Activation of NFAT signal by p53-K120R mutant
The tumor suppressor p53 is activated by phosphorylation and/or acetylation. We constructed 14 non-phosphorylated, 11 phospho-mimetic, and 1 non-acetylated point p53 mutations and compared their transactivation ability in U-87 human glioblastoma cells by the luciferase reporter assay. Despite mutati...
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| Veröffentlicht in: | FEBS letters 2009-06, Vol.583 (12), p.1916-1922 |
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| container_issue | 12 |
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| container_title | FEBS letters |
| container_volume | 583 |
| creator | Shinmen, Natsuko Koshida, Toshifumi Kumazawa, Takeshi Sato, Keizo Shimada, Hideaki Matsutani, Tomoo Iwadate, Yasuo Takiguchi, Masaki Hiwasa, Takaki |
| description | The tumor suppressor p53 is activated by phosphorylation and/or acetylation. We constructed 14 non-phosphorylated, 11 phospho-mimetic, and 1 non-acetylated point p53 mutations and compared their transactivation ability in U-87 human glioblastoma cells by the luciferase reporter assay. Despite mutations at the phosphorylation sites, only the p53-K120R and p53-S9E mutants had marginally reduced activities. On the other hand, the Nuclear factor of activated T-cells (NFAT)-luciferase reporter was more potently activated by p53-K120R than by wild-type p53 and other mutants in glioblastoma, hepatoma and esophageal carcinoma cells. This suggests that acetylation at Lys-120 of p53 negatively regulates a signaling pathway leading to NFAT activation. |
| doi_str_mv | 10.1016/j.febslet.2009.04.041 |
| format | Article |
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We constructed 14 non-phosphorylated, 11 phospho-mimetic, and 1 non-acetylated point p53 mutations and compared their transactivation ability in U-87 human glioblastoma cells by the luciferase reporter assay. Despite mutations at the phosphorylation sites, only the p53-K120R and p53-S9E mutants had marginally reduced activities. On the other hand, the Nuclear factor of activated T-cells (NFAT)-luciferase reporter was more potently activated by p53-K120R than by wild-type p53 and other mutants in glioblastoma, hepatoma and esophageal carcinoma cells. This suggests that acetylation at Lys-120 of p53 negatively regulates a signaling pathway leading to NFAT activation.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2009.04.041</identifier><identifier>PMID: 19416725</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Acetylation ; Binding Sites - genetics ; Calcium signal ; Carcinoma, Hepatocellular - genetics ; Carcinoma, Hepatocellular - metabolism ; Cell Line, Tumor ; Esophageal Neoplasms - genetics ; Esophageal Neoplasms - metabolism ; Genes, Reporter ; Glioblastoma - genetics ; Glioblastoma - metabolism ; Humans ; Luciferase reporter assay ; Luciferases - genetics ; Lysine - chemistry ; Mutagenesis, Site-Directed ; NFATC Transcription Factors - genetics ; NFATC Transcription Factors - metabolism ; Nuclear factor of activated T-cell ; p53 ; Phosphorylation ; Point Mutation ; Proline Oxidase - metabolism ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; RNA, Neoplasm - genetics ; RNA, Neoplasm - metabolism ; Signal Transduction ; Transcriptional Activation ; Transfection ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Protein p53 - genetics ; Tumor Suppressor Protein p53 - metabolism ; Urinary Bladder Neoplasms - genetics ; Urinary Bladder Neoplasms - metabolism</subject><ispartof>FEBS letters, 2009-06, Vol.583 (12), p.1916-1922</ispartof><rights>2009 Federation of European Biochemical Societies</rights><rights>FEBS Letters 583 (2009) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5722-843b9c405884801209dcabe1890f4b05519a8cafc7151c4a04350f3eb8c7b0d73</citedby><cites>FETCH-LOGICAL-c5722-843b9c405884801209dcabe1890f4b05519a8cafc7151c4a04350f3eb8c7b0d73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2009.04.041$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579309003342$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19416725$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shinmen, Natsuko</creatorcontrib><creatorcontrib>Koshida, Toshifumi</creatorcontrib><creatorcontrib>Kumazawa, Takeshi</creatorcontrib><creatorcontrib>Sato, Keizo</creatorcontrib><creatorcontrib>Shimada, Hideaki</creatorcontrib><creatorcontrib>Matsutani, Tomoo</creatorcontrib><creatorcontrib>Iwadate, Yasuo</creatorcontrib><creatorcontrib>Takiguchi, Masaki</creatorcontrib><creatorcontrib>Hiwasa, Takaki</creatorcontrib><title>Activation