A molecular explanation for the recessive nature of parkin-linked Parkinson's disease.
Identifieur interne : 000989 ( PubMed/Corpus ); précédent : 000988; suivant : 000990A molecular explanation for the recessive nature of parkin-linked Parkinson's disease.
Auteurs : Donald E. Spratt ; R Julio Martinez-Torres ; Yeong J. Noh ; Pascal Mercier ; Noah Manczyk ; Kathryn R. Barber ; Jacob D. Aguirre ; Lynn Burchell ; Andrew Purkiss ; Helen Walden ; Gary S. ShawSource :
- Nature communications [ 2041-1723 ] ; 2013.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Biocatalysis, Drosophila melanogaster, Genes, Recessive (genetics), Humans, Models, Molecular, Molecular Sequence Data, Mutation (genetics), Parkinson Disease (genetics), Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Substrate Specificity, Ubiquitin-Conjugating Enzymes (metabolism), Ubiquitin-Protein Ligases (chemistry), Ubiquitin-Protein Ligases (genetics).
- MESH :
- chemical , chemistry : Ubiquitin-Protein Ligases.
- chemical , genetics : Ubiquitin-Protein Ligases.
- chemical , metabolism : Ubiquitin-Conjugating Enzymes.
- genetics : Genes, Recessive, Mutation, Parkinson Disease.
- Amino Acid Sequence, Animals, Biocatalysis, Drosophila melanogaster, Humans, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Tertiary, Sequence Alignment, Substrate Specificity.
Abstract
Mutations in the park2 gene, encoding the RING-inBetweenRING-RING E3 ubiquitin ligase parkin, cause 50% of autosomal recessive juvenile Parkinsonism cases. More than 70 known pathogenic mutations occur throughout parkin, many of which cluster in the inhibitory amino-terminal ubiquitin-like domain, and the carboxy-terminal RING2 domain that is indispensable for ubiquitin transfer. A structural rationale showing how autosomal recessive juvenile Parkinsonism mutations alter parkin function is still lacking. Here we show that the structure of parkin RING2 is distinct from canonical RING E3 ligases and lacks key elements required for E2-conjugating enzyme recruitment. Several pathogenic mutations in RING2 alter the environment of a single surface-exposed catalytic cysteine to inhibit ubiquitination. Native parkin adopts a globular inhibited conformation in solution facilitated by the association of the ubiquitin-like domain with the RING-inBetweenRING-RING C-terminus. Autosomal recessive juvenile Parkinsonism mutations disrupt this conformation. Finally, parkin autoubiquitinates only in cis, providing a molecular explanation for the recessive nature of autosomal recessive juvenile Parkinsonism.
DOI: 10.1038/ncomms2983
PubMed: 23770917
Links to Exploration step
pubmed:23770917Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A molecular explanation for the recessive nature of parkin-linked Parkinson's disease.</title><author><name sortKey="Spratt, Donald E" sort="Spratt, Donald E" uniqKey="Spratt D" first="Donald E" last="Spratt">Donald E. Spratt</name><affiliation><nlm:affiliation>Department of Biochemistry, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.</nlm:affiliation></affiliation></author><author><name sortKey="Martinez Torres, R Julio" sort="Martinez Torres, R Julio" uniqKey="Martinez Torres R" first="R Julio" last="Martinez-Torres">R Julio Martinez-Torres</name></author><author><name sortKey="Noh, Yeong J" sort="Noh, Yeong J" uniqKey="Noh Y" first="Yeong J" last="Noh">Yeong J. Noh</name></author><author><name sortKey="Mercier, Pascal" sort="Mercier, Pascal" uniqKey="Mercier P" first="Pascal" last="Mercier">Pascal Mercier</name></author><author><name sortKey="Manczyk, Noah" sort="Manczyk, Noah" uniqKey="Manczyk N" first="Noah" last="Manczyk">Noah Manczyk</name></author><author><name sortKey="Barber, Kathryn R" sort="Barber, Kathryn R" uniqKey="Barber K" first="Kathryn R" last="Barber">Kathryn R. Barber</name></author><author><name sortKey="Aguirre, Jacob D" sort="Aguirre, Jacob D" uniqKey="Aguirre J" first="Jacob D" last="Aguirre">Jacob D. Aguirre</name></author><author><name sortKey="Burchell, Lynn" sort="Burchell, Lynn" uniqKey="Burchell L" first="Lynn" last="Burchell">Lynn Burchell</name></author><author><name sortKey="Purkiss, Andrew" sort="Purkiss, Andrew" uniqKey="Purkiss A" first="Andrew" last="Purkiss">Andrew Purkiss</name></author><author><name sortKey="Walden, Helen" sort="Walden, Helen" uniqKey="Walden H" first="Helen" last="Walden">Helen Walden</name></author><author><name sortKey="Shaw, Gary S" sort="Shaw, Gary S" uniqKey="Shaw G" first="Gary S" last="Shaw">Gary S. 