UBE2O is a quality control factor for orphans of multiprotein complexes
Many nascent proteins are assembled into multiprotein complexes of defined stoichiometry. Imbalances in the synthesis of individual subunits result in orphans. How orphans are selectively eliminated to maintain protein homeostasis is poorly understood. Here, we found that the conserved ubiquitin-con...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2017-08, Vol.357 (6350), p.472-475 |
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| creator | Yanagitani, Kota Juszkiewicz, Szymon Hegde, Ramanujan S. |
| description | Many nascent proteins are assembled into multiprotein complexes of defined stoichiometry. Imbalances in the synthesis of individual subunits result in orphans. How orphans are selectively eliminated to maintain protein homeostasis is poorly understood. Here, we found that the conserved ubiquitin-conjugating enzyme UBE2O directly recognized juxtaposed basic and hydrophobic patches on unassembled proteins to mediate ubiquitination without a separate ubiquitin ligase. In reticulocytes, where UBE2O is highly up-regulated, unassembled α-globin molecules that failed to assemble with β-globin were selectively ubiquitinated by UBE2O. In nonreticulocytes, ribosomal proteins that did not engage nuclear import factors were targets for UBE2O. Thus, UBE2O is a self-contained quality control factor that comprises substrate recognition and ubiquitin transfer activities within a single protein to efficiently target orphans of multiprotein complexes for degradation. |
| doi_str_mv | 10.1126/science.aan0178 |
| format | Article |
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Imbalances in the synthesis of individual subunits result in orphans. How orphans are selectively eliminated to maintain protein homeostasis is poorly understood. Here, we found that the conserved ubiquitin-conjugating enzyme UBE2O directly recognized juxtaposed basic and hydrophobic patches on unassembled proteins to mediate ubiquitination without a separate ubiquitin ligase. In reticulocytes, where UBE2O is highly up-regulated, unassembled α-globin molecules that failed to assemble with β-globin were selectively ubiquitinated by UBE2O. In nonreticulocytes, ribosomal proteins that did not engage nuclear import factors were targets for UBE2O. Thus, UBE2O is a self-contained quality control factor that comprises substrate recognition and ubiquitin transfer activities within a single protein to efficiently target orphans of multiprotein complexes for degradation.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.aan0178</identifier><identifier>PMID: 28774922</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Active Transport, Cell Nucleus ; alpha-Globins - metabolism ; beta-Globins - metabolism ; Cytosol - enzymology ; Degradation ; Dissection ; Enzymes ; Erythrocytes ; HEK293 Cells ; Hemoglobin ; Homeostasis ; Humans ; Hydrophobic and Hydrophilic Interactions ; Hydrophobicity ; Individualized Instruction ; Multiprotein Complexes - metabolism ; Nuclear transport ; Proteins ; Proteolysis ; Quality control ; Reticulocytes ; Reticulocytes - enzymology ; Ribosomal proteins ; Ribosomal Proteins - metabolism ; Ribosomes ; SEC Translocation Channels - metabolism ; Stoichiometry ; Substrates ; Ubiquitin ; Ubiquitin - metabolism ; Ubiquitin-conjugating enzyme ; Ubiquitin-Conjugating Enzymes - metabolism ; Ubiquitin-protein ligase ; Ubiquitination</subject><ispartof>Science (American Association for the Advancement of Science), 2017-08, Vol.357 (6350), p.472-475</ispartof><rights>Copyright © 2017 by the American Association for the Advancement of Science</rights><rights>Copyright © 2017 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. 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Imbalances in the synthesis of individual subunits result in orphans. How orphans are selectively eliminated to maintain protein homeostasis is poorly understood. Here, we found that the conserved ubiquitin-conjugating enzyme UBE2O directly recognized juxtaposed basic and hydrophobic patches on unassembled proteins to mediate ubiquitination without a separate ubiquitin ligase. In reticulocytes, where UBE2O is highly up-regulated, unassembled α-globin molecules that failed to assemble with β-globin were selectively ubiquitinated by UBE2O. In nonreticulocytes, ribosomal proteins that did not engage nuclear import factors were targets for UBE2O. Thus, UBE2O is a self-contained quality control factor that comprises substrate recognition and ubiquitin transfer activities within a single protein to efficiently target orphans of multiprotein complexes for degradation.