OTUD5 regulates p53 stability by deubiquitinating p53
The p53 tumour suppressor protein is a transcription factor that prevents oncogenic progression by activating the expression of apoptosis and cell-cycle arrest genes in stressed cells. The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by its negative regulat...
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| Veröffentlicht in: | PloS one 2013-10, Vol.8 (10), p.e77682 |
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| creator | Luo, Judong Lu, Zhonghua Lu, Xujing Chen, Ling Cao, Jianping Zhang, Shuyu Ling, Yang Zhou, Xifa |
| description | The p53 tumour suppressor protein is a transcription factor that prevents oncogenic progression by activating the expression of apoptosis and cell-cycle arrest genes in stressed cells. The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by its negative regulators ubiquitin ligase MDM2.
In this study, we have identified OTUD5 as a DUB that interacts with and deubiquitinates p53. OTUD5 forms a direct complex with p53 and controls level of ubiquitination. The function of OTUD5 is required to allow the rapid activation of p53-dependent transcription and a p53-dependent apoptosis in response to DNA damage stress.
As a novel deubiquitinating enzyme for p53, OTUD5 is required for the stabilization and the activation of a p53 response. |
| doi_str_mv | 10.1371/journal.pone.0077682 |
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In this study, we have identified OTUD5 as a DUB that interacts with and deubiquitinates p53. OTUD5 forms a direct complex with p53 and controls level of ubiquitination. The function of OTUD5 is required to allow the rapid activation of p53-dependent transcription and a p53-dependent apoptosis in response to DNA damage stress.
As a novel deubiquitinating enzyme for p53, OTUD5 is required for the stabilization and the activation of a p53 response.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0077682</identifier><identifier>PMID: 24143256</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Apoptosis ; Bone marrow ; Cell cycle ; Cell Line ; Deoxyribonucleic acid ; DNA ; DNA Damage ; Endopeptidases - metabolism ; Enzymes ; Gene expression ; Humans ; Laboratories ; Ligases ; MDM2 protein ; Medical screening ; Medicine ; Oxidative stress ; p53 Protein ; Protein Stability ; Proteins ; Radiation therapy ; Regulation ; Stability ; Transcription (Genetics) ; Transcription activation ; Tumor proteins ; Tumor Suppressor Protein p53 - chemistry ; Tumor Suppressor Protein p53 - metabolism ; Tumorigenesis ; Tumors ; Ubiquitin ; Ubiquitin-protein ligase ; Ubiquitin-Specific Proteases - metabolism ; Ubiquitination</subject><ispartof>PloS one, 2013-10, Vol.8 (10), p.e77682</ispartof><rights>COPYRIGHT 2013 Public Library of Science</rights><rights>2013 Luo et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2013 Luo et al 2013 Luo et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6072-4cf340bcf6adb5c106228d34c3a2c07c814aba9f71a56f39facbe86d2dddcbf33</citedby><cites>FETCH-LOGICAL-c6072-4cf340bcf6adb5c106228d34c3a2c07c814aba9f71a56f39facbe86d2dddcbf33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3797110/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3797110/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79343,79344</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24143256$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Luo, Judong</creatorcontrib><creatorcontrib>Lu, Zhonghua</creatorcontrib><creatorcontrib>Lu, Xujing</creatorcontrib><creatorcontrib>Chen, Ling</creatorcontrib><creatorcontrib>Cao, Jianping</creatorcontrib><creatorcontrib>Zhang, Shuyu</creatorcontrib><creatorcontrib>Ling, Yang</creatorcontrib><creatorcontrib>Zhou, Xifa</creatorcontrib><title>OTUD5 regulates p53 stability by deubiquitinating p53</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The p53 tumour suppressor protein is a transcription factor that prevents oncogenic progression by activating the expression of apoptosis and cell-cycle arrest genes in stressed cells. The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by its negative regulators ubiquitin ligase MDM2.
In this study, we have identified OTUD5 as a DUB that interacts with and deubiquitinates p53. OTUD5 forms a direct complex with p53 and controls level of ubiquitination. The function of OTUD5 is required to allow the rapid activation of p53-dependent transcription and a p53-dependent apoptosis in response to DNA damage stress.