of NFAT signal by p53-K120R mutant</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The tumor suppressor p53 is activated by phosphorylation and/or acetylation. We constructed 14 non-phosphorylated, 11 phospho-mimetic, and 1 non-acetylated point p53 mutations and compared their transactivation ability in U-87 human glioblastoma cells by the luciferase reporter assay. Despite mutations at the phosphorylation sites, only the p53-K120R and p53-S9E mutants had marginally reduced activities. On the other hand, the Nuclear factor of activated T-cells (NFAT)-luciferase reporter was more potently activated by p53-K120R than by wild-type p53 and other mutants in glioblastoma, hepatoma and esophageal carcinoma cells. This suggests that acetylation at Lys-120 of p53 negatively regulates a signaling pathway leading to NFAT activation.</description><subject>Acetylation</subject><subject>Binding Sites - genetics</subject><subject>Calcium signal</subject><subject>Carcinoma, Hepatocellular - genetics</subject><subject>Carcinoma, Hepatocellular - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Esophageal Neoplasms - genetics</subject><subject>Esophageal Neoplasms - metabolism</subject><subject>Genes, Reporter</subject><subject>Glioblastoma - genetics</subject><subject>Glioblastoma - metabolism</subject><subject>Humans</subject><subject>Luciferase reporter assay</subject><subject>Luciferases - genetics</subject><subject>Lysine - chemistry</subject><subject>Mutagenesis, Site-Directed</subject><subject>NFATC Transcription Factors - genetics</subject><subject>NFATC Transcription Factors - metabolism</subject><subject>Nuclear factor of activated T-cell</subject><subject>p53</subject><subject>Phosphorylation</subject><subject>Point Mutation</subject><subject>Proline Oxidase - metabolism</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>RNA, Messenger - genetics</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA, Neoplasm - genetics</subject><subject>RNA, Neoplasm - metabolism</subject><subject>Signal Transduction</subject><subject>Transcriptional Activation</subject><subject>Transfection</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor Suppressor Protein p53 - genetics</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Urinary Bladder Neoplasms - genetics</subject><subject>Urinary Bladder Neoplasms - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkFFLwzAUhYMobk5_gtIn3zrvbZI2eZI5NicOBZ3PIU1Tyeja2XST_XszNvBR4cDlwjnnXj5CrhGGCJjeLYelzX1lu2ECIIfAgvCE9FFkNKYsFaekD4As5pmkPXLh_RLCLlCekx5KhmmW8D6JR6ZzW925po6aMnqZjhaRd5-1rqJ8F605jZ8xgbdotel03V2Ss1JX3l4d54B8TCeL8Syevz4-jUfz2PAsSWLBaC4NAy4EExDysjA6tygklCwHzlFqYXRpMuRomAZGOZTU5sJkORQZHZDbQ--6bb421ndq5byxVaVr22y8SiDlGaZpMPKD0bSN960t1bp1K93uFILac1JLdeSk9pwUsCAMuZvjgU2-ssVv6ggmGGYHw7er7O5_rWo6eUje99D3zEECUMqSUHV_qLKB2NbZVnnjbG1s4VprOlU07o9vfwD45o2T</recordid><startdate>20090618</startdate><enddate>20090618</enddate><creator>Shinmen, Natsuko</creator><creator>Koshida, Toshifumi</creator><creator>Kumazawa, Takeshi</creator><creator>Sato, Keizo</creator><creator>Shimada, Hideaki</creator><creator>Matsutani, Tomoo</creator><creator>Iwadate, Yasuo</creator><creator>Takiguchi, Masaki</creator><creator>Hiwasa, Takaki</creator><general>Elsevier B.V</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>H94</scope></search><sort><creationdate>20090618</creationdate><title>Activation of NFAT signal by p53-K120R mutant</title><author>Shinmen, Natsuko ; Koshida, Toshifumi ; Kumazawa, Takeshi ; Sato, Keizo ; Shimada, Hideaki ; Matsutani, Tomoo ; Iwadate, Yasuo ; Takiguchi, Masaki ; Hiwasa, Takaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5722-843b9c405884801209dcabe1890f4b05519a8cafc7151c4a04350f3eb8c7b0d73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Acetylation</topic><topic>Binding Sites - genetics</topic><topic>Calcium signal</topic><topic>Carcinoma, Hepatocellular - genetics</topic><topic>Carcinoma, Hepatocellular - metabolism</topic><topic>Cell Line, Tumor</topic><topic>Esophageal