Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)
The tumor suppressor protein p53 functions as a transcriptional factor that activates genes controlling cell cycle arrest and apoptosis. Here, we report that protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid a...
Gespeichert in:
| Veröffentlicht in: | The Journal of biological chemistry 2002-03, Vol.277 (10), p.8255-8259 |
|---|---|
| Hauptverfasser: | , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 8259 |
|---|---|
| container_issue | 10 |
| container_start_page | 8255 |
| container_title | The Journal of biological chemistry |
| container_volume | 277 |
| creator | Megidish, Tamar Xu, Juliana H. Xu, C. Wilson |
| description | The tumor suppressor protein p53 functions as a transcriptional factor that activates genes controlling cell cycle arrest and apoptosis. Here, we report that protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses. Endogenous PIAS1 is also associated with endogenous p53 in mammalian cells. Ectopic expression of PIAS1 activates p53-mediated expression in mouse embryonic fibroblast cells (p53−/−) as well as a variety of other cell lines. Furthermore, ectopic expression of PIAS1 induces p53-mediated expression of cyclin-dependent kinase inhibitor p21 and G1arrest of the cell cycle in H1299 cells. In addition, a PIAS1 mutant without the RING-finger domain required for sumoylation could still activate p53-mediated gene expression, indicating that activation of p53 by PIAS1 does not require the RING-finger domain. Taken together, our results suggest that PIAS1 is a novel activator of p53. |
| doi_str_mv | 10.1074/jbc.C200001200 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_71500048</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0021925819364269</els_id><sourcerecordid>71500048</sourcerecordid><originalsourceid>FETCH-LOGICAL-c505t-d2a765c225ca81f08cb8990ed16c12e68c79c641c4e48c6aaa1a92d1f8d988713</originalsourceid><addsrcrecordid>eNqF0MFr2zAUBnBROtq027XHYiiM7eBMT7Gs52MIWxcotNANdhOy_NyoJFYqKS397yuTQE9lOkgH_d6H9DF2AXwKXFU_Hls7XQieF-T9iE2A46ycSfh3zCacCygbIfGUncX4OKqqgRN2CqAQpcIJm89tcs8mOT8Uvi-2cla0r8Vd8IncUCyHlWtd8mG8O0jqivtkEhTf7pbze_j-mX3qzTrSl8N5zv7--vln8bu8ub1eLuY3pZVcprITRtXSCiGtQeg52habhlMHtQVBNVrV2LoCW1GFtjbGgGlEBz12DaKC2Tn7us_dBv-0o5j0xkVL67UZyO-iViDH_-F_IaColYQ6w-ke2uBjDNTrbXAbE141cD22q3O7-r3dPHB5SN61G-re-aHODK72YOUeVi8ukG6dtyvaaKHUmIpCyqxwryjX9ewo6GgdDZa6PGGT7rz76AVvNseQhQ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18267516</pqid></control><display><type>article</type><title>Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)</title><source>MEDLINE</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Megidish, Tamar ; Xu, Juliana H. ; Xu, C. Wilson</creator><creatorcontrib>Megidish, Tamar ; Xu, Juliana H. ; Xu, C. Wilson</creatorcontrib><description>The tumor suppressor protein p53 functions as a transcriptional factor that activates genes controlling cell cycle arrest and apoptosis. Here, we report that protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses. Endogenous PIAS1 is also associated with endogenous p53 in mammalian cells. Ectopic expression of PIAS1 activates p53-mediated expression in mouse embryonic fibroblast cells (p53−/−) as well as a variety of other cell lines. Furthermore, ectopic expression of PIAS1 induces p53-mediated expression of cyclin-dependent kinase inhibitor p21 and G1arrest of the cell cycle in H1299 cells. In addition, a PIAS1 mutant without the RING-finger domain required for sumoylation could still activate p53-mediated gene expression, indicating that activation of p53 by PIAS1 does not require the RING-finger domain. Taken together, our results suggest that PIAS1 is a novel activator of p53.