Regulation of TIP60 by ATF2 Modulates ATM Activation
TIP60 (HTATIP) is a histone acetyltransferase (HAT) whose function is critical in regulating ataxia-telangiectasia mutated (ATM) activation, gene expression, and chromatin acetylation in DNA repair. Here we show that under non-stressed conditions, activating transcription factor-2 (ATF2) in cooperat...
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| Veröffentlicht in: | The Journal of biological chemistry 2008-06, Vol.283 (25), p.17605-17614 |
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| creator | Bhoumik, Anindita Singha, Netai O'Connell, Matthew J. Ronai, Ze'ev A. |
| description | TIP60 (HTATIP) is a histone acetyltransferase (HAT) whose function is critical in regulating ataxia-telangiectasia mutated (ATM) activation, gene expression, and chromatin acetylation in DNA repair. Here we show that under non-stressed conditions, activating transcription factor-2 (ATF2) in cooperation with Cul3 ubiquitin ligase promotes degradation of TIP60, thereby attenuating its HAT activity. Inhibiting either ATF2 or Cul3 expression by small interfering RNA stabilizes the TIP60 protein. ATF2 association with TIP60 on chromatin is decreased following exposure to ionizing radiation (IR), resulting in enhanced TIP60 stability and activity. We also identified a panel of melanoma and prostate cancer cell lines whose ATF2 expression is inversely correlated with TIP60 levels and ATM activation after IR. Inhibition of ATF2 expression in these lines restored TIP60 protein levels and both basal and IR-induced levels of ATM activity. Our study provides novel insight into regulation of ATM activation by ATF2-dependent control of TIP60 stability and activity. |
| doi_str_mv | 10.1074/jbc.M802030200 |
| format | Article |
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Here we show that under non-stressed conditions, activating transcription factor-2 (ATF2) in cooperation with Cul3 ubiquitin ligase promotes degradation of TIP60, thereby attenuating its HAT activity. Inhibiting either ATF2 or Cul3 expression by small interfering RNA stabilizes the TIP60 protein. ATF2 association with TIP60 on chromatin is decreased following exposure to ionizing radiation (IR), resulting in enhanced TIP60 stability and activity. We also identified a panel of melanoma and prostate cancer cell lines whose ATF2 expression is inversely correlated with TIP60 levels and ATM activation after IR. Inhibition of ATF2 expression in these lines restored TIP60 protein levels and both basal and IR-induced levels of ATM activity. 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Our study provides novel insight into regulation of ATM activation by ATF2-dependent control of TIP60 stability and activity.</description><subject>Activating Transcription Factor 2 - metabolism</subject><subject>Ataxia Telangiectasia Mutated Proteins</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Line, Tumor</subject><subject>Chromatin - metabolism</subject><subject>Cullin Proteins - metabolism</subject><subject>DNA Damage</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Gene Expression Regulation</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>HeLa Cells</subject><subject>Histone Acetyltransferases - chemistry</subject><subject>Histone Acetyltransferases - metabolism</subject><subject>Humans</subject><subject>Lysine Acetyltransferase 5</subject><subject>Models, Biological</subject><subject>Models, Genetic</subject><subject>Protein Binding</subject><subject>Protein Synthesis, Post-Translational Modification, and Degradation</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>RNA Interference</subject><subject>Tumor Suppressor Proteins - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc-LEzEUx4Mobq1ePeocxNvUl1-T5CKUxdWFLYp2wVtIMpk2y3Sym0wr-9-bOsXVg_ggPB7v8758wxehlxgWGAR7d2PdYiWBAC0PHqEZBklryvH3x2gGQHCtCJdn6FnON1CKKfwUnWFJlZCSzRD76jf73owhDlXsqvXllwYqe18t1xekWsX2uPO5jKtq6cZw-EU-R08602f_4tTn6Priw_r8U331-ePl-fKqdpzgsXbKEMoMlZJS1_nWNo2iBCTrCJhGWMMlY5YLK4TilhglnaOd5bTBnSUc6By9n3Rv93bnW-eHMZle36awM-leRxP035shbPUmHjRhRNBSc_T2JJDi3d7nUe9Cdr7vzeDjPutGEQy8Ef8FCQipGD-Ciwl0KeacfPfbDQZ9TESXRPRDIuXg1Z9_eMBPERTgzQRsw2b7IySvbYhu63eaSKoJ11g0wAv2esI6E7XZpJD19TcCmAIo4IIdrcmJ8CWSQ_BJZxf84HxbRN2o2xj-ZfIn0zSsaw</recordid><startdate>20080620</startdate><enddate>20080620</enddate><creator>Bhoumik, Anindita</creator><creator>Singha, Netai</creator><creator>O'Connell, Matthew J.</creator><creator>Ronai, Ze'ev A.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080620</creationdate><title>Regulation of TIP60 by ATF2 Modulates ATM Activation</title><author>Bhoumik, Anindita ; 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| subjects | Activating Transcription Factor 2 - metabolism Ataxia Telangiectasia Mutated Proteins Cell Cycle Proteins - metabolism Cell Line, Tumor Chromatin - metabolism Cullin Proteins - metabolism DNA Damage DNA-Binding Proteins - metabolism Gene Expression Regulation Gene Expression Regulation, Neoplastic HeLa Cells Histone Acetyltransferases - chemistry Histone Acetyltransferases - metabolism Humans Lysine Acetyltransferase 5 Models, Biological Models, Genetic Protein Binding Protein Synthesis, Post-Translational Modification, and Degradation Protein-Serine-Threonine Kinases - metabolism RNA Interference Tumor Suppressor Proteins - metabolism |
| title | Regulation of TIP60 by ATF2 Modulates ATM Activation |
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