Neoplasms - genetics</topic><topic>Esophageal Neoplasms - metabolism</topic><topic>Genes, Reporter</topic><topic>Glioblastoma - genetics</topic><topic>Glioblastoma - metabolism</topic><topic>Humans</topic><topic>Luciferase reporter assay</topic><topic>Luciferases - genetics</topic><topic>Lysine - chemistry</topic><topic>Mutagenesis, Site-Directed</topic><topic>NFATC Transcription Factors - genetics</topic><topic>NFATC Transcription Factors - metabolism</topic><topic>Nuclear factor of activated T-cell</topic><topic>p53</topic><topic>Phosphorylation</topic><topic>Point Mutation</topic><topic>Proline Oxidase - metabolism</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA, Messenger - genetics</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA, Neoplasm - genetics</topic><topic>RNA, Neoplasm - metabolism</topic><topic>Signal Transduction</topic><topic>Transcriptional Activation</topic><topic>Transfection</topic><topic>Tumor Suppressor Protein p53 - chemistry</topic><topic>Tumor Suppressor Protein p53 - genetics</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><topic>Urinary Bladder Neoplasms - genetics</topic><topic>Urinary Bladder Neoplasms - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shinmen, Natsuko</creatorcontrib><creatorcontrib>Koshida, Toshifumi</creatorcontrib><creatorcontrib>Kumazawa, Takeshi</creatorcontrib><creatorcontrib>Sato, Keizo</creatorcontrib><creatorcontrib>Shimada, Hideaki</creatorcontrib><creatorcontrib>Matsutani, Tomoo</creatorcontrib><creatorcontrib>Iwadate, Yasuo</creatorcontrib><creatorcontrib>Takiguchi, Masaki</creatorcontrib><creatorcontrib>Hiwasa, Takaki</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>AIDS and Cancer Research Abstracts</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shinmen, Natsuko</au><au>Koshida, Toshifumi</au><au>Kumazawa, Takeshi</au><au>Sato, Keizo</au><au>Shimada, Hideaki</au><au>Matsutani, Tomoo</au><au>Iwadate, Yasuo</au><au>Takiguchi, Masaki</au><au>Hiwasa, Takaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Activation of NFAT signal by p53-K120R mutant</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2009-06-18</date><risdate>2009</risdate><volume>583</volume><issue>12</issue><spage>1916</spage><epage>1922</epage><pages>1916-1922</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The tumor suppressor p53 is activated by phosphorylation and/or acetylation. We constructed 14 non-phosphorylated, 11 phospho-mimetic, and 1 non-acetylated point p53 mutations and compared their transactivation ability in U-87 human glioblastoma cells by the luciferase reporter assay. Despite mutations at the phosphorylation sites, only the p53-K120R and p53-S9E mutants had marginally reduced activities. On the other hand, the Nuclear factor of activated T-cells (NFAT)-luciferase reporter was more potently activated by p53-K120R than by wild-type p53 and other mutants in glioblastoma, hepatoma and esophageal carcinoma cells. This suggests that acetylation at Lys-120 of p53 negatively regulates a signaling pathway leading to NFAT activation.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>19416725</pmid><doi>10.1016/j.febslet.2009.04.041</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Acetylation Binding Sites - genetics Calcium signal Carcinoma, Hepatocellular - genetics Carcinoma, Hepatocellular - metabolism Cell Line, Tumor Esophageal Neoplasms - genetics Esophageal Neoplasms - metabolism Genes, Reporter Glioblastoma - genetics Glioblastoma - metabolism Humans Luciferase reporter assay Luciferases - genetics Lysine - chemistry Mutagenesis, Site-Directed NFATC Transcription Factors - genetics NFATC Transcription Factors - metabolism Nuclear factor of activated T-cell p53 Phosphorylation Point Mutation Proline Oxidase - metabolism Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism RNA, Messenger - genetics RNA, Messenger - metabolism RNA, Neoplasm - genetics RNA, Neoplasm - metabolism Signal Transduction Transcriptional Activation Transfection Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - genetics Tumor Suppressor Protein p53 - metabolism Urinary Bladder Neoplasms - genetics Urinary Bladder Neoplasms - metabolism |
| title | Activation of NFAT signal by p53-K120R mutant |
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