Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival
PML/RARalpha is the abnormal protein product of the Acute Promyelocytic Leukemia-specific 15;17 translocation. Both the PML and RARalpha components are required for the PML/RARalpha biological activities, namely its capacity to block differentiation and to increase survival of haematopoietic precurs...
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| Veröffentlicht in: | Oncogene 1998-06, Vol.16 (22), p.2905-2913 |
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| creator | FAGIOLI, M ALCALAY, M PELICCI, P. G TOMASSON, L FERRUCCI, P. F MENCARELLI, A RIGANELLI, D GRIGNANI, Francesco POZZAN, T NICOLETTI, I GRIGNANI, Fausto |
| description | PML/RARalpha is the abnormal protein product of the Acute Promyelocytic Leukemia-specific 15;17 translocation. Both the PML and RARalpha components are required for the PML/RARalpha biological activities, namely its capacity to block differentiation and to increase survival of haematopoietic precursors. The physiological role of PML and its contribution to the function of the fusion protein are unknown. PML localizes to the cytoplasm and within specific nuclear bodies (NBs). In vitro, overexpression of PML correlates with suppression of cell transformation. The PML aminoterminal portion retained within the PML/RARalpha protein contains the RING finger, two newly defined cystein/histidine-rich motifs called B-boxes (B1 and B2) and a coiled-coil region. We report here that PML has a growth suppressive activity in all the cell lines tested, regardless of their transformed phenotype, and that the cellular basis for the PML growth suppression is induction of apoptotic cell death. Analysis of various nuclear and cytoplasmic PML isoforms showed that the PML growth suppressive activity correlates with its nuclear localization. Analysis of the localization and growth suppressive activity demonstrated that: (i) the Ring + B1-B2 and coiled-coil regions are both indispensable and sufficient to target PML to the NBs; (ii) individual deletions of the various PML domains have no effect on its growth suppressor activity; (iii) the Ring + B1-B2 region exerts a partial growth suppressor activity but its fusion with the coiled-coil region is sufficient to recapitulate the suppressive function of wild type PML. These results indicate that PML is involved in cell survival regulation and that the PML component of the fusion protein (Ring + B1-B2 and coiled-coil regions) retains intact biological activity, thereby suggesting that the effects of PML/RARalpha on survival derive from the activation of the incorporated PML sequence. |
| doi_str_mv | 10.1038/sj.onc.1201811 |
| format | Article |
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G ; TOMASSON, L ; FERRUCCI, P. F ; MENCARELLI, A ; RIGANELLI, D ; GRIGNANI, Francesco ; POZZAN, T ; NICOLETTI, I ; GRIGNANI, Fausto</creator><creatorcontrib>FAGIOLI, M ; ALCALAY, M ; PELICCI, P. G ; TOMASSON, L ; FERRUCCI, P. F ; MENCARELLI, A ; RIGANELLI, D ; GRIGNANI, Francesco ; POZZAN, T ; NICOLETTI, I ; GRIGNANI, Fausto</creatorcontrib><description>PML/RARalpha is the abnormal protein product of the Acute Promyelocytic Leukemia-specific 15;17 translocation. Both the PML and RARalpha components are required for the PML/RARalpha biological activities, namely its capacity to block differentiation and to increase survival of haematopoietic precursors. The physiological role of PML and its contribution to the function of the fusion protein are unknown. PML localizes to the cytoplasm and within specific nuclear bodies (NBs). In vitro, overexpression of PML correlates with suppression of cell transformation. The PML aminoterminal portion retained within the PML/RARalpha protein contains the RING finger, two newly defined cystein/histidine-rich motifs called B-boxes (B1 and B2) and a coiled-coil region. We report here that PML has a growth suppressive activity in all the cell lines tested, regardless of their transformed phenotype, and that the cellular basis for the PML growth suppression is induction of apoptotic cell death. Analysis of various nuclear and cytoplasmic PML isoforms showed that the PML growth suppressive activity correlates with its nuclear localization. Analysis of the localization and growth suppressive activity demonstrated that: (i) the Ring + B1-B2 and coiled-coil regions are both indispensable and sufficient to target PML to the NBs; (ii) individual deletions of the various PML domains have no effect on its growth suppressor activity; (iii) the Ring + B1-B2 region exerts a partial growth suppressor activity but its fusion with the coiled-coil region is sufficient to recapitulate the suppressive function of wild type PML. These results indicate that PML is involved in cell survival regulation and that the PML component of the fusion protein (Ring + B1-B2 and coiled-coil regions) retains intact biological activity, thereby suggesting that the effects of PML/RARalpha on survival derive from the activation of the incorporated PML sequence.