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.C200001200</identifier><identifier>PMID: 11788578</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Blotting, Western ; Cell Cycle ; Cell Line ; Cells, Cultured ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins - metabolism ; DNA, Complementary - metabolism ; Fibroblasts - metabolism ; G1 Phase ; Genes, p53 - genetics ; Genes, Reporter ; Glucose-6-Phosphate - metabolism ; HeLa Cells ; Humans ; Luciferases - metabolism ; Mice ; PIAS1 protein ; Plasmids - metabolism ; Precipitin Tests ; Protein Binding ; Protein Inhibitors of Activated STAT ; Protein Structure, Tertiary ; Proteins - chemistry ; Proteins - metabolism ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53 - metabolism ; Two-Hybrid System Techniques</subject><ispartof>The Journal of biological chemistry, 2002-03, Vol.277 (10), p.8255-8259</ispartof><rights>2002 © 2002 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-c505t-d2a765c225ca81f08cb8990ed16c12e68c79c641c4e48c6aaa1a92d1f8d988713</citedby><cites>FETCH-LOGICAL-c505t-d2a765c225ca81f08cb8990ed16c12e68c79c641c4e48c6aaa1a92d1f8d988713</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11788578$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Megidish, Tamar</creatorcontrib><creatorcontrib>Xu, Juliana H.</creatorcontrib><creatorcontrib>Xu, C. Wilson</creatorcontrib><title>Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The tumor suppressor protein p53 functions as a transcriptional factor that activates genes controlling cell cycle arrest and apoptosis. Here, we report that protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses. Endogenous PIAS1 is also associated with endogenous p53 in mammalian cells. Ectopic expression of PIAS1 activates p53-mediated expression in mouse embryonic fibroblast cells (p53−/−) as well as a variety of other cell lines. Furthermore, ectopic expression of PIAS1 induces p53-mediated expression of cyclin-dependent kinase inhibitor p21 and G1arrest of the cell cycle in H1299 cells. In addition, a PIAS1 mutant without the RING-finger domain required for sumoylation could still activate p53-mediated gene expression, indicating that activation of p53 by PIAS1 does not require the RING-finger domain. Taken together, our results suggest that PIAS1 is a novel activator of p53.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Blotting, Western</subject><subject>Cell Cycle</subject><subject>Cell Line</subject><subject>Cells, Cultured</subject><subject>Cyclin-Dependent Kinase Inhibitor p21</subject><subject>Cyclins - metabolism</subject><subject>DNA, Complementary - metabolism</subject><subject>Fibroblasts - metabolism</subject><subject>G1 Phase</subject><subject>Genes, p53 - genetics</subject><subject>Genes, Reporter</subject><subject>Glucose-6-Phosphate - metabolism</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Luciferases - metabolism</subject><subject>Mice</subject><subject>PIAS1 protein</subject><subject>Plasmids - metabolism</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Protein Inhibitors of Activated STAT</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Transcription, Genetic</subject><subject>Transfection</subject><subject>Tumor Cells, Cultured</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Two-Hybrid System Techniques</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0MFr2zAUBnBROtq027XHYiiM7eBMT7Gs52MIWxcotNANdhOy_NyoJFYqKS397yuTQE9lOkgH_d6H9DF2AXwKXFU_Hls7XQieF-T9iE2A46ycSfh3zCacCygbIfGUncX4OKqqgRN2CqAQpcIJm89tcs8mOT8Uvi-2cla0r8Vd8IncUCyHlWtd8mG8O0jqivtkEhTf7pbze_j-mX3qzTrSl8N5zv7--vln8bu8ub1eLuY3pZVcprITRtXSCiGtQeg52habhlMHtQVBNVrV2LoCW1GFtjbGgGlEBz12DaKC2Tn7us_dBv-0o5j0xkVL67UZyO-iViDH_-F_IaColYQ6w-ke2uBjDNTrbXAbE141cD22q3O7-r3dPHB5SN61G-re-aHODK72YOUeVi8ukG6dtyvaaKHUmIpCyqxwryjX9ewo6GgdDZa6PGGT7rz76AVvNseQhQ</recordid><startdate>20020308</startdate><enddate>20020308</enddate><creator>Megidish, Tamar</creator><creator>Xu, Juliana H.