RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation
The PTEN tumor suppressor is a lipid phosphatase that has a central role in regulating the phosphatidylinositol-3- kinase （PI3K） signal transduction cascade. Nevertheless, the mechanism by which the PTEN activity is regulated in cells needs further elucidation. Although previous studies have shown t...
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| Veröffentlicht in: | Cell research 2013-04, Vol.23 (4), p.552-564 |
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| creator | Lee, James T Shan, Jing Zhong, Jiayun Li, Muyang Zhou, Brenda Zhou, Amanda Parsons, Ramon Gu, Wei |
| description | The PTEN tumor suppressor is a lipid phosphatase that has a central role in regulating the phosphatidylinositol-3- kinase （PI3K） signal transduction cascade. Nevertheless, the mechanism by which the PTEN activity is regulated in cells needs further elucidation. Although previous studies have shown that ubiquitination of PTEN can modulate its stability and subcellular localization, the role of ubiquitination in the most critical aspect of PTEN function, its phos- phatase activity, has not been fully addressed. Here, we identify a novel E3 ubiquitin ligase of PTEN, Ret finger pro- tein （RFP）, that is able to promote atypical polyubiquitinations of PTEN. These ubiquitinations do not lead to PTEN instability or relocalization, but rather significantly inhibit PTEN phosphatase activity and therefore modulate its ability to regulate the PI3K signal transduction cascade. Indeed, RFP overexpression relieves PTEN-mediated inhibi- tory effects on AKT activation; in contrast, RNAi-mediated knockdown of endogenous RFP enhances the ability of PTEN to suppress AKT activation. Moreover, RFP-mediated ubiquitination of PTEN inhibits PTEN-dependent ac- tivation of TRAIL expression and also suppresses its ability to induce apoptosis. Our findings demonstrate a crucial role of RFP-mediated ubiquitination in controlling PTEN activity. |
| doi_str_mv | 10.1038/cr.2013.27 |
| format | Article |
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Nevertheless, the mechanism by which the PTEN activity is regulated in cells needs further elucidation. Although previous studies have shown that ubiquitination of PTEN can modulate its stability and subcellular localization, the role of ubiquitination in the most critical aspect of PTEN function, its phos- phatase activity, has not been fully addressed. Here, we identify a novel E3 ubiquitin ligase of PTEN, Ret finger pro- tein （RFP）, that is able to promote atypical polyubiquitinations of PTEN. These ubiquitinations do not lead to PTEN instability or relocalization, but rather significantly inhibit PTEN phosphatase activity and therefore modulate its ability to regulate the PI3K signal transduction cascade. Indeed, RFP overexpression relieves PTEN-mediated inhibi- tory effects on AKT activation; in contrast, RNAi-mediated knockdown of endogenous RFP enhances the ability of PTEN to suppress AKT activation. Moreover, RFP-mediated ubiquitination of PTEN inhibits PTEN-dependent ac- tivation of TRAIL expression and also suppresses its ability to induce apoptosis. Our findings demonstrate a crucial role of RFP-mediated ubiquitination in controlling PTEN activity.</description><identifier>ISSN: 1001-0602</identifier><identifier>EISSN: 1748-7838</identifier><identifier>DOI: 10.1038/cr.2013.27</identifier><identifier>PMID: 23419514</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/45/612/645 ; 631/67/581 ; 631/80/458/1733 ; 631/80/86 ; AKT ; Apoptosis - genetics ; Biomedical and Life Sciences ; Cell Biology ; Cell Line, Tumor ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Gene Expression Regulation ; Humans ; Life Sciences ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Original ; original-article ; Phosphatidylinositol 3-Kinases - genetics ; Phosphatidylinositol 3-Kinases - metabolism ; Proto-Oncogene Proteins c-akt - genetics ; Proto-Oncogene Proteins c-akt - metabolism ; PTEN ; PTEN Phosphohydrolase - genetics ; PTEN Phosphohydrolase - metabolism ; RNA, Small Interfering - genetics ; Signal Transduction ; TNF-Related Apoptosis-Inducing Ligand - genetics ; TNF-Related Apoptosis-Inducing Ligand - metabolism ; Ubiquitination ; 亚细胞定位 ; 化调 ; 基因介导 ; 泛素化 ; 活化 ; 磷脂酰肌醇-3</subject><ispartof>Cell research, 2013-04, Vol.23 (4), p.552-564</ispartof><rights>Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences 2013</rights><rights>Copyright Nature Publishing Group Apr 2013</rights><rights>Copyright © 2013 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences 2013 Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c534t-dca3488b0e62081cf04b75537dd673f3ec553793382c112f75114357194f439a3</citedby><cites>FETCH-LOGICAL-c534t-dca3488b0e62081cf04b75537dd673f3ec553793382c112f75114357194f439a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://image.cqvip.com/vip1000/qk/85240X/85240X.jpg</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3616435/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3616435/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,41488,42557,51319,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23419514$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lee, James T</creatorcontrib><creatorcontrib>Shan, Jing</creatorcontrib><creatorcontrib>Zhong, Jiayun</creatorcontrib><creatorcontrib>Li, Muyang</creatorcontrib><creatorcontrib>Zhou, Brenda</creatorcontrib><creatorcontrib>Zhou, Amanda</creatorcontrib><creatorcontrib>Parsons, Ramon</creatorcontrib><creatorcontrib>Gu, Wei</creatorcontrib><title>RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation</title><title>Cell research</title><addtitle>Cell Res</addtitle><addtitle>Cell Research</addtitle><description>The PTEN tumor suppressor is a lipid phosphatase that has a central role in regulating the phosphatidylinositol-3- kinase （PI3K） signal transduction cascade. Nevertheless, the mechanism by which the PTEN activity is regulated in cells needs further elucidation. Although previous studies have shown that ubiquitination of PTEN can modulate its stability and subcellular localization, the role of ubiquitination in the most critical aspect of PTEN function, its phos- phatase activity, has not been fully addressed. Here, we identify a novel E3 ubiquitin ligase of PTEN, Ret finger pro- tein （RFP）, that is able to promote atypical polyubiquitinations of PTEN. These ubiquitinations do not lead to PTEN instability or relocalization, but rather significantly inhibit PTEN phosphatase activity and therefore modulate its ability to regulate the PI3K signal transduction cascade. Indeed, RFP overexpression relieves PTEN-mediated inhibi- tory effects on AKT activation; in contrast, RNAi-mediated knockdown of endogenous RFP enhances the ability of PTEN to suppress AKT activation. Moreover, RFP-mediated ubiquitination of PTEN inhibits PTEN-dependent ac- tivation of TRAIL expression and also suppresses its ability to induce apoptosis. Our findings demonstrate a crucial role of RFP-mediated ubiquitination in controlling PTEN activity.</description><subject>631/45/612/645</subject><subject>631/67/581</subject><subject>631/80/458/1733</subject><subject>631/80/86</subject><subject>AKT</subject><subject>Apoptosis - genetics</subject><subject>Biomedical and Life Sciences</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Gene Expression Regulation</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Original</subject><subject>original-article</subject><subject>Phosphatidylinositol 3-Kinases - genetics</subject><subject>Phosphatidylinositol 3-Kinases - metabolism</subject><subject>Proto-Oncogene Proteins c-akt - genetics</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>PTEN</subject><subject>PTEN Phosphohydrolase - genetics</subject><subject>PTEN Phosphohydrolase - metabolism</subject><subject>RNA, Small Interfering - genetics</subject><subject>Signal Transduction</subject><subject>TNF-Related Apoptosis-Inducing Ligand - genetics</subject><subject>TNF-Related Apoptosis-Inducing Ligand - metabolism</subject><subject>Ubiquitination</subject><subject>亚细胞定位</subject><subject>化调</subject><subject>基因介导</subject><subject>泛素化</subject><subject>活化</subject><subject>磷脂酰肌醇-3</subject><issn>1001-0602</issn><issn>1748-7838</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNptkV1LHDEUhkNpqdb2xh8gU7wpltnm5GOSuRFE1H5IK2V7HbKZZI3MTtwkI_jvzXS3iy29SsJ58pz3cBA6BDwDTOUnE2cEA50R8QLtg2CyFpLKl-WOMdS4wWQPvUnpDmPCGYfXaI9QBi0Hto--_ry8qVe28zrbrhoXfj367AedfRiq4Kqb-cX3ahW6sS9AqnxOlXXOmlyV-tm3eaVN9g-_8bfoldN9su-25wH6dXkxP_9cX_-4-nJ-dl0bTlmuO6Mpk3KBbUOwBOMwWwjOqei6RlBHrZkeLaWSGADiBAdglAtomWO01fQAnW689-OiJDd2yFH36j76lY6PKmiv_q4M_lYtw4OiDTTFVAQftoIY1qNNWa18Mrbv9WDDmBRQQgRpeSsKevwPehfGOJTxJgokcNGSQp1sKBNDStG6XRjAalqRMlFNK1JkUh49j79D_-ykAB83QCqlYWnjs57_073f9r4Nw3JdPuyMjDfFyBl9ArK0o3s</recordid><startdate>20130401</startdate><enddate>20130401</enddate><creator>Lee, James T</creator><creator>Shan, Jing</creator><creator>Zhong, Jiayun</creator><creator>Li, Muyang</creator><creator>Zhou, Brenda</creator><creator>Zhou, Amanda</creator><creator>Parsons, Ramon</creator><creator>Gu, Wei</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W94</scope><scope>WU4</scope><scope>~WA</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>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20130401</creationdate><title>RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation</title><author>Lee, James T ; Shan, Jing ; Zhong, Jiayun ; Li, Muyang ; Zhou, Brenda ; Zhou, Amanda ; Parsons, Ramon ; Gu, Wei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c534t-dca3488b0e62081cf04b75537dd673f3ec553793382c112f75114357194f439a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>631/45/612/645</topic><topic>631/67/581</topic><topic>631/80/458/1733</topic><topic>631/80/86</topic><topic>AKT</topic><topic>Apoptosis - genetics</topic><topic>Biomedical and Life Sciences</topic><topic>Cell Biology</topic><topic>Cell Line, Tumor</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Gene Expression Regulation</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Original</topic><topic>original-article</topic><topic>Phosphatidylinositol 3-Kinases - genetics</topic><topic>Phosphatidylinositol 3-Kinases - metabolism</topic><topic>Proto-Oncogene Proteins c-akt - genetics</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>PTEN</topic><topic>PTEN Phosphohydrolase - genetics</topic><topic>PTEN Phosphohydrolase - metabolism</topic><topic>RNA, Small Interfering - genetics</topic><topic>Signal Transduction</topic><topic>TNF-Related Apoptosis-Inducing Ligand - genetics</topic><topic>TNF-Related Apoptosis-Inducing Ligand - metabolism</topic><topic>Ubiquitination</topic><topic>亚细胞定位</topic><topic>化调</topic><topic>基因介导</topic><topic>泛素化</topic><topic>活化</topic><topic>磷脂酰肌醇-3</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, James T</creatorcontrib><creatorcontrib>Shan, Jing</creatorcontrib><creatorcontrib>Zhong, Jiayun</creatorcontrib><creatorcontrib>Li, Muyang</creatorcontrib><creatorcontrib>Zhou, Brenda</creatorcontrib><creatorcontrib>Zhou, Amanda</creatorcontrib><creatorcontrib>Parsons, Ramon</creatorcontrib><creatorcontrib>Gu, Wei</creatorcontrib><collection>中文科技期刊数据库</collection><collection>中文科技期刊数据库-CALIS站点</collection><collection>中文科技期刊数据库-7.0平台</collection><collection>中文科技期刊数据库-自然科学</collection><collection>中文科技期刊数据库-自然科学-生物科学</collection><collection>中文科技期刊数据库- 镜像站点</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, James T</au><au>Shan, Jing</au><au>Zhong, Jiayun</au><au>Li, Muyang</au><au>Zhou, Brenda</au><au>Zhou, Amanda</au><au>Parsons, Ramon</au><au>Gu, Wei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation</atitle><jtitle>Cell research</jtitle><stitle>Cell Res</stitle><addtitle>Cell Research</addtitle><date>2013-04-01</date><risdate>2013</risdate><volume>23</volume><issue>4</issue><spage>552</spage><epage>564</epage><pages>552-564</pages><issn>1001-0602</issn><eissn>1748-7838</eissn><abstract>The PTEN tumor suppressor is a lipid phosphatase that has a central role in regulating the phosphatidylinositol-3- kinase （PI3K） signal transduction cascade. Nevertheless, the mechanism by which the PTEN activity is regulated in cells needs further elucidation. Although previous studies have shown that ubiquitination of PTEN can modulate its stability and subcellular localization, the role of ubiquitination in the most critical aspect of PTEN function, its phos- phatase activity, has not been fully addressed. Here, we identify a novel E3 ubiquitin ligase of PTEN, Ret finger pro- tein （RFP）, that is able to promote atypical polyubiquitinations of PTEN. These ubiquitinations do not lead to PTEN instability or relocalization, but rather significantly inhibit PTEN phosphatase activity and therefore modulate its ability to regulate the PI3K signal transduction cascade. Indeed, RFP overexpression relieves PTEN-mediated inhibi- tory effects on AKT activation; in contrast, RNAi-mediated knockdown of endogenous RFP enhances the ability of PTEN to suppress AKT activation. Moreover, RFP-mediated ubiquitination of PTEN inhibits PTEN-dependent ac- tivation of TRAIL expression and also suppresses its ability to induce apoptosis. Our findings demonstrate a crucial role of RFP-mediated ubiquitination in controlling PTEN activity.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>23419514</pmid><doi>10.1038/cr.2013.27</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/45/612/645 631/67/581 631/80/458/1733 631/80/86 AKT Apoptosis - genetics Biomedical and Life Sciences Cell Biology Cell Line, Tumor DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Gene Expression Regulation Humans Life Sciences Nuclear Proteins - genetics Nuclear Proteins - metabolism Original original-article Phosphatidylinositol 3-Kinases - genetics Phosphatidylinositol 3-Kinases - metabolism Proto-Oncogene Proteins c-akt - genetics Proto-Oncogene Proteins c-akt - metabolism PTEN PTEN Phosphohydrolase - genetics PTEN Phosphohydrolase - metabolism RNA, Small Interfering - genetics Signal Transduction TNF-Related Apoptosis-Inducing Ligand - genetics TNF-Related Apoptosis-Inducing Ligand - metabolism Ubiquitination 亚细胞定位 化调 基因介导 泛素化 活化 磷脂酰肌醇-3 |
| title | RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation |
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