Phosphorylation-dependent activity of the deubiquitinase DUBA
Protease phosphorylation has been reported to affect many signaling pathways connected to proteolytic activity, but the underlying mechanisms have not been clearly elucidated. Structural and biochemical analyses of the deubiquitinase DUBA reveal that phosphorylation is necessary for productive ubiqu...
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| Veröffentlicht in: | Nat. Struct. Mol. Biol 2012-02, Vol.19 (2), p.171-175 |
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| creator | Huang, Oscar W Ma, Xiaolei Yin, JianPing Flinders, Jeremy Maurer, Till Kayagaki, Nobuhiko Phung, Qui Bosanac, Ivan Arnott, David Dixit, Vishva M Hymowitz, Sarah G Starovasnik, Melissa A Cochran, Andrea G |
| description | Protease phosphorylation has been reported to affect many signaling pathways connected to proteolytic activity, but the underlying mechanisms have not been clearly elucidated. Structural and biochemical analyses of the deubiquitinase DUBA reveal that phosphorylation is necessary for productive ubiquitin substrate recognition and for enzyme activity.
Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of interactions involving the phosphate and the C-terminal tail of ubiquitin cause DUBA to fold around its substrate, revealing why phosphorylation is essential for deubiquitinase activity. Phosphoactivation of DUBA represents an unprecedented mode of protease regulation and a clear link between two major cellular signal transduction systems: phosphorylation and ubiquitin modification. |
| doi_str_mv | 10.1038/nsmb.2206 |
| format | Article |
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Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of interactions involving the phosphate and the C-terminal tail of ubiquitin cause DUBA to fold around its substrate, revealing why phosphorylation is essential for deubiquitinase activity. Phosphoactivation of DUBA represents an unprecedented mode of protease regulation and a clear link between two major cellular signal transduction systems: phosphorylation and ubiquitin modification.</description><identifier>ISSN: 1545-9993</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/nsmb.2206</identifier><identifier>PMID: 22245969</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/337/458/1733 ; 631/337/474/582 ; 631/45/535 ; Biochemistry ; Biological Microscopy ; Biomedical and Life Sciences ; Cellular biology ; Crystal structure ; Crystallography, X-Ray ; Endopeptidases - metabolism ; Genetic aspects ; Humans ; Life Sciences ; Membrane Biology ; Models, Molecular ; Phosphorylation ; Physiological aspects ; Proteases ; Protein Conformation ; Protein Processing, Post-Translational ; Protein Structure ; Proteins ; Serine - metabolism ; Signaling ; Substrates ; Ubiquitin ; Ubiquitin - metabolism</subject><ispartof>Nat. Struct. Mol. Biol, 2012-02, Vol.19 (2), p.171-175</ispartof><rights>Springer Nature America, Inc. 2012</rights><rights>COPYRIGHT 2012 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 2012</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c475t-4186ac43a74ee6ac74783e5d81a3ec9103e37386d0bae715e605350178e6d6dd3</citedby><cites>FETCH-LOGICAL-c475t-4186ac43a74ee6ac74783e5d81a3ec9103e37386d0bae715e605350178e6d6dd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/nsmb.2206$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/nsmb.2206$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,882,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22245969$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1093485$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Huang, Oscar W</creatorcontrib><creatorcontrib>Ma, Xiaolei</creatorcontrib><creatorcontrib>Yin, JianPing</creatorcontrib><creatorcontrib>Flinders, Jeremy</creatorcontrib><creatorcontrib>Maurer, Till</creatorcontrib><creatorcontrib>Kayagaki, Nobuhiko</creatorcontrib><creatorcontrib>Phung, Qui</creatorcontrib><creatorcontrib>Bosanac, Ivan</creatorcontrib><creatorcontrib>Arnott, David</creatorcontrib><creatorcontrib>Dixit, Vishva M</creatorcontrib><creatorcontrib>Hymowitz, Sarah G</creatorcontrib><creatorcontrib>Starovasnik, Melissa A</creatorcontrib><creatorcontrib>Cochran, Andrea G</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Phosphorylation-dependent activity of the deubiquitinase DUBA</title><title>Nat. Struct. Mol. Biol</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>Protease phosphorylation has been reported to affect many signaling pathways connected to proteolytic activity, but the underlying mechanisms have not been clearly elucidated. Structural and biochemical analyses of the deubiquitinase DUBA reveal that phosphorylation is necessary for productive ubiquitin substrate recognition and for enzyme activity.
Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of interactions involving the phosphate and the C-terminal tail of ubiquitin cause DUBA to fold around its substrate, revealing why phosphorylation is essential for deubiquitinase activity. Phosphoactivation of DUBA represents an unprecedented mode of protease regulation and a clear link between two major cellular signal transduction systems: phosphorylation and ubiquitin modification.</description><subject>631/337/458/1733</subject><subject>631/337/474/582</subject><subject>631/45/535</subject><subject>Biochemistry</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Cellular biology</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Endopeptidases - metabolism</subject><subject>Genetic aspects</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Biology</subject><subject>Models, Molecular</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Proteases</subject><subject>Protein Conformation</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure</subject><subject>Proteins</subject><subject>Serine - metabolism</subject><subject>Signaling</subject><subject>Substrates</subject><subject>Ubiquitin</subject><subject>Ubiquitin - metabolism</subject><issn>1545-9993</issn><issn>1545-9985</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</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>eNptkV1rHCEYhSW05Puif6AM7UVJYbY6jjN6kYttmiaBQEuTXIur7-waZnSjTsn--7psmi-CF77o8x7O4SD0geAJwZR_c3GYTaoKN1tol7CalUJw9u5xFnQH7cV4i3HFWEu30U5VVTUTjdhFx78XPi4XPqx6lax3pYElOAMuFUon-9emVeG7Ii2gMDDO7N1ok3UqQvHj5vv0AL3vVB_h8OHeRzc_T69PzsvLX2cXJ9PLUtctS2VNeKN0TVVbA-SprVtOgRlOFAUtcgagLeWNwTMFLWHQYEYZJi2HxjTG0H30aaPrY7IyaptAL7R3DnSSBAtac5ahLxtoGfzdCDHJwUYNfa8c-DFKQYRgrOI8k59fkbd-DC4nyGJUUJ4FxRM1Vz1I6zqfgtJrTTmtOMYiSzWZmrxB5WNgsNkidDa_v1g4erGQmQT3aa7GGOXF1Z83WR18jAE6uQx2UGGVfa6tcrmuXq6rz-zHh1DjbADzSP7vOgNfN0DMX24O4Xnq12r_ACaps5s</recordid><startdate>20120201</startdate><enddate>20120201</enddate><creator>Huang, Oscar W</creator><creator>Ma, Xiaolei</creator><creator>Yin, JianPing</creator><creator>Flinders, Jeremy</creator><creator>Maurer, Till</creator><creator>Kayagaki, Nobuhiko</creator><creator>Phung, Qui</creator><creator>Bosanac, Ivan</creator><creator>Arnott, David</creator><creator>Dixit, Vishva M</creator><creator>Hymowitz, Sarah G</creator><creator>Starovasnik, Melissa A</creator><creator>Cochran, Andrea G</creator><general>Nature Publishing Group US</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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</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>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</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>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PADUT</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>OTOTI</scope></search><sort><creationdate>20120201</creationdate><title>Phosphorylation-dependent activity of the deubiquitinase DUBA</title><author>Huang, Oscar W ; 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Struct. Mol. Biol</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huang, Oscar W</au><au>Ma, Xiaolei</au><au>Yin, JianPing</au><au>Flinders, Jeremy</au><au>Maurer, Till</au><au>Kayagaki, Nobuhiko</au><au>Phung, Qui</au><au>Bosanac, Ivan</au><au>Arnott, David</au><au>Dixit, Vishva M</au><au>Hymowitz, Sarah G</au><au>Starovasnik, Melissa A</au><au>Cochran, Andrea G</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation-dependent activity of the deubiquitinase DUBA</atitle><jtitle>Nat. Struct. Mol. Biol</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2012-02-01</date><risdate>2012</risdate><volume>19</volume><issue>2</issue><spage>171</spage><epage>175</epage><pages>171-175</pages><issn>1545-9993</issn><eissn>1545-9985</eissn><abstract>Protease phosphorylation has been reported to affect many signaling pathways connected to proteolytic activity, but the underlying mechanisms have not been clearly elucidated. Structural and biochemical analyses of the deubiquitinase DUBA reveal that phosphorylation is necessary for productive ubiquitin substrate recognition and for enzyme activity.
Addition and removal of ubiquitin or ubiquitin chains to and from proteins is a tightly regulated process that contributes to cellular signaling and protein stability. Here we show that phosphorylation of the human deubiquitinase DUBA (OTUD5) at a single residue, Ser177, is both necessary and sufficient to activate the enzyme. The crystal structure of the ubiquitin aldehyde adduct of active DUBA reveals a marked cooperation between phosphorylation and substrate binding. An intricate web of interactions involving the phosphate and the C-terminal tail of ubiquitin cause DUBA to fold around its substrate, revealing why phosphorylation is essential for deubiquitinase activity. Phosphoactivation of DUBA represents an unprecedented mode of protease regulation and a clear link between two major cellular signal transduction systems: phosphorylation and ubiquitin modification.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>22245969</pmid><doi>10.1038/nsmb.2206</doi><tpages>5</tpages></addata></record> |
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| subjects | 631/337/458/1733 631/337/474/582 631/45/535 Biochemistry Biological Microscopy Biomedical and Life Sciences Cellular biology Crystal structure Crystallography, X-Ray Endopeptidases - metabolism Genetic aspects Humans Life Sciences Membrane Biology Models, Molecular Phosphorylation Physiological aspects Proteases Protein Conformation Protein Processing, Post-Translational Protein Structure Proteins Serine - metabolism Signaling Substrates Ubiquitin Ubiquitin - metabolism |
| title | Phosphorylation-dependent activity of the deubiquitinase DUBA |
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