</creator><creator>Xu, C. Wilson</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>7TO</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20020308</creationdate><title>Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)</title><author>Megidish, Tamar ; Xu, Juliana H. ; Xu, C. Wilson</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-d2a765c225ca81f08cb8990ed16c12e68c79c641c4e48c6aaa1a92d1f8d988713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Blotting, Western</topic><topic>Cell Cycle</topic><topic>Cell Line</topic><topic>Cells, Cultured</topic><topic>Cyclin-Dependent Kinase Inhibitor p21</topic><topic>Cyclins - metabolism</topic><topic>DNA, Complementary - metabolism</topic><topic>Fibroblasts - metabolism</topic><topic>G1 Phase</topic><topic>Genes, p53 - genetics</topic><topic>Genes, Reporter</topic><topic>Glucose-6-Phosphate - metabolism</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Luciferases - metabolism</topic><topic>Mice</topic><topic>PIAS1 protein</topic><topic>Plasmids - metabolism</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Protein Inhibitors of Activated STAT</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins - chemistry</topic><topic>Proteins - metabolism</topic><topic>Transcription, Genetic</topic><topic>Transfection</topic><topic>Tumor Cells, Cultured</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Megidish, Tamar</creatorcontrib><creatorcontrib>Xu, Juliana H.</creatorcontrib><creatorcontrib>Xu, C. Wilson</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>Oncogenes and Growth Factors Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Megidish, Tamar</au><au>Xu, Juliana H.</au><au>Xu, C. Wilson</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1)</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-03-08</date><risdate>2002</risdate><volume>277</volume><issue>10</issue><spage>8255</spage><epage>8259</epage><pages>8255-8259</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The tumor suppressor protein p53 functions as a transcriptional factor that activates genes controlling cell cycle arrest and apoptosis. Here, we report that protein inhibitor of activated Stat1 (PIAS1) interacts with the tetramerization and C-terminal regulatory domains of p53 in yeast two-hybrid analyses. Endogenous PIAS1 is also associated with endogenous p53 in mammalian cells. Ectopic expression of PIAS1 activates p53-mediated expression in mouse embryonic fibroblast cells (p53−/−) as well as a variety of other cell lines. Furthermore, ectopic expression of PIAS1 induces p53-mediated expression of cyclin-dependent kinase inhibitor p21 and G1arrest of the cell cycle in H1299 cells. In addition, a PIAS1 mutant without the RING-finger domain required for sumoylation could still activate p53-mediated gene expression, indicating that activation of p53 by PIAS1 does not require the RING-finger domain. Taken together, our results suggest that PIAS1 is a novel activator of p53.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11788578</pmid><doi>10.1074/jbc.C200001200</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 2002-03, Vol.277 (10), p.8255-8259 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71500048 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Adenosine Triphosphate - metabolism Animals Blotting, Western Cell Cycle Cell Line Cells, Cultured Cyclin-Dependent Kinase Inhibitor p21 Cyclins - metabolism DNA, Complementary - metabolism Fibroblasts - metabolism G1 Phase Genes, p53 - genetics Genes, Reporter Glucose-6-Phosphate - metabolism HeLa Cells Humans Luciferases - metabolism Mice PIAS1 protein Plasmids - metabolism Precipitin Tests Protein Binding Protein Inhibitors of Activated STAT Protein Structure, Tertiary Proteins - chemistry Proteins - metabolism Transcription, Genetic Transfection Tumor Cells, Cultured Tumor Suppressor Protein p53 - metabolism Two-Hybrid System Techniques |
| title | Activation of p53 by Protein Inhibitor of Activated Stat1 (PIAS1) |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T00%3A55%3A22IST&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=Activation%20of%20p53%20by%20Protein%20Inhibitor%20of%20Activated%20Stat1%20(PIAS1)&rft.jtitle=The%20Journal%20of%20biological%20chemistry&rft.au=Megidish,%20Tamar&rft.date=2002-03-08&rft.volume=277&rft.issue=10&rft.spage=8255&rft.epage=8259&rft.pages=8255-8259&rft.issn=0021-9258&rft.eissn=1083-351X&rft_id=info:doi/10.1074/jbc.C200001200&rft_dat=%3Cproquest_cross%3E71500048%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=18267516&rft_id=info:pmid/11788578&rft_els_id=S0021925819364269&rfr_iscdi=true |