SUMOylation regulates AKT1 activity
Serine threonine kinase AKT has a central role in the cell, controlling survival, proliferation, metabolism and angiogenesis. Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquiti...
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| Veröffentlicht in: | Oncogene 2015-03, Vol.34 (11), p.1442-1450 |
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| creator | de la Cruz-Herrera, C F Campagna, M Lang, V del Carmen González-Santamaría, J Marcos-Villar, L Rodríguez, M S Vidal, A Collado, M Rivas, C |
| description | Serine threonine kinase AKT has a central role in the cell, controlling survival, proliferation, metabolism and angiogenesis. Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquitin-like modifier (SUMO) protein. Interestingly, neither SUMO conjugation nor activation of SUMOylated AKT is regulated by the classical AKT targeting to the cell membrane or by the phosphoinositide 3-kinase pathway. We demonstrate that SUMO induces the activation of AKT, whereas, conversely, down-modulation of the SUMO machinery diminishes AKT activation and cell proliferation. Furthermore, an AKT SUMOylation mutant shows reduced activation, and decreased anti-apoptotic and pro-tumoral activities in comparison with the wild-type protein. These results identify SUMO as a novel key regulator of AKT phosphorylation and activity. |
| doi_str_mv | 10.1038/onc.2014.48 |
| format | Article |
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Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquitin-like modifier (SUMO) protein. Interestingly, neither SUMO conjugation nor activation of SUMOylated AKT is regulated by the classical AKT targeting to the cell membrane or by the phosphoinositide 3-kinase pathway. We demonstrate that SUMO induces the activation of AKT, whereas, conversely, down-modulation of the SUMO machinery diminishes AKT activation and cell proliferation. Furthermore, an AKT SUMOylation mutant shows reduced activation, and decreased anti-apoptotic and pro-tumoral activities in comparison with the wild-type protein. These results identify SUMO as a novel key regulator of AKT phosphorylation and activity.</description><identifier>ISSN: 0950-9232</identifier><identifier>EISSN: 1476-5594</identifier><identifier>DOI: 10.1038/onc.2014.48</identifier><identifier>PMID: 24704831</identifier><identifier>CODEN: ONCNES</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>3T3 Cells ; 631/337/458/538 ; 631/67/1059/153 ; 631/80/86 ; AKT protein ; AKT1 protein ; Analysis ; Angiogenesis ; Animals ; Apoptosis ; Apoptosis - genetics ; Cancer ; Cell activation ; Cell Biology ; Cell Line, Tumor ; Cell membranes ; Cell Proliferation ; Cell survival ; Chlorocebus aethiops ; COS Cells ; Enzyme Activation ; Female ; Genetic aspects ; HEK293 Cells ; HeLa Cells ; Human Genetics ; Humans ; Internal Medicine ; Kinases ; MCF-7 Cells ; Medicine ; Medicine & Public Health ; Metabolism ; Mice ; Mutants ; Mutation ; Neoplasms - pathology ; Oncology ; original-article ; Phosphoinositide-3 Kinase Inhibitors ; Phosphorylation ; Physiological aspects ; Post-translation ; Protein kinases ; Protein-serine/threonine kinase ; Proto-Oncogene Proteins c-akt - antagonists & inhibitors ; Proto-Oncogene Proteins c-akt - genetics ; Proto-Oncogene Proteins c-akt - metabolism ; Signal Transduction ; Small Ubiquitin-Related Modifier Proteins - metabolism ; SUMO protein ; SUMO-1 Protein - metabolism ; Sumoylation - genetics ; Sumoylation - physiology ; Ubiquitin ; Ubiquitins - metabolism</subject><ispartof>Oncogene, 2015-03, Vol.34 (11), p.1442-1450</ispartof><rights>Macmillan Publishers Limited 2015</rights><rights>COPYRIGHT 2015 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Mar 12, 2015</rights><rights>Macmillan Publishers Limited 2015.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c589t-b0323e7637a7ac9acbd96302d83ad5bd28f83401d244a69264980c5a931a6ff23</citedby><cites>FETCH-LOGICAL-c589t-b0323e7637a7ac9acbd96302d83ad5bd28f83401d244a69264980c5a931a6ff23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24704831$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>de la Cruz-Herrera, C F</creatorcontrib><creatorcontrib>Campagna, M</creatorcontrib><creatorcontrib>Lang, V</creatorcontrib><creatorcontrib>del Carmen González-Santamaría, J</creatorcontrib><creatorcontrib>Marcos-Villar, L</creatorcontrib><creatorcontrib>Rodríguez, M S</creatorcontrib><creatorcontrib>Vidal, A</creatorcontrib><creatorcontrib>Collado, M</creatorcontrib><creatorcontrib>Rivas, C</creatorcontrib><title>SUMOylation regulates AKT1 activity</title><title>Oncogene</title><addtitle>Oncogene</addtitle><addtitle>Oncogene</addtitle><description>Serine threonine kinase AKT has a central role in the cell, controlling survival, proliferation, metabolism and angiogenesis. Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquitin-like modifier (SUMO) protein. Interestingly, neither SUMO conjugation nor activation of SUMOylated AKT is regulated by the classical AKT targeting to the cell membrane or by the phosphoinositide 3-kinase pathway. We demonstrate that SUMO induces the activation of AKT, whereas, conversely, down-modulation of the SUMO machinery diminishes AKT activation and cell proliferation. Furthermore, an AKT SUMOylation mutant shows reduced activation, and decreased anti-apoptotic and pro-tumoral activities in comparison with the wild-type protein. These results identify SUMO as a novel key regulator of AKT phosphorylation and activity.</description><subject>3T3 Cells</subject><subject>631/337/458/538</subject><subject>631/67/1059/153</subject><subject>631/80/86</subject><subject>AKT protein</subject><subject>AKT1 protein</subject><subject>Analysis</subject><subject>Angiogenesis</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Apoptosis - genetics</subject><subject>Cancer</subject><subject>Cell activation</subject><subject>Cell Biology</subject><subject>Cell Line, Tumor</subject><subject>Cell membranes</subject><subject>Cell Proliferation</subject><subject>Cell survival</subject><subject>Chlorocebus aethiops</subject><subject>COS Cells</subject><subject>Enzyme Activation</subject><subject>Female</subject><subject>Genetic aspects</subject><subject>HEK293 Cells</subject><subject>HeLa Cells</subject><subject>Human Genetics</subject><subject>Humans</subject><subject>Internal Medicine</subject><subject>Kinases</subject><subject>MCF-7 Cells</subject><subject>Medicine</subject><subject>Medicine & Public Health</subject><subject>Metabolism</subject><subject>Mice</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Neoplasms - pathology</subject><subject>Oncology</subject><subject>original-article</subject><subject>Phosphoinositide-3 Kinase Inhibitors</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Post-translation</subject><subject>Protein kinases</subject><subject>Protein-serine/threonine kinase</subject><subject>Proto-Oncogene Proteins c-akt - antagonists & inhibitors</subject><subject>Proto-Oncogene Proteins c-akt - genetics</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>Signal Transduction</subject><subject>Small Ubiquitin-Related Modifier Proteins - metabolism</subject><subject>SUMO protein</subject><subject>SUMO-1 Protein - metabolism</subject><subject>Sumoylation - genetics</subject><subject>Sumoylation - physiology</subject><subject>Ubiquitin</subject><subject>Ubiquitins - metabolism</subject><issn>0950-9232</issn><issn>1476-5594</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkc9LwzAUx4MoOqcn7zLYRdDOl7w0TY5D_IUTD7pzyNJ0VLp2Jq2w_96MqaiISA4Jyed9Xh5fQo4ojCigPG9qO2JA-YjLLdKjPBNJmiq-TXqgUkgUQ7ZH9kN4BoBMAdsle4xnwCXSHhk-Tu8fVpVpy6YeeDfv4tGFwfjuiQ6MbcvXsl0dkJ3CVMEdvu99Mr26fLq4SSYP17cX40liU6naZAbI0GUCM5MZq4yd5UogsFyiydNZzmQhkQPNGedGKCa4kmBTo5AaURQM--Rk41365qVzodWLMlhXVaZ2TRc0FUKyDCBa_4GiSDNEFdHhD_S56XwdB9EMkQoqgYq_qOhiXFCEL665qZwu66JpvbHr1nrMQUSPVBCp0S9UXLlblLapXVHG-28Fp5sC65sQvCv00pcL41eagl5nrGPGep2xjqn1yfH7V7vZwuWf7EeoETjbACE-1XPnv8zyi-8Nh3Op1Q</recordid><startdate>20150312</startdate><enddate>20150312</enddate><creator>de la Cruz-Herrera, C F</creator><creator>Campagna, M</creator><creator>Lang, V</creator><creator>del Carmen González-Santamaría, J</creator><creator>Marcos-Villar, L</creator><creator>Rodríguez, M S</creator><creator>Vidal, A</creator><creator>Collado, M</creator><creator>Rivas, C</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><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>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</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>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20150312</creationdate><title>SUMOylation regulates AKT1 activity</title><author>de la Cruz-Herrera, C F ; Campagna, M ; Lang, V ; del Carmen González-Santamaría, J ; Marcos-Villar, L ; Rodríguez, M S ; Vidal, A ; Collado, M ; Rivas, C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c589t-b0323e7637a7ac9acbd96302d83ad5bd28f83401d244a69264980c5a931a6ff23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>3T3 Cells</topic><topic>631/337/458/538</topic><topic>631/67/1059/153</topic><topic>631/80/86</topic><topic>AKT protein</topic><topic>AKT1 protein</topic><topic>Analysis</topic><topic>Angiogenesis</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Apoptosis - genetics</topic><topic>Cancer</topic><topic>Cell activation</topic><topic>Cell Biology</topic><topic>Cell Line, Tumor</topic><topic>Cell membranes</topic><topic>Cell Proliferation</topic><topic>Cell survival</topic><topic>Chlorocebus aethiops</topic><topic>COS Cells</topic><topic>Enzyme Activation</topic><topic>Female</topic><topic>Genetic aspects</topic><topic>HEK293 Cells</topic><topic>HeLa Cells</topic><topic>Human Genetics</topic><topic>Humans</topic><topic>Internal Medicine</topic><topic>Kinases</topic><topic>MCF-7 Cells</topic><topic>Medicine</topic><topic>Medicine & Public Health</topic><topic>Metabolism</topic><topic>Mice</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Neoplasms - pathology</topic><topic>Oncology</topic><topic>original-article</topic><topic>Phosphoinositide-3 Kinase Inhibitors</topic><topic>Phosphorylation</topic><topic>Physiological aspects</topic><topic>Post-translation</topic><topic>Protein kinases</topic><topic>Protein-serine/threonine kinase</topic><topic>Proto-Oncogene Proteins c-akt - 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Academic</collection><jtitle>Oncogene</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>de la Cruz-Herrera, C F</au><au>Campagna, M</au><au>Lang, V</au><au>del Carmen González-Santamaría, J</au><au>Marcos-Villar, L</au><au>Rodríguez, M S</au><au>Vidal, A</au><au>Collado, M</au><au>Rivas, C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>SUMOylation regulates AKT1 activity</atitle><jtitle>Oncogene</jtitle><stitle>Oncogene</stitle><addtitle>Oncogene</addtitle><date>2015-03-12</date><risdate>2015</risdate><volume>34</volume><issue>11</issue><spage>1442</spage><epage>1450</epage><pages>1442-1450</pages><issn>0950-9232</issn><eissn>1476-5594</eissn><coden>ONCNES</coden><abstract>Serine threonine kinase AKT has a central role in the cell, controlling survival, proliferation, metabolism and angiogenesis. Deregulation of its activity underlies a wide range of pathological situations, including cancer. Here we show that AKT is post-translationally modified by the small ubiquitin-like modifier (SUMO) protein. Interestingly, neither SUMO conjugation nor activation of SUMOylated AKT is regulated by the classical AKT targeting to the cell membrane or by the phosphoinositide 3-kinase pathway. We demonstrate that SUMO induces the activation of AKT, whereas, conversely, down-modulation of the SUMO machinery diminishes AKT activation and cell proliferation. Furthermore, an AKT SUMOylation mutant shows reduced activation, and decreased anti-apoptotic and pro-tumoral activities in comparison with the wild-type protein. These results identify SUMO as a novel key regulator of AKT phosphorylation and activity.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>24704831</pmid><doi>10.1038/onc.2014.48</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 3T3 Cells 631/337/458/538 631/67/1059/153 631/80/86 AKT protein AKT1 protein Analysis Angiogenesis Animals Apoptosis Apoptosis - genetics Cancer Cell activation Cell Biology Cell Line, Tumor Cell membranes Cell Proliferation Cell survival Chlorocebus aethiops COS Cells Enzyme Activation Female Genetic aspects HEK293 Cells HeLa Cells Human Genetics Humans Internal Medicine Kinases MCF-7 Cells Medicine Medicine & Public Health Metabolism Mice Mutants Mutation Neoplasms - pathology Oncology original-article Phosphoinositide-3 Kinase Inhibitors Phosphorylation Physiological aspects Post-translation Protein kinases Protein-serine/threonine kinase Proto-Oncogene Proteins c-akt - antagonists & inhibitors Proto-Oncogene Proteins c-akt - genetics Proto-Oncogene Proteins c-akt - metabolism Signal Transduction Small Ubiquitin-Related Modifier Proteins - metabolism SUMO protein SUMO-1 Protein - metabolism Sumoylation - genetics Sumoylation - physiology Ubiquitin Ubiquitins - metabolism |
| title | SUMOylation regulates AKT1 activity |
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