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/sj.onc.1201811</identifier><identifier>PMID: 9671411</identifier><language>eng</language><publisher>Basingstoke: Nature Publishing</publisher><subject>3T3 Cells ; Acute promyeloid leukemia ; Animals ; Apoptosis ; Binding Sites ; Biological activity ; Biological and medical sciences ; Cell death ; Cell Division ; Cell Line, Transformed ; Cell physiology ; Cell Survival ; Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes ; Cysteine - genetics ; Cysteine - physiology ; Cytoplasm ; Cytoplasm - metabolism ; Fundamental and applied biological sciences. Psychology ; Fusion protein ; HeLa Cells ; Hematologic and hematopoietic diseases ; Histidine ; Histidine - genetics ; Histidine - physiology ; Humans ; Isoforms ; Isomerism ; Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis ; Localization ; Medical sciences ; Mice ; Molecular and cellular biology ; Mutagenesis ; Neoplasm Proteins - genetics ; Neoplasm Proteins - physiology ; Nuclear Proteins ; Phenotypes ; Promyelocytic Leukemia Protein ; Promyeloid leukemia ; Proteins ; Transcription Factors - genetics ; Transcription Factors - physiology ; Tumor Cells, Cultured ; Tumor Suppressor Proteins ; Zinc Fingers - genetics ; Zinc Fingers - physiology</subject><ispartof>Oncogene, 1998-06, Vol.16 (22), p.2905-2913</ispartof><rights>1998 INIST-CNRS</rights><rights>Macmillan Publishers Limited 1998.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c378t-f95f3e4f09879cdf39d7fce8ef93a70b6104f91d9de0e60b628d33395792b3143</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2303320$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9671411$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>FAGIOLI, M</creatorcontrib><creatorcontrib>ALCALAY, M</creatorcontrib><creatorcontrib>PELICCI, P. G</creatorcontrib><creatorcontrib>TOMASSON, L</creatorcontrib><creatorcontrib>FERRUCCI, P. F</creatorcontrib><creatorcontrib>MENCARELLI, A</creatorcontrib><creatorcontrib>RIGANELLI, D</creatorcontrib><creatorcontrib>GRIGNANI, Francesco</creatorcontrib><creatorcontrib>POZZAN, T</creatorcontrib><creatorcontrib>NICOLETTI, I</creatorcontrib><creatorcontrib>GRIGNANI, Fausto</creatorcontrib><title>Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival</title><title>Oncogene</title><addtitle>Oncogene</addtitle><description>PML/RARalpha is the abnormal protein product of the Acute Promyelocytic Leukemia-specific 15;17 translocation. Both the PML and RARalpha components are required for the PML/RARalpha biological activities, namely its capacity to block differentiation and to increase survival of haematopoietic precursors. The physiological role of PML and its contribution to the function of the fusion protein are unknown. PML localizes to the cytoplasm and within specific nuclear bodies (NBs). In vitro, overexpression of PML correlates with suppression of cell transformation. The PML aminoterminal portion retained within the PML/RARalpha protein contains the RING finger, two newly defined cystein/histidine-rich motifs called B-boxes (B1 and B2) and a coiled-coil region. We report here that PML has a growth suppressive activity in all the cell lines tested, regardless of their transformed phenotype, and that the cellular basis for the PML growth suppression is induction of apoptotic cell death. Analysis of various nuclear and cytoplasmic PML isoforms showed that the PML growth suppressive activity correlates with its nuclear localization. Analysis of the localization and growth suppressive activity demonstrated that: (i) the Ring + B1-B2 and coiled-coil regions are both indispensable and sufficient to target PML to the NBs; (ii) individual deletions of the various PML domains have no effect on its growth suppressor activity; (iii) the Ring + B1-B2 region exerts a partial growth suppressor activity but its fusion with the coiled-coil region is sufficient to recapitulate the suppressive function of wild type PML. These results indicate that PML is involved in cell survival regulation and that the PML component of the fusion protein (Ring + B1-B2 and coiled-coil regions) retains intact biological activity, thereby suggesting that the effects of PML/RARalpha on survival derive from the activation of the incorporated PML sequence.