p53 and little brother p53/47: linking IRES activities with protein functions
The tumor suppressor p53 represents a paradigm for gene regulation. Its rapid induction in response to DNA damage conditions has been attributed to both increased half-life of p53 protein and also increased translation of p53 mRNA. Recent advances in our understanding of the post-transcriptional reg...
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| Veröffentlicht in: | Oncogene 2009-07, Vol.28 (30), p.2766-2772 |
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| creator | Grover, R Candeias, M M Fåhraeus, R Das, S |
| description | The tumor suppressor p53 represents a paradigm for gene regulation. Its rapid induction in response to DNA damage conditions has been attributed to both increased half-life of p53 protein and also increased translation of p53 mRNA. Recent advances in our understanding of the post-transcriptional regulation of p53 include the discovery of internal ribosome entry sites (IRESs) within the p53 mRNA. These IRES elements regulate the translation of the full length as well as the N-terminally truncated isoform, p53/47. The p53/47 isoform is generated by alternative initiation at an internal AUG codon present within the p53 ORF. The aim of this review is to summarize the role of translational control mechanisms in regulating p53 functions. We discuss here in detail how diverse cellular stress pathways trigger alterations in the cap-dependent and cap-independent translation of p53 mRNA and how changes in the relative expression levels of p53 isoforms result in more differentiated p53 activity. |
| doi_str_mv | 10.1038/onc.2009.138 |
| format | Article |
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Its rapid induction in response to DNA damage conditions has been attributed to both increased half-life of p53 protein and also increased translation of p53 mRNA. Recent advances in our understanding of the post-transcriptional regulation of p53 include the discovery of internal ribosome entry sites (IRESs) within the p53 mRNA. These IRES elements regulate the translation of the full length as well as the N-terminally truncated isoform, p53/47. The p53/47 isoform is generated by alternative initiation at an internal AUG codon present within the p53 ORF. The aim of this review is to summarize the role of translational control mechanisms in regulating p53 functions. We discuss here in detail how diverse cellular stress pathways trigger alterations in the cap-dependent and cap-independent translation of p53 mRNA and how changes in the relative expression levels of p53 isoforms result in more differentiated p53 activity.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/onc.2009.138</identifier><identifier>PMID: 19483723</identifier><identifier>CODEN: ONCNES</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Apoptosis ; Biological and medical sciences ; Cancer ; Cell Biology ; Cell physiology ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Cellular biology ; Cellular stress response ; DNA damage ; Fundamental and applied biological sciences. Psychology ; Gene regulation ; Genetic aspects ; Genetic translation ; Genetics ; Human Genetics ; Humans ; Internal Medicine ; Isoforms ; Medicine ; Medicine & Public Health ; Molecular and cellular biology ; oncogenomics ; Oncology ; p53 Protein ; Physiological aspects ; Post-transcription ; Properties ; Protein Biosynthesis ; Protein Isoforms - physiology ; Ribonucleic acid ; Ribosomes - metabolism ; RNA ; RNA, Messenger - analysis ; Stress, Physiological ; Translation ; Tumor suppressor genes ; Tumor Suppressor Protein p53 - physiology ; Tumors</subject><ispartof>Oncogene, 2009-07, Vol.28 (30), p.2766-2772</ispartof><rights>Macmillan Publishers Limited 2009</rights><rights>2009 INIST-CNRS</rights><rights>COPYRIGHT 2009 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Jul 30, 2009</rights><rights>Macmillan Publishers Limited 2009.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c478t-f0732d60820cf144f473b5c618b09f552534880d4ed74d9c7a1bbf82ffd1ed353</citedby><cites>FETCH-LOGICAL-c478t-f0732d60820cf144f473b5c618b09f552534880d4ed74d9c7a1bbf82ffd1ed353</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/onc.2009.138$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/onc.2009.138$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21819966$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19483723$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Grover, R</creatorcontrib><creatorcontrib>Candeias, M M</creatorcontrib><creatorcontrib>Fåhraeus, R</creatorcontrib><creatorcontrib>Das, S</creatorcontrib><title>p53 and little brother p53/47: linking IRES activities with protein functions</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>The tumor suppressor p53 represents