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Spratt</name><affiliation><nlm:affiliation>Department of Biochemistry, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.</nlm:affiliation></affiliation></author><author><name sortKey="Martinez Torres, R Julio" sort="Martinez Torres, R Julio" uniqKey="Martinez Torres R" first="R Julio" last="Martinez-Torres">R Julio Martinez-Torres</name></author><author><name sortKey="Noh, Yeong J" sort="Noh, Yeong J" uniqKey="Noh Y" first="Yeong J" last="Noh">Yeong J. Noh</name></author><author><name sortKey="Mercier, Pascal" sort="Mercier, Pascal" uniqKey="Mercier P" first="Pascal" last="Mercier">Pascal Mercier</name></author><author><name sortKey="Manczyk, Noah" sort="Manczyk, Noah" uniqKey="Manczyk N" first="Noah" last="Manczyk">Noah Manczyk</name></author><author><name sortKey="Barber, Kathryn R" sort="Barber, Kathryn R" uniqKey="Barber K" first="Kathryn R" last="Barber">Kathryn R. Barber</name></author><author><name sortKey="Aguirre, Jacob D" sort="Aguirre, Jacob D" uniqKey="Aguirre J" first="Jacob D" last="Aguirre">Jacob D. Aguirre</name></author><author><name sortKey="Burchell, Lynn" sort="Burchell, Lynn" uniqKey="Burchell L" first="Lynn" last="Burchell">Lynn Burchell</name></author><author><name sortKey="Purkiss, Andrew" sort="Purkiss, Andrew" uniqKey="Purkiss A" first="Andrew" last="Purkiss">Andrew Purkiss</name></author><author><name sortKey="Walden, Helen" sort="Walden, Helen" uniqKey="Walden H" first="Helen" last="Walden">Helen Walden</name></author><author><name sortKey="Shaw, Gary S" sort="Shaw, Gary S" uniqKey="Shaw G" first="Gary S" last="Shaw">Gary S. Shaw</name></author></analytic><series><title level="j">Nature communications</title><idno type="eISSN">2041-1723</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Biocatalysis</term><term>Drosophila melanogaster</term><term>Genes, Recessive (genetics)</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutation (genetics)</term><term>Parkinson Disease (genetics)</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Substrate Specificity</term><term>Ubiquitin-Conjugating Enzymes (metabolism)</term><term>Ubiquitin-Protein Ligases (chemistry)</term><term>Ubiquitin-Protein Ligases (genetics)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ubiquitin-Conjugating Enzymes</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Genes, Recessive</term><term>Mutation</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Biocatalysis</term><term>Drosophila melanogaster</term><term>Humans</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Protein Binding</term><term>Protein Structure, Tertiary</term><term>Sequence Alignment</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mutations in the park2 gene, encoding the RING-inBetweenRING-RING E3 ubiquitin ligase parkin, cause 50% of autosomal recessive juvenile Parkinsonism cases. More than 70 known pathogenic mutations occur throughout parkin, many of which cluster in the inhibitory amino-terminal ubiquitin-like domain, and the carboxy-terminal RING2 domain that is indispensable for ubiquitin transfer. A structural rationale showing how autosomal recessive juvenile Parkinsonism mutations alter parkin function is still lacking. Here we show that the structure of parkin RING2 is distinct from canonical RING E3 ligases and lacks key elements required for E2-conjugating enzyme recruitment. Several pathogenic mutations in RING2 alter the environment of a single surface-exposed catalytic cysteine to inhibit ubiquitination. Native parkin adopts a globular inhibited conformation in solution facilitated by the association of the ubiquitin-like domain with the RING-inBetweenRING-RING C-terminus. Autosomal recessive juvenile Parkinsonism mutations disrupt this conformation. Finally, parkin autoubiquitinates only in cis, providing a molecular explanation for the recessive nature of autosomal recessive juvenile Parkinsonism.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23770917</PMID><DateCreated><Year>2013</Year><Month>06</Month><Day>17</Day></DateCreated><DateCompleted><Year>2013</Year><Month>12</Month><Day>30</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN><JournalIssue CitedMedium="Internet"><Volume>4</Volume><PubDate><Year>2013</Year></PubDate></JournalIssue><Title>Nature communications</Title><ISOAbbreviation>Nat Commun</ISOAbbreviation></Journal><ArticleTitle>A molecular explanation for the recessive nature of parkin-linked Parkinson's disease.