The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications.
Identifieur interne : 000499 ( PubMed/Curation ); précédent : 000498; suivant : 000500The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications.
Auteurs : Thomas M. Durcan [Canada] ; Edward A. Fon [Canada]Source :
- Genes & development [ 1549-5477 ] ; 2015.
English descriptors
- KwdEn :
- Enzyme Activation, Humans, Mitochondria (enzymology), Mitochondria (genetics), Mitochondria (pathology), Mitochondrial Degradation (genetics), Mitochondrial Degradation (physiology), Parkinson Disease (enzymology), Parkinson Disease (pathology), Phosphorylation, Protein Kinases (genetics), Protein Kinases (metabolism), Protein Processing, Post-Translational, Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism), Ubiquitination.
- MESH :
- chemical , genetics : Protein Kinases, Ubiquitin-Protein Ligases.
- enzymology : Mitochondria, Parkinson Disease.
- genetics : Mitochondria, Mitochondrial Degradation.
- chemical , metabolism : Protein Kinases, Ubiquitin-Protein Ligases.
- pathology : Mitochondria, Parkinson Disease.
- physiology : Mitochondrial Degradation.
- Enzyme Activation, Humans, Phosphorylation, Protein Processing, Post-Translational, Ubiquitination.
Abstract
Two Parkinson's disease (PD)-associated proteins, the mitochondrial kinase PINK1 and the E3-ubiquitin (Ub) ligase PARKIN, are central to mitochondrial quality control. In this pathway, PINK1 accumulates on defective mitochondria, eliciting the translocation of PARKIN from the cytosol to mediate the clearance of damaged mitochondria via autophagy (mitophagy). Throughout the different stages of mitophagy, post-translational modifications (PTMs) are critical for the regulation of PINK1 and PARKIN activity and function. Indeed, activation and recruitment of PARKIN onto damaged mitochondria involves PINK1-mediated phosphorylation of both PARKIN and Ub. Through a stepwise cascade, PARKIN is converted from an autoinhibited enzyme into an active phospho-Ub-dependent E3 ligase. Upon activation, PARKIN ubiquitinates itself in concert with many different mitochondrial substrates. The Ub conjugates attached to these substrates can in turn be phosphorylated by PINK1, which triggers further cycles of PARKIN recruitment and activation. This feed-forward amplification loop regulates both PARKIN activity and mitophagy. However, the precise steps and sequence of PTMs in this cascade are only now being uncovered. For instance, the Ub conjugates assembled by PARKIN consist predominantly of noncanonical K6-linked Ub chains. Moreover, these modifications are reversible and can be disassembled by deubiquitinating enzymes (DUBs), including Ub-specific protease 8 (USP8), USP15, and USP30. However, PINK1-mediated phosphorylation of Ub can impede the activity of these DUBs, adding a new layer of complexity to the regulation of PARKIN-mediated mitophagy by PTMs. It is therefore evident that further insight into how PTMs regulate the PINK1-PARKIN pathway will be critical for our understanding of mitochondrial quality control.
DOI: 10.1101/gad.262758.115
PubMed: 25995186
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Fon</name><affiliation wicri:level="1"><nlm:affiliation>McGill Parkinson's Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.</nlm:affiliation><country wicri:rule="url">Canada</country><wicri:regionArea>McGill Parkinson's Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25995186</idno><idno type="pmid">25995186</idno><idno type="doi">10.1101/gad.262758.115</idno><idno type="wicri:Area/PubMed/Corpus">000499</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000499</idno><idno type="wicri:Area/PubMed/Curation">000499</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000499</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications.</title><author><name sortKey="Durcan, Thomas M" sort="Durcan, Thomas M" uniqKey="Durcan T" first="Thomas M" last="Durcan">Thomas M. 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Fon</name><affiliation wicri:level="1"><nlm:affiliation>McGill Parkinson's Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.</nlm:affiliation><country wicri:rule="url">Canada</country><wicri:regionArea>McGill Parkinson's Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4</wicri:regionArea></affiliation></author></analytic><series><title level="j">Genes & development</title><idno type="eISSN">1549-5477</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Enzyme Activation</term><term>Humans</term><term>Mitochondria (enzymology)</term><term>Mitochondria (genetics)</term><term>Mitochondria (pathology)</term><term>Mitochondrial Degradation (genetics)</term><term>Mitochondrial Degradation (physiology)</term><term>Parkinson Disease (enzymology)</term><term>Parkinson Disease (pathology)</term><term>Phosphorylation</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (metabolism)</term><term>Protein Processing, Post-Translational</term><term>Ubiquitin-Protein Ligases (genetics)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Protein Kinases</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Mitochondria</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Mitochondria</term><term>Mitochondrial Degradation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein Kinases</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Mitochondria</term><term>Parkinson Disease</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Mitochondrial Degradation</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme Activation</term><term>Humans</term><term>Phosphorylation</term><term>Protein Processing, Post-Translational</term><term>Ubiquitination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Two Parkinson's disease (PD)-associated proteins, the mitochondrial kinase PINK1 and the E3-ubiquitin (Ub) ligase PARKIN, are central to mitochondrial quality control. In this pathway, PINK1 accumulates on defective mitochondria, eliciting the translocation of PARKIN from the cytosol to mediate the clearance of damaged mitochondria via autophagy (mitophagy). Throughout the different stages of mitophagy, post-translational modifications (PTMs) are critical for the regulation of PINK1 and PARKIN activity and function. Indeed, activation and recruitment of PARKIN onto damaged mitochondria involves PINK1-mediated phosphorylation of both PARKIN and Ub. Through a stepwise cascade, PARKIN is converted from an autoinhibited enzyme into an active phospho-Ub-dependent E3 ligase. Upon activation, PARKIN ubiquitinates itself in concert with many different mitochondrial substrates. The Ub conjugates attached to these substrates can in turn be phosphorylated by PINK1, which triggers further cycles of PARKIN recruitment and activation. This feed-forward amplification loop regulates both PARKIN activity and mitophagy. However, the precise steps and sequence of PTMs in this cascade are only now being uncovered. For instance, the Ub conjugates assembled by PARKIN consist predominantly of noncanonical K6-linked Ub chains. Moreover, these modifications are reversible and can be disassembled by deubiquitinating enzymes (DUBs), including Ub-specific protease 8 (USP8), USP15, and USP30. However, PINK1-mediated phosphorylation of Ub can impede the activity of these DUBs, adding a new layer of complexity to the regulation of PARKIN-mediated mitophagy by PTMs. It is therefore evident that further insight into how PTMs regulate the PINK1-PARKIN pathway will be critical for our understanding of mitochondrial quality control.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25995186</PMID><DateCreated><Year>2015</Year><Month>05</Month><Day>21</Day></DateCreated><DateCompleted><Year>2015</Year><Month>07</Month><Day>21</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1549-5477</ISSN><JournalIssue CitedMedium="Internet"><Volume>29</Volume><Issue>10</Issue><PubDate><Year>2015</Year><Month>May</Month><Day>15</Day></PubDate></JournalIssue><Title>Genes & development</Title><ISOAbbreviation>Genes Dev.</ISOAbbreviation></Journal><ArticleTitle>The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications.</ArticleTitle><Pagination><MedlinePgn>989-99</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1101/gad.262758.115</ELocationID><Abstract><AbstractText>Two Parkinson's disease (PD)-associated proteins, the mitochondrial kinase PINK1 and the E3-ubiquitin (Ub) ligase PARKIN, are central to mