Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain
Parkin, a product of the causative gene of autosomal‐recessive juvenile parkinsonism (AR‐JP), is a RING‐type E3 ubiquitin ligase and has an amino‐terminal ubiquitin‐like (Ubl) domain. Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutat...
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| Veröffentlicht in: | EMBO reports 2003-03, Vol.4 (3), p.301-306 |
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| creator | Sakata, Eri Yamaguchi, Yoshiki Kurimoto, Eiji Kikuchi, Jun Yokoyama, Shigeyuki Yamada, Shingo Kawahara, Hiroyuki Yokosawa, Hideyoshi Hattori, Nobutaka Mizuno, Yoshikuni Tanaka, Keiji Kato, Koichi |
| description | Parkin, a product of the causative gene of autosomal‐recessive juvenile parkinsonism (AR‐JP), is a RING‐type E3 ubiquitin ligase and has an amino‐terminal ubiquitin‐like (Ubl) domain. Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutation) has been identified in AR‐JP patients, the function of this domain is not clear. In this study, we determined the three‐dimensional structure of the Ubl domain of parkin by NMR, in particular by extensive use of backbone 15 N‐1 H residual dipolar‐coupling data. Inspection of chemical‐shift‐perturbation data showed that the parkin Ubl domain binds the Rpn10 subunit of 26S proteasomes via the region of parkin that includes position 42. Our findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10‐binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR‐JP. |
| doi_str_mv | 10.1038/sj.embor.embor764 |
| format | Article |
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Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutation) has been identified in AR‐JP patients, the function of this domain is not clear. In this study, we determined the three‐dimensional structure of the Ubl domain of parkin by NMR, in particular by extensive use of backbone 15 N‐1 H residual dipolar‐coupling data. Inspection of chemical‐shift‐perturbation data showed that the parkin Ubl domain binds the Rpn10 subunit of 26S proteasomes via the region of parkin that includes position 42. Our findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10‐binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR‐JP.</description><identifier>ISSN: 1469-221X</identifier><identifier>EISSN: 1469-3178</identifier><identifier>EISSN: 1469-221X</identifier><identifier>DOI: 10.1038/sj.embor.embor764</identifier><identifier>PMID: 12634850</identifier><identifier>CODEN: ERMEAX</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Amino Acid Substitution ; Binding Sites ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; Genes, Recessive ; Humans ; Inspection ; Ligases - chemistry ; Ligases - metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Parkinsonian Disorders - genetics ; Peptide Hydrolases - chemistry ; Peptide Hydrolases - metabolism ; Proteasome Endopeptidase Complex ; Protein Conformation ; Scientific Report ; Sequence Alignment ; Sequence Homology, Amino Acid ; Ubiquitin - chemistry ; Ubiquitin - metabolism ; Ubiquitin-Protein Ligases</subject><ispartof>EMBO reports, 2003-03, Vol.4 (3), p.301-306</ispartof><rights>Copyright © 2003 European Molecular Biology Organisation</rights><rights>Copyright Nature Publishing Group Mar 2003</rights><rights>Copyright © 2003, European Molecular Biology Organisation 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5594-f047472e0d9e86fb3e8593973fcdce581cda5de82dcb7ee234748707e4da00dd3</citedby><cites>FETCH-LOGICAL-c5594-f047472e0d9e86fb3e8593973fcdce581cda5de82dcb7ee234748707e4da00dd3</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/PMC1315892/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1315892/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,315,728,781,785,886,1418,1434,27929,27930,45579,45580,46414,46838,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12634850$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sakata, Eri</creatorcontrib><creatorcontrib>Yamaguchi, Yoshiki</creatorcontrib><creatorcontrib>Kurimoto, Eiji</creatorcontrib><creatorcontrib>Kikuchi, Jun</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</creatorcontrib><creatorcontrib>Yamada, Shingo</creatorcontrib><creatorcontrib>Kawahara, Hiroyuki</creatorcontrib><creatorcontrib>Yokosawa, Hideyoshi</creatorcontrib><creatorcontrib>Hattori, Nobutaka</creatorcontrib><creatorcontrib>Mizuno, Yoshikuni</creatorcontrib><creatorcontrib>Tanaka, Keiji</creatorcontrib><creatorcontrib>Kato, Koichi</creatorcontrib><title>Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><description>Parkin, a product of the causative gene of autosomal‐recessive juvenile parkinsonism (AR‐JP), is a RING‐type E3 ubiquitin ligase and has an amino‐terminal ubiquitin‐like (Ubl) domain. Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutation) has been identified in AR‐JP patients, the function of this domain is not clear. In this study, we determined the three‐dimensional structure of the Ubl domain of parkin by NMR, in particular by extensive use of backbone 15 N‐1 H residual dipolar‐coupling data. Inspection of chemical‐shift‐perturbation data showed that the parkin Ubl domain binds the Rpn10 subunit of 26S proteasomes via the region of parkin that includes position 42. Our findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10‐binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR‐JP.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Substitution</subject><subject>Binding Sites</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>Genes, Recessive</subject><subject>Humans</subject><subject>Inspection</subject><subject>Ligases - chemistry</subject><subject>Ligases - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Parkinsonian Disorders - genetics</subject><subject>Peptide Hydrolases - chemistry</subject><subject>Peptide Hydrolases - metabolism</subject><subject>Proteasome Endopeptidase Complex</subject><subject>Protein Conformation</subject><subject>Scientific 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domain</atitle><jtitle>EMBO reports</jtitle><addtitle>EMBO Rep</addtitle><date>2003-03</date><risdate>2003</risdate><volume>4</volume><issue>3</issue><spage>301</spage><epage>306</epage><pages>301-306</pages><issn>1469-221X</issn><eissn>1469-3178</eissn><eissn>1469-221X</eissn><coden>ERMEAX</coden><abstract>Parkin, a product of the causative gene of autosomal‐recessive juvenile parkinsonism (AR‐JP), is a RING‐type E3 ubiquitin ligase and has an amino‐terminal ubiquitin‐like (Ubl) domain. Although a single mutation that causes an Arg to Pro substitution at position 42 of the Ubl domain (the Arg 42 mutation) has been identified in AR‐JP patients, the function of this domain is not clear. In this study, we determined the three‐dimensional structure of the Ubl domain of parkin by NMR, in particular by extensive use of backbone 15 N‐1 H residual dipolar‐coupling data. Inspection of chemical‐shift‐perturbation data showed that the parkin Ubl domain binds the Rpn10 subunit of 26S proteasomes via the region of parkin that includes position 42. Our findings suggest that the Arg 42 mutation induces a conformational change in the Rpn10‐binding site of Ubl, resulting in impaired proteasomal binding of parkin, which could be the cause of AR‐JP.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>12634850</pmid><doi>10.1038/sj.embor.embor764</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino Acid Substitution Binding Sites Carrier Proteins - chemistry Carrier Proteins - metabolism Genes, Recessive Humans Inspection Ligases - chemistry Ligases - metabolism Models, Molecular Molecular Sequence Data Mutagenesis, Site-Directed Mutation Parkinsonian Disorders - genetics Peptide Hydrolases - chemistry Peptide Hydrolases - metabolism Proteasome Endopeptidase Complex Protein Conformation Scientific Report Sequence Alignment Sequence Homology, Amino Acid Ubiquitin - chemistry Ubiquitin - metabolism Ubiquitin-Protein Ligases |
| title | Parkin binds the Rpn10 subunit of 26S proteasomes through its ubiquitin-like domain |
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