Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases
Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of numerous processes. One example is ADP-ribosylation of the carboxyl terminus of ubiquitin by the E3 DTX3L/ADP-ribosyltransferase PARP9 heterodimer, but the mechanism remains elusive....
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| Veröffentlicht in: | Science advances 2020-09, Vol.6 (38) |
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| container_issue | 38 |
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| container_title | Science advances |
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| creator | Chatrin, Chatrin Gabrielsen, Mads Buetow, Lori Nakasone, Mark A Ahmed, Syed F Sumpton, David Sibbet, Gary J Smith, Brian O Huang, Danny T |
| description | Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of numerous processes. One example is ADP-ribosylation of the carboxyl terminus of ubiquitin by the E3 DTX3L/ADP-ribosyltransferase PARP9 heterodimer, but the mechanism remains elusive. Here, we show that independently of PARP9, the conserved carboxyl-terminal RING and DTC (Deltex carboxyl-terminal) domains of DTX3L and other human Deltex proteins (DTX1 to DTX4) catalyze ADP-ribosylation of ubiquitin's Gly
Structural studies reveal a hitherto unknown function of the DTC domain in binding NAD
Deltex RING domain recruits E2 thioesterified with ubiquitin and juxtaposes it with NAD
bound to the DTC domain to facilitate ADP-ribosylation of ubiquitin. This ubiquitin modification prevents its activation but is reversed by the linkage nonspecific deubiquitinases. Our study provides mechanistic insights into ADP-ribosylation of ubiquitin by Deltex E3s and will enable future studies directed at understanding the increasingly complex network of ubiquitin cross-talk. |
| doi_str_mv | 10.1126/sciadv.abc0418 |
| format | Article |
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Structural studies reveal a hitherto unknown function of the DTC domain in binding NAD
Deltex RING domain recruits E2 thioesterified with ubiquitin and juxtaposes it with NAD
bound to the DTC domain to facilitate ADP-ribosylation of ubiquitin. This ubiquitin modification prevents its activation but is reversed by the linkage nonspecific deubiquitinases. Our study provides mechanistic insights into ADP-ribosylation of ubiquitin by Deltex E3s and will enable future studies directed at understanding the increasingly complex network of ubiquitin cross-talk.</description><identifier>ISSN: 2375-2548</identifier><identifier>EISSN: 2375-2548</identifier><identifier>DOI: 10.1126/sciadv.abc0418</identifier><identifier>PMID: 32948590</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>ADP-Ribosylation ; Biochemistry ; Humans ; NAD - metabolism ; SciAdv r-articles ; Structural Biology ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases - metabolism ; Ubiquitination</subject><ispartof>Science advances, 2020-09, Vol.6 (38)</ispartof><rights>Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).</rights><rights>Copyright © 2020 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). 2020 The Authors</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c390t-4bcbbb3c7a55df58e848a6cd9b354d2f2429e3c461009a126a28260287662a73</citedby><cites>FETCH-LOGICAL-c390t-4bcbbb3c7a55df58e848a6cd9b354d2f2429e3c461009a126a28260287662a73</cites><orcidid>0000-0002-9848-2276 ; 0000-0002-5666-3175 ; 0000-0003-4951-8057 ; 0000-0003-3363-4168 ; 0000-0002-6192-259X ; 0000-0002-1362-191X ; 0000-0003-1033-2538 ; 0000-0002-9004-4079</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7500938/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7500938/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/32948590$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chatrin, Chatrin</creatorcontrib><creatorcontrib>Gabrielsen, Mads</creatorcontrib><creatorcontrib>Buetow, Lori</creatorcontrib><creatorcontrib>Nakasone, Mark A</creatorcontrib><creatorcontrib>Ahmed, Syed F</creatorcontrib><creatorcontrib>Sumpton, David</creatorcontrib><creatorcontrib>Sibbet, Gary J</creatorcontrib><creatorcontrib>Smith, Brian O</creatorcontrib><creatorcontrib>Huang, Danny T</creatorcontrib><title>Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases</title><title>Science advances</title><addtitle>Sci Adv</addtitle><description>Cellular cross-talk between ubiquitination and other posttranslational modifications contributes to the regulation of numerous processes. One example is ADP-ribosylation of the carboxyl terminus of ubiquitin by the E3 DTX3L/ADP-ribosyltransferase PARP9 heterodimer, but the mechanism remains elusive. Here, we show that independently of PARP9, the conserved carboxyl-terminal RING and DTC (Deltex carboxyl-terminal) domains of DTX3L and other human Deltex proteins (DTX1 to DTX4) catalyze ADP-ribosylation of ubiquitin's Gly
Structural studies reveal a hitherto unknown function of the DTC domain in binding NAD
Deltex RING domain recruits E2 thioesterified with ubiquitin and juxtaposes it with NAD
bound to the DTC domain to facilitate ADP-ribosylation of ubiquitin. This ubiquitin modification prevents its activation but is reversed by the linkage nonspecific deubiquitinases. 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Structural studies reveal a hitherto unknown function of the DTC domain in binding NAD
Deltex RING domain recruits E2 thioesterified with ubiquitin and juxtaposes it with NAD
bound to the DTC domain to facilitate ADP-ribosylation of ubiquitin. This ubiquitin modification prevents its activation but is reversed by the linkage nonspecific deubiquitinases. Our study provides mechanistic insights into ADP-ribosylation of ubiquitin by Deltex E3s and will enable future studies directed at understanding the increasingly complex network of ubiquitin cross-talk.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>32948590</pmid><doi>10.1126/sciadv.abc0418</doi><orcidid>https://orcid.org/0000-0002-9848-2276</orcidid><orcidid>https://orcid.org/0000-0002-5666-3175</orcidid><orcidid>https://orcid.org/0000-0003-4951-8057</orcidid><orcidid>https://orcid.org/0000-0003-3363-4168</orcidid><orcidid>https://orcid.org/0000-0002-6192-259X</orcidid><orcidid>https://orcid.org/0000-0002-1362-191X</orcidid><orcidid>https://orcid.org/0000-0003-1033-2538</orcidid><orcidid>https://orcid.org/0000-0002-9004-4079</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | ADP-Ribosylation Biochemistry Humans NAD - metabolism SciAdv r-articles Structural Biology Ubiquitin - metabolism Ubiquitin-Protein Ligases - metabolism Ubiquitination |
| title | Structural insights into ADP-ribosylation of ubiquitin by Deltex family E3 ubiquitin ligases |
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