</ArticleTitle><Pagination><MedlinePgn>1983</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/ncomms2983</ELocationID><Abstract><AbstractText>Mutations in the park2 gene, encoding the RING-inBetweenRING-RING E3 ubiquitin ligase parkin, cause 50% of autosomal recessive juvenile Parkinsonism cases. More than 70 known pathogenic mutations occur throughout parkin, many of which cluster in the inhibitory amino-terminal ubiquitin-like domain, and the carboxy-terminal RING2 domain that is indispensable for ubiquitin transfer. A structural rationale showing how autosomal recessive juvenile Parkinsonism mutations alter parkin function is still lacking. Here we show that the structure of parkin RING2 is distinct from canonical RING E3 ligases and lacks key elements required for E2-conjugating enzyme recruitment. Several pathogenic mutations in RING2 alter the environment of a single surface-exposed catalytic cysteine to inhibit ubiquitination. Native parkin adopts a globular inhibited conformation in solution facilitated by the association of the ubiquitin-like domain with the RING-inBetweenRING-RING C-terminus. Autosomal recessive juvenile Parkinsonism mutations disrupt this conformation. Finally, parkin autoubiquitinates only in cis, providing a molecular explanation for the recessive nature of autosomal recessive juvenile Parkinsonism.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Spratt</LastName><ForeName>Donald E</ForeName><Initials>DE</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Schulich School of Medicine and Dentistry, University of Western Ontario, London, Ontario, Canada N6A 5C1.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martinez-Torres</LastName><ForeName>R Julio</ForeName><Initials>RJ</Initials></Author><Author ValidYN="Y"><LastName>Noh</LastName><ForeName>Yeong J</ForeName><Initials>YJ</Initials></Author><Author ValidYN="Y"><LastName>Mercier</LastName><ForeName>Pascal</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Manczyk</LastName><ForeName>Noah</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Barber</LastName><ForeName>Kathryn R</ForeName><Initials>KR</Initials></Author><Author ValidYN="Y"><LastName>Aguirre</LastName><ForeName>Jacob D</ForeName><Initials>JD</Initials></Author><Author ValidYN="Y"><LastName>Burchell</LastName><ForeName>Lynn</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Purkiss</LastName><ForeName>Andrew</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Walden</LastName><ForeName>Helen</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Shaw</LastName><ForeName>Gary S</ForeName><Initials>GS</Initials></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>2LWR</AccessionNumber><AccessionNumber>2M48</AccessionNumber></AccessionNumberList></DataBank></DataBankList><GrantList CompleteYN="Y"><Grant><GrantID>MOP-14606</GrantID><Agency>Canadian Institutes of Health Research</Agency><Country>Canada</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nat Commun</MedlineTA><NlmUniqueID>101528555</NlmUniqueID><ISSNLinking>2041-1723</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 2.3.2.23</RegistryNumber><NameOfSubstance UI="D044763">Ubiquitin-Conjugating Enzymes</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber><NameOfSubstance UI="D044767">Ubiquitin-Protein Ligases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber><NameOfSubstance UI="C111567">parkin protein</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Protein Sci. 2012 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MajorTopicYN="N">Drosophila melanogaster</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005808" MajorTopicYN="N">Genes, Recessive</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein 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|area= ParkinsonCanadaV1
|flux= PubMed
|étape= Corpus
|type= RBID
|clé= pubmed:23770917
|texte= A molecular explanation for the recessive nature of parkin-linked Parkinson's disease.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:23770917" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \
| NlmPubMed2Wicri -a ParkinsonCanadaV1
| This area was generated with Dilib version V0.6.29. |  |