As a novel deubiquitinating enzyme for p53, OTUD5 is required for the stabilization and the activation of a p53 response.</description><subject>Apoptosis</subject><subject>Bone marrow</subject><subject>Cell cycle</subject><subject>Cell Line</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA Damage</subject><subject>Endopeptidases - metabolism</subject><subject>Enzymes</subject><subject>Gene expression</subject><subject>Humans</subject><subject>Laboratories</subject><subject>Ligases</subject><subject>MDM2 protein</subject><subject>Medical screening</subject><subject>Medicine</subject><subject>Oxidative stress</subject><subject>p53 Protein</subject><subject>Protein Stability</subject><subject>Proteins</subject><subject>Radiation therapy</subject><subject>Regulation</subject><subject>Stability</subject><subject>Transcription (Genetics)</subject><subject>Transcription activation</subject><subject>Tumor proteins</subject><subject>Tumor Suppressor Protein p53 - chemistry</subject><subject>Tumor Suppressor Protein p53 - metabolism</subject><subject>Tumorigenesis</subject><subject>Tumors</subject><subject>Ubiquitin</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitin-Specific Proteases - metabolism</subject><subject>Ubiquitination</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNkmuLEzEUhgdR3HX1H4gWBMEPrblOMl-EZb0VFgq669dwJpdpynTSnWTE_ntTO7t0QEFCSEie9z0nJ6coXmK0wFTg95sw9B20i13o7AIhIUpJHhXnuKJkXhJEH5_sz4pnMW4Q4lSW5dPijDDMKOHlecFXN7cf-ay3zdBCsnG243QWE9S-9Wk_q_czY4fa3w0--Q7ybA7E8-KJgzbaF-N6Udx-_nRz9XV-vfqyvLq8nusSCTJn2lGGau1KMDXXGJWESEOZpkA0ElpiBjVUTmDgpaOVA11bWRpijNG1o_SieH303bUhqvHFUWHGCK4IIyQTyyNhAmzUrvdb6PcqgFd_DkLfKOiT161ViHHsgNTEWWBMV1K6HJNJcIwIY2X2-jBGG-qtNdp2qYd2Yjq96fxaNeGnoqISGKNs8GY06MPdYGP6R8oj1UDOyncuZDO99VGrSyYk4ZILnqnFX6g8jN16nf_c-Xw-EbybCDKT7K_UwBCjWn7_9v_s6seUfXvCri20aR1DOyQfujgF2RHUfYixt-6hchipQ8veV0MdWlaNLZtlr06r_iC671H6GxKM5aw</recordid><startdate>20131015</startdate><enddate>20131015</enddate><creator>Luo, Judong</creator><creator>Lu, Zhonghua</creator><creator>Lu, Xujing</creator><creator>Chen, Ling</creator><creator>Cao, Jianping</creator><creator>Zhang, Shuyu</creator><creator>Ling, Yang</creator><creator>Zhou, Xifa</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</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>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20131015</creationdate><title>OTUD5 regulates p53 stability by deubiquitinating p53</title><author>Luo, Judong ; Lu, Zhonghua ; Lu, Xujing ; Chen, Ling ; Cao, Jianping ; Zhang, Shuyu ; Ling, Yang ; Zhou, Xifa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6072-4cf340bcf6adb5c106228d34c3a2c07c814aba9f71a56f39facbe86d2dddcbf33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Apoptosis</topic><topic>Bone marrow</topic><topic>Cell cycle</topic><topic>Cell Line</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA Damage</topic><topic>Endopeptidases - metabolism</topic><topic>Enzymes</topic><topic>Gene expression</topic><topic>Humans</topic><topic>Laboratories</topic><topic>Ligases</topic><topic>MDM2 protein</topic><topic>Medical screening</topic><topic>Medicine</topic><topic>Oxidative stress</topic><topic>p53 Protein</topic><topic>Protein Stability</topic><topic>Proteins</topic><topic>Radiation therapy</topic><topic>Regulation</topic><topic>Stability</topic><topic>Transcription (Genetics)</topic><topic>Transcription activation</topic><topic>Tumor proteins</topic><topic>Tumor Suppressor Protein p53 - chemistry</topic><topic>Tumor Suppressor Protein p53 - metabolism</topic><topic>Tumorigenesis</topic><topic>Tumors</topic><topic>Ubiquitin</topic><topic>Ubiquitin-protein ligase</topic><topic>Ubiquitin-Specific Proteases - metabolism</topic><topic>Ubiquitination</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Luo, Judong</creatorcontrib><creatorcontrib>Lu, Zhonghua</creatorcontrib><creatorcontrib>Lu, Xujing</creatorcontrib><creatorcontrib>Chen, Ling</creatorcontrib><creatorcontrib>Cao, Jianping</creatorcontrib><creatorcontrib>Zhang, Shuyu</creatorcontrib><creatorcontrib>Ling, Yang</creatorcontrib><creatorcontrib>Zhou, Xifa</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology 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>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</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>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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The stability of p53 is tightly regulated by ubiquitin-dependent degradation, driven mainly by its negative regulators ubiquitin ligase MDM2.
In this study, we have identified OTUD5 as a DUB that interacts with and deubiquitinates p53. OTUD5 forms a direct complex with p53 and controls level of ubiquitination. The function of OTUD5 is required to allow the rapid activation of p53-dependent transcription and a p53-dependent apoptosis in response to DNA damage stress.
As a novel deubiquitinating enzyme for p53, OTUD5 is required for the stabilization and the activation of a p53 response.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24143256</pmid><doi>10.1371/journal.pone.0077682</doi><tpages>e77682</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Apoptosis Bone marrow Cell cycle Cell Line Deoxyribonucleic acid DNA DNA Damage Endopeptidases - metabolism Enzymes Gene expression Humans Laboratories Ligases MDM2 protein Medical screening Medicine Oxidative stress p53 Protein Protein Stability Proteins Radiation therapy Regulation Stability Transcription (Genetics) Transcription activation Tumor proteins Tumor Suppressor Protein p53 - chemistry Tumor Suppressor Protein p53 - metabolism Tumorigenesis Tumors Ubiquitin Ubiquitin-protein ligase Ubiquitin-Specific Proteases - metabolism Ubiquitination |
| title | OTUD5 regulates p53 stability by deubiquitinating p53 |
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