions allow these mRNAs to be actively translated despite the overall cessation of protein synthesis. Here we tested the hypothesis that the IRES elements of genes that are involved in the control of cell survival are distinctly regulated by cellular stresses. We show that the transient conditions of cellular stress favor the translation of pro-survival IRES, while the severe apoptotic conditions support translation of pro-death IRES elements. Furthermore, activation of pro-death IRES during the etoposide-induced apoptosis is caspase-dependent and correlates with the expression of apoptotic fragments of two members of the eIF4G translation initiation factor family, p97/DAP5/NAT1 and eIF4GI. Our results suggest that the regulation of IRES translation during stress contributes to the fine-tuning of cell fate.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12458215</pmid><doi>10.1074/jbc.M206781200</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2003-02, Vol.278 (6), p.3572-3579 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_18652110 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Apoptosis Cell Line Etoposide - pharmacology Eukaryotic Initiation Factor-4G Humans Oxidative Stress Peptide Fragments - physiology Peptide Initiation Factors - physiology Protein Biosynthesis - drug effects Protein Biosynthesis - physiology Ribosomes - metabolism RNA, Messenger - genetics |
| title | Distinct Regulation of Internal Ribosome Entry Site-mediated Translation following Cellular Stress Is Mediated by Apoptotic Fragments of eIF4G Translation Initiation Factor Family Members eIF4GI and p97/DAP5/NAT1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T17%3A27%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Distinct%20Regulation%20of%20Internal%20Ribosome%20Entry%20Site-mediated%20Translation%20following%20Cellular%20Stress%20Is%20Mediated%20by%20Apoptotic%20Fragments%20of%20eIF4G%20Translation%20Initiation%20Factor%20Family%20Members%20eIF4GI%20and%20p97/DAP5/NAT1&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Nevins,%20Tara%20A.&rft.date=2003-02-07&rft.volume=278&rft.issue=6&rft.spage=3572&rft.epage=3579&rft.pages=3572-3579&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.M206781200&rft_dat=%3Cproquest_cross%3E18652110%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=18652110&rft_id=info:pmid/12458215&rft_els_id=S0021925819307604&rfr_iscdi=true |