</description><subject>3T3 Cells</subject><subject>Acute promyeloid leukemia</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Binding Sites</subject><subject>Biological activity</subject><subject>Biological and medical sciences</subject><subject>Cell death</subject><subject>Cell Division</subject><subject>Cell Line, Transformed</subject><subject>Cell physiology</subject><subject>Cell Survival</subject><subject>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</subject><subject>Cysteine - genetics</subject><subject>Cysteine - physiology</subject><subject>Cytoplasm</subject><subject>Cytoplasm - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fusion protein</subject><subject>HeLa Cells</subject><subject>Hematologic and hematopoietic diseases</subject><subject>Histidine</subject><subject>Histidine - genetics</subject><subject>Histidine - physiology</subject><subject>Humans</subject><subject>Isoforms</subject><subject>Isomerism</subject><subject>Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis</subject><subject>Localization</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Mutagenesis</subject><subject>Neoplasm Proteins - genetics</subject><subject>Neoplasm Proteins - physiology</subject><subject>Nuclear Proteins</subject><subject>Phenotypes</subject><subject>Promyelocytic Leukemia Protein</subject><subject>Promyeloid leukemia</subject><subject>Proteins</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - physiology</subject><subject>Tumor Cells, Cultured</subject><subject>Tumor Suppressor Proteins</subject><subject>Zinc Fingers - genetics</subject><subject>Zinc Fingers - physiology</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc9rVDEQx4Moda1evQkBxYu8NZPk_cjRLrUW1lZEzyGbTDDL22SbvNfif2-WPnrw9GWYz3yZmS8hb4GtgYnhc9mvU7Rr4AwGgGdkBbLvmrZV8jlZMdWyRnHBX5JXpewZY71i_Iycqa4HCbAid5uUjpjNFFKkO5weECOd_iD9eX1zRT_RC2guODXRUZvCiK45CXXpYEIsNHn64_uWhkIjWizF5L_Up0zDVCh6j7Zq9bU4jrTM-T7cm_E1eeHNWPDNoufk99fLX5tvzfb26nrzZdtY0Q9T41XrBUrP1NAr67xQrvcWB_RKmJ7tOmDSK3DKIcOu1nxwQgjV9orvBEhxTj4--h5zupuxTPoQymkTEzHNRUMnJZPQVfD9f-A-zTnW3TTvJAjWiVZUav1I2ZxKyej1MYdDPVgD06ckdNnrmoRekqgD7xbbeXdA94Qvr6_9D0vfFGtGn020oTxhXDAhOBP_AN1Kj4A</recordid><startdate>19980604</startdate><enddate>19980604</enddate><creator>FAGIOLI, M</creator><creator>ALCALAY, M</creator><creator>PELICCI, P. G</creator><creator>TOMASSON, L</creator><creator>FERRUCCI, P. F</creator><creator>MENCARELLI, A</creator><creator>RIGANELLI, D</creator><creator>GRIGNANI, Francesco</creator><creator>POZZAN, T</creator><creator>NICOLETTI, I</creator><creator>GRIGNANI, Fausto</creator><general>Nature Publishing</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>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>19980604</creationdate><title>Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival</title><author>FAGIOLI, M ; ALCALAY, M ; PELICCI, P. G ; TOMASSON, L ; FERRUCCI, P. F ; MENCARELLI, A ; RIGANELLI, D ; GRIGNANI, Francesco ; POZZAN, T ; NICOLETTI, I ; GRIGNANI, Fausto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-f95f3e4f09879cdf39d7fce8ef93a70b6104f91d9de0e60b628d33395792b3143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>3T3 Cells</topic><topic>Acute promyeloid leukemia</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Binding Sites</topic><topic>Biological activity</topic><topic>Biological and medical sciences</topic><topic>Cell death</topic><topic>Cell Division</topic><topic>Cell Line, Transformed</topic><topic>Cell physiology</topic><topic>Cell Survival</topic><topic>Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes</topic><topic>Cysteine - genetics</topic><topic>Cysteine - physiology</topic><topic>Cytoplasm</topic><topic>Cytoplasm - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fusion protein</topic><topic>HeLa Cells</topic><topic>Hematologic and hematopoietic diseases</topic><topic>Histidine</topic><topic>Histidine - genetics</topic><topic>Histidine - physiology</topic><topic>Humans</topic><topic>Isoforms</topic><topic>Isomerism</topic><topic>Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis</topic><topic>Localization</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Mutagenesis</topic><topic>Neoplasm Proteins - genetics</topic><topic>Neoplasm Proteins - physiology</topic><topic>Nuclear Proteins</topic><topic>Phenotypes</topic><topic>Promyelocytic Leukemia Protein</topic><topic>Promyeloid leukemia</topic><topic>Proteins</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - physiology</topic><topic>Tumor Cells, Cultured</topic><topic>Tumor Suppressor Proteins</topic><topic>Zinc Fingers - genetics</topic><topic>Zinc Fingers - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>FAGIOLI, M</creatorcontrib><creatorcontrib>ALCALAY, M</creatorcontrib><creatorcontrib>PELICCI, P. G</creatorcontrib><creatorcontrib>TOMASSON, L</creatorcontrib><creatorcontrib>FERRUCCI, P. F</creatorcontrib><creatorcontrib>MENCARELLI, A</creatorcontrib><creatorcontrib>RIGANELLI, D</creatorcontrib><creatorcontrib>GRIGNANI, Francesco</creatorcontrib><creatorcontrib>POZZAN, T</creatorcontrib><creatorcontrib>NICOLETTI, I</creatorcontrib><creatorcontrib>GRIGNANI, Fausto</creatorcontrib><collection>Pascal-Francis</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>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>FAGIOLI, M</au><au>ALCALAY, M</au><au>PELICCI, P. G</au><au>TOMASSON, L</au><au>FERRUCCI, P. F</au><au>MENCARELLI, A</au><au>RIGANELLI, D</au><au>GRIGNANI, Francesco</au><au>POZZAN, T</au><au>NICOLETTI, I</au><au>GRIGNANI, Fausto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival</atitle><jtitle>Oncogene</jtitle><addtitle>Oncogene</addtitle><date>1998-06-04</date><risdate>1998</risdate><volume>16</volume><issue>22</issue><spage>2905</spage><epage>2913</epage><pages>2905-2913</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><abstract>PML/RARalpha is the abnormal protein product of the Acute Promyelocytic Leukemia-specific 15;17 translocation. Both the PML and RARalpha components are required for the PML/RARalpha biological activities, namely its capacity to block differentiation and to increase survival of haematopoietic precursors. The physiological role of PML and its contribution to the function of the fusion protein are unknown. PML localizes to the cytoplasm and within specific nuclear bodies (NBs). In vitro, overexpression of PML correlates with suppression of cell transformation. The PML aminoterminal portion retained within the PML/RARalpha protein contains the RING finger, two newly defined cystein/histidine-rich motifs called B-boxes (B1 and B2) and a coiled-coil region. We report here that PML has a growth suppressive activity in all the cell lines tested, regardless of their transformed phenotype, and that the cellular basis for the PML growth suppression is induction of apoptotic cell death. Analysis of various nuclear and cytoplasmic PML isoforms showed that the PML growth suppressive activity correlates with its nuclear localization. Analysis of the localization and growth suppressive activity demonstrated that: (i) the Ring + B1-B2 and coiled-coil regions are both indispensable and sufficient to target PML to the NBs; (ii) individual deletions of the various PML domains have no effect on its growth suppressor activity; (iii) the Ring + B1-B2 region exerts a partial growth suppressor activity but its fusion with the coiled-coil region is sufficient to recapitulate the suppressive function of wild type PML. These results indicate that PML is involved in cell survival regulation and that the PML component of the fusion protein (Ring + B1-B2 and coiled-coil regions) retains intact biological activity, thereby suggesting that the effects of PML/RARalpha on survival derive from the activation of the incorporated PML sequence.</abstract><cop>Basingstoke</cop><pub>Nature Publishing</pub><pmid>9671411</pmid><doi>10.1038/sj.onc.1201811</doi><tpages>9</tpages></addata></record> |
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| identifier | ISSN: 0950-9232 |
| ispartof | Oncogene, 1998-06, Vol.16 (22), p.2905-2913 |
| issn | 0950-9232 1476-5594 |
| language | eng |
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| source | MEDLINE; SpringerLink Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Nature Journals Online |
| subjects | 3T3 Cells Acute promyeloid leukemia Animals Apoptosis Binding Sites Biological activity Biological and medical sciences Cell death Cell Division Cell Line, Transformed Cell physiology Cell Survival Cell transformation and carcinogenesis. Action of oncogenes and antioncogenes Cysteine - genetics Cysteine - physiology Cytoplasm Cytoplasm - metabolism Fundamental and applied biological sciences. Psychology Fusion protein HeLa Cells Hematologic and hematopoietic diseases Histidine Histidine - genetics Histidine - physiology Humans Isoforms Isomerism Leukemias. Malignant lymphomas. Malignant reticulosis. Myelofibrosis Localization Medical sciences Mice Molecular and cellular biology Mutagenesis Neoplasm Proteins - genetics Neoplasm Proteins - physiology Nuclear Proteins Phenotypes Promyelocytic Leukemia Protein Promyeloid leukemia Proteins Transcription Factors - genetics Transcription Factors - physiology Tumor Cells, Cultured Tumor Suppressor Proteins Zinc Fingers - genetics Zinc Fingers - physiology |
| title | Cooperation between the RING + B1-B2 and coiled-coil domains of PML is necessary for its effects on cell survival |
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