</description><subject>Active Transport, Cell Nucleus</subject><subject>alpha-Globins - metabolism</subject><subject>beta-Globins - metabolism</subject><subject>Cytosol - enzymology</subject><subject>Degradation</subject><subject>Dissection</subject><subject>Enzymes</subject><subject>Erythrocytes</subject><subject>HEK293 Cells</subject><subject>Hemoglobin</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hydrophobicity</subject><subject>Individualized Instruction</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Nuclear transport</subject><subject>Proteins</subject><subject>Proteolysis</subject><subject>Quality control</subject><subject>Reticulocytes</subject><subject>Reticulocytes - enzymology</subject><subject>Ribosomal proteins</subject><subject>Ribosomal Proteins - metabolism</subject><subject>Ribosomes</subject><subject>SEC Translocation Channels - metabolism</subject><subject>Stoichiometry</subject><subject>Substrates</subject><subject>Ubiquitin</subject><subject>Ubiquitin - metabolism</subject><subject>Ubiquitin-conjugating enzyme</subject><subject>Ubiquitin-Conjugating Enzymes - metabolism</subject><subject>Ubiquitin-protein ligase</subject><subject>Ubiquitination</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkD1PwzAQhi0EoqUwM4EssbCk9Ufs5EaoSkGq1KXMkXFskSqJWzuR6L_H0AASw-mGe-7V3YPQNSVTSpmcBV2ZVpupUi2hWX6CxpSASIARforGhHCZ5CQTI3QRwpaQOAN-jkYsz7IUGBuj5evjgq1xFbDC-17VVXfA2rWddzW2SnfOYxvL-d27agN2Fjd93VU77zpTtRFtdrX5MOESnVlVB3M19AnaPC028-dktV6-zB9WiU5F2iVcktJympYWOAhVMs7zlGZGcGYNkwao5aXJrACAUlOgwtBcZvEFZmkOfILuj7HxgH1vQlc0VdCmrlVrXB8KCkzKnKeSRfTuH7p1vW_jcZGK34Nk34GzI6W9C8EbW-x81Sh_KCgpvhQXg-JiUBw3bofc_q0x5S__4zQCN0dgG6K-v7nkACL6_wRX94Fp</recordid><startdate>20170804</startdate><enddate>20170804</enddate><creator>Yanagitani, Kota</creator><creator>Juszkiewicz, Szymon</creator><creator>Hegde, Ramanujan S.</creator><general>American Association for the Advancement of Science</general><general>The American Association for the Advancement of Science</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>7QF</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QQ</scope><scope>7QR</scope><scope>7SC</scope><scope>7SE</scope><scope>7SN</scope><scope>7SP</scope><scope>7SR</scope><scope>7SS</scope><scope>7T7</scope><scope>7TA</scope><scope>7TB</scope><scope>7TK</scope><scope>7TM</scope><scope>7U5</scope><scope>7U9</scope><scope>8BQ</scope><scope>8FD</scope><scope>C1K</scope><scope>F28</scope><scope>FR3</scope><scope>H8D</scope><scope>H8G</scope><scope>H94</scope><scope>JG9</scope><scope>JQ2</scope><scope>K9.</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3361-7264</orcidid><orcidid>https://orcid.org/0000-0002-5905-9950</orcidid><orcidid>https://orcid.org/0000-0001-8338-852X</orcidid></search><sort><creationdate>20170804</creationdate><title>UBE2O is a quality control factor for orphans of multiprotein complexes</title><author>Yanagitani, Kota ; 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Imbalances in the synthesis of individual subunits result in orphans. How orphans are selectively eliminated to maintain protein homeostasis is poorly understood. Here, we found that the conserved ubiquitin-conjugating enzyme UBE2O directly recognized juxtaposed basic and hydrophobic patches on unassembled proteins to mediate ubiquitination without a separate ubiquitin ligase. In reticulocytes, where UBE2O is highly up-regulated, unassembled α-globin molecules that failed to assemble with β-globin were selectively ubiquitinated by UBE2O. In nonreticulocytes, ribosomal proteins that did not engage nuclear import factors were targets for UBE2O. 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| source | American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE |
| subjects | Active Transport, Cell Nucleus alpha-Globins - metabolism beta-Globins - metabolism Cytosol - enzymology Degradation Dissection Enzymes Erythrocytes HEK293 Cells Hemoglobin Homeostasis Humans Hydrophobic and Hydrophilic Interactions Hydrophobicity Individualized Instruction Multiprotein Complexes - metabolism Nuclear transport Proteins Proteolysis Quality control Reticulocytes Reticulocytes - enzymology Ribosomal proteins Ribosomal Proteins - metabolism Ribosomes SEC Translocation Channels - metabolism Stoichiometry Substrates Ubiquitin Ubiquitin - metabolism Ubiquitin-conjugating enzyme Ubiquitin-Conjugating Enzymes - metabolism Ubiquitin-protein ligase Ubiquitination |
| title | UBE2O is a quality control factor for orphans of multiprotein complexes |
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