a paradigm for gene regulation. Its rapid induction in response to DNA damage conditions has been attributed to both increased half-life of p53 protein and also increased translation of p53 mRNA. Recent advances in our understanding of the post-transcriptional regulation of p53 include the discovery of internal ribosome entry sites (IRESs) within the p53 mRNA. These IRES elements regulate the translation of the full length as well as the N-terminally truncated isoform, p53/47. The p53/47 isoform is generated by alternative initiation at an internal AUG codon present within the p53 ORF. The aim of this review is to summarize the role of translational control mechanisms in regulating p53 functions. We discuss here in detail how diverse cellular stress pathways trigger alterations in the cap-dependent and cap-independent translation of p53 mRNA and how changes in the relative expression levels of p53 isoforms result in more differentiated p53 activity.</description><subject>Animals</subject><subject>Apoptosis</subject><subject>Biological and medical sciences</subject><subject>Cancer</subject><subject>Cell Biology</subject><subject>Cell physiology</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Cellular biology</subject><subject>Cellular stress response</subject><subject>DNA damage</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene regulation</subject><subject>Genetic aspects</subject><subject>Genetic translation</subject><subject>Genetics</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>Isoforms</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Molecular and cellular biology</subject><subject>oncogenomics</subject><subject>Oncology</subject><subject>p53 Protein</subject><subject>Physiological aspects</subject><subject>Post-transcription</subject><subject>Properties</subject><subject>Protein Biosynthesis</subject><subject>Protein Isoforms - physiology</subject><subject>Ribonucleic acid</subject><subject>Ribosomes - metabolism</subject><subject>RNA</subject><subject>RNA, Messenger - analysis</subject><subject>Stress, Physiological</subject><subject>Translation</subject><subject>Tumor suppressor genes</subject><subject>Tumor Suppressor Protein p53 - physiology</subject><subject>Tumors</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkttrFDEUh4Modlt981mCok_O9uQ2SXwrpWqhInh5DplMsk2dzazJjNL_3qy7uCgVyUPgnO_cfwg9IbAkwNTpmNySAuglYeoeWhAu20YIze-jBWgBjaaMHqHjUm4AQGqgD9ER0VwxSdkCvd8Ihm3q8RCnafC4y-N07TOu5lMuX1dz-hrTCl9-vPiErZvi9zhFX_CPOF3jTYV9TDjMqXrGVB6hB8EOxT_e_yfoy5uLz-fvmqsPby_Pz64ax6WamgCS0b4FRcEFwnngknXCtUR1oIMQVDCuFPTc95L32klLui4oGkJPfM8EO0Evd3lrB99mXyazjsX5YbDJj3MxrRSMAZP_BSkhdSWgKvj8L_BmnHOqQxjacsI0YS1U6tk_KSoZb0XbHlKt7OBNTGGcsnXbuuaM1gsIKSir1PIOqr7er6Mbkw-x2v8IeLULcHksJftgNjmubb41BMxWCaYqwWyVYKoSKv503-rcrX1_gPenr8CLPWCLs0PINrlYfnOUKKL1r3GaHVeqK618Psx8Z-GfMNfFFQ</recordid><startdate>20090730</startdate><enddate>20090730</enddate><creator>Grover, R</creator><creator>Candeias, M M</creator><creator>Fåhraeus, R</creator><creator>Das, S</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>IQODW</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>3V.</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20090730</creationdate><title>p53 and little brother p53/47: linking IRES activities with protein functions</title><author>Grover, R ; Candeias, M M ; Fåhraeus, R ; Das, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-f0732d60820cf144f473b5c618b09f552534880d4ed74d9c7a1bbf82ffd1ed353</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Apoptosis</topic><topic>Biological and medical sciences</topic><topic>Cancer</topic><topic>Cell Biology</topic><topic>Cell physiology</topic><topic>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</topic><topic>Cellular biology</topic><topic>Cellular stress response</topic><topic>DNA damage</topic><topic>Fundamental and applied biological sciences. 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| subjects | Animals Apoptosis Biological and medical sciences Cancer Cell Biology Cell physiology Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cellular biology Cellular stress response DNA damage Fundamental and applied biological sciences. Psychology Gene regulation Genetic aspects Genetic translation Genetics Human Genetics Humans Internal Medicine Isoforms Medicine Medicine & Public Health Molecular and cellular biology oncogenomics Oncology p53 Protein Physiological aspects Post-transcription Properties Protein Biosynthesis Protein Isoforms - physiology Ribonucleic acid Ribosomes - metabolism RNA RNA, Messenger - analysis Stress, Physiological Translation Tumor suppressor genes Tumor Suppressor Protein p53 - physiology Tumors |
| title | p53 and little brother p53/47: linking IRES activities with protein functions |
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