Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins
Targeted protein degradation is a powerful tool in determining the function of specific proteins or protein complexes. We fused nanobodies to SPOP, an adaptor protein of the Cullin-RING E3 ubiquitin ligase complex, resulting in rapid ubiquitination and subsequent proteasome-dependent degradation of...
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| Veröffentlicht in: | Scientific reports 2015-09, Vol.5 (1), p.14269-14269, Article 14269 |
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| creator | Ju Shin, Yeong Kyun Park, Seung Jung Jung, Yoo Na Kim, Ye Sung Kim, Ki Kyu Park, Ok Kwon, Seung-Hae Ho Jeon, Sung Trinh, Le A. Fraser, Scott E. Kee, Yun Joon Hwang, Byung |
| description | Targeted protein degradation is a powerful tool in determining the function of specific proteins or protein complexes. We fused nanobodies to SPOP, an adaptor protein of the Cullin-RING E3 ubiquitin ligase complex, resulting in rapid ubiquitination and subsequent proteasome-dependent degradation of specific nuclear proteins in mammalian cells and zebrafish embryos. This approach is easily modifiable, as substrate specificity is conferred by an antibody domain that can be adapted to target virtually any protein. |
| doi_str_mv | 10.1038/srep14269 |
| format | Article |
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We fused nanobodies to SPOP, an adaptor protein of the Cullin-RING E3 ubiquitin ligase complex, resulting in rapid ubiquitination and subsequent proteasome-dependent degradation of specific nuclear proteins in mammalian cells and zebrafish embryos. This approach is easily modifiable, as substrate specificity is conferred by an antibody domain that can be adapted to target virtually any protein.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep14269</identifier><identifier>PMID: 26373678</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/136/2086/1456 ; 631/1647/1511 ; 631/208/199 ; 631/337/474/2073 ; Animals ; Biodegradation ; Cullin ; Embryos ; Gene Expression ; Genes, Reporter ; HMGA2 Protein - genetics ; HMGA2 Protein - metabolism ; Humanities and Social Sciences ; Mammalian cells ; multidisciplinary ; Nanobodies ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; Proteasomes ; Protein Binding ; Proteins ; Proteolysis ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; RNA Interference ; Science ; Single-Domain Antibodies - immunology ; Single-Domain Antibodies - metabolism ; Substrate specificity ; Ubiquitin ; Ubiquitin-protein ligase ; Ubiquitin-Protein Ligase Complexes - immunology ; Ubiquitin-Protein Ligase Complexes - metabolism ; Ubiquitin-Protein Ligases - genetics ; Ubiquitin-Protein Ligases - immunology ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination ; Zebrafish</subject><ispartof>Scientific reports, 2015-09, Vol.5 (1), p.14269-14269, Article 14269</ispartof><rights>The Author(s) 2015</rights><rights>Copyright Nature Publishing Group Sep 2015</rights><rights>Copyright © 2015, Macmillan Publishers Limited 2015 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c574t-72d7c3235a6c43dcbd418aa47f4e78ef47d42b400c14ae92803d0b55751677053</citedby><cites>FETCH-LOGICAL-c574t-72d7c3235a6c43dcbd418aa47f4e78ef47d42b400c14ae92803d0b55751677053</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/PMC4571616/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4571616/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26373678$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ju Shin, Yeong</creatorcontrib><creatorcontrib>Kyun Park, Seung</creatorcontrib><creatorcontrib>Jung Jung, Yoo</creatorcontrib><creatorcontrib>Na Kim, Ye</creatorcontrib><creatorcontrib>Sung Kim, Ki</creatorcontrib><creatorcontrib>Kyu Park, Ok</creatorcontrib><creatorcontrib>Kwon, Seung-Hae</creatorcontrib><creatorcontrib>Ho Jeon, Sung</creatorcontrib><creatorcontrib>Trinh, Le A.</creatorcontrib><creatorcontrib>Fraser, Scott E.</creatorcontrib><creatorcontrib>Kee, Yun</creatorcontrib><creatorcontrib>Joon Hwang, Byung</creatorcontrib><title>Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Targeted protein degradation is a powerful tool in determining the function of specific proteins or protein complexes. We fused nanobodies to SPOP, an adaptor protein of the Cullin-RING E3 ubiquitin ligase complex, resulting in rapid ubiquitination and subsequent proteasome-dependent degradation of specific nuclear proteins in mammalian cells and zebrafish embryos. This approach is easily modifiable, as substrate specificity is conferred by an antibody domain that can be adapted to target virtually any protein.</description><subject>631/136/2086/1456</subject><subject>631/1647/1511</subject><subject>631/208/199</subject><subject>631/337/474/2073</subject><subject>Animals</subject><subject>Biodegradation</subject><subject>Cullin</subject><subject>Embryos</subject><subject>Gene Expression</subject><subject>Genes, Reporter</subject><subject>HMGA2 Protein - genetics</subject><subject>HMGA2 Protein - metabolism</subject><subject>Humanities and Social Sciences</subject><subject>Mammalian cells</subject><subject>multidisciplinary</subject><subject>Nanobodies</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Proteasomes</subject><subject>Protein Binding</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>RNA Interference</subject><subject>Science</subject><subject>Single-Domain Antibodies - immunology</subject><subject>Single-Domain Antibodies - metabolism</subject><subject>Substrate specificity</subject><subject>Ubiquitin</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitin-Protein Ligase Complexes - immunology</subject><subject>Ubiquitin-Protein Ligase Complexes - metabolism</subject><subject>Ubiquitin-Protein Ligases - genetics</subject><subject>Ubiquitin-Protein Ligases - immunology</subject><subject>Ubiquitin-Protein Ligases - metabolism</subject><subject>Ubiquitination</subject><subject>Zebrafish</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNplkU9LxDAQxYMoKroHv4AUvKhQzd-mvQiy6CqIXvQc0mS2RrpJTVrRb29ldVl1LjMwP9684SF0QPAZwaw8TxE6wmlRbaBdirnIKaN0c23eQZOUXvBYglacVNtohxZMskKWu2h2r32og_3Iex0b6MFmVywfavc6uN75rHWNTpCZsOhaeM8sNFFbSJkfTAs6Zl0MPTif9tHWXLcJJt99Dz1dXz1Ob_K7h9nt9PIuN0LyPpfUSsMoE7ownFlTW05Krbmcc5AlzLm0nNYcY0O4hoqWmFlcCyEFKaTEgu2hi6VuN9QLsAZ8H3WruugWOn6ooJ36vfHuWTXhTXEhSUGKUeD4WyCG1wFSrxYuGWhb7SEMSRFJmGCYlmxEj_6gL2GIfnxPkbKqJBOYfTk6WVImhjSGMV-ZIVh9JaRWCY3s4br7FfmTxwicLoE0rnwDce3kP7VP6eGaJA</recordid><startdate>20150916</startdate><enddate>20150916</enddate><creator>Ju Shin, Yeong</creator><creator>Kyun Park, Seung</creator><creator>Jung Jung, Yoo</creator><creator>Na Kim, Ye</creator><creator>Sung Kim, Ki</creator><creator>Kyu Park, Ok</creator><creator>Kwon, Seung-Hae</creator><creator>Ho Jeon, Sung</creator><creator>Trinh, Le A.</creator><creator>Fraser, Scott E.</creator><creator>Kee, Yun</creator><creator>Joon Hwang, Byung</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20150916</creationdate><title>Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins</title><author>Ju Shin, Yeong ; Kyun Park, Seung ; Jung Jung, Yoo ; Na Kim, Ye ; Sung Kim, Ki ; Kyu Park, Ok ; Kwon, Seung-Hae ; Ho Jeon, Sung ; Trinh, Le A. ; Fraser, Scott E. ; Kee, Yun ; Joon Hwang, Byung</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c574t-72d7c3235a6c43dcbd418aa47f4e78ef47d42b400c14ae92803d0b55751677053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>631/136/2086/1456</topic><topic>631/1647/1511</topic><topic>631/208/199</topic><topic>631/337/474/2073</topic><topic>Animals</topic><topic>Biodegradation</topic><topic>Cullin</topic><topic>Embryos</topic><topic>Gene Expression</topic><topic>Genes, Reporter</topic><topic>HMGA2 Protein - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ju Shin, Yeong</au><au>Kyun Park, Seung</au><au>Jung Jung, Yoo</au><au>Na Kim, Ye</au><au>Sung Kim, Ki</au><au>Kyu Park, Ok</au><au>Kwon, Seung-Hae</au><au>Ho Jeon, Sung</au><au>Trinh, Le A.</au><au>Fraser, Scott E.</au><au>Kee, Yun</au><au>Joon Hwang, Byung</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2015-09-16</date><risdate>2015</risdate><volume>5</volume><issue>1</issue><spage>14269</spage><epage>14269</epage><pages>14269-14269</pages><artnum>14269</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Targeted protein degradation is a powerful tool in determining the function of specific proteins or protein complexes. We fused nanobodies to SPOP, an adaptor protein of the Cullin-RING E3 ubiquitin ligase complex, resulting in rapid ubiquitination and subsequent proteasome-dependent degradation of specific nuclear proteins in mammalian cells and zebrafish embryos. This approach is easily modifiable, as substrate specificity is conferred by an antibody domain that can be adapted to target virtually any protein.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>26373678</pmid><doi>10.1038/srep14269</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/136/2086/1456 631/1647/1511 631/208/199 631/337/474/2073 Animals Biodegradation Cullin Embryos Gene Expression Genes, Reporter HMGA2 Protein - genetics HMGA2 Protein - metabolism Humanities and Social Sciences Mammalian cells multidisciplinary Nanobodies Nuclear Proteins - genetics Nuclear Proteins - metabolism Proteasomes Protein Binding Proteins Proteolysis Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - metabolism RNA Interference Science Single-Domain Antibodies - immunology Single-Domain Antibodies - metabolism Substrate specificity Ubiquitin Ubiquitin-protein ligase Ubiquitin-Protein Ligase Complexes - immunology Ubiquitin-Protein Ligase Complexes - metabolism Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - immunology Ubiquitin-Protein Ligases - metabolism Ubiquitination Zebrafish |
| title | Nanobody-targeted E3-ubiquitin ligase complex degrades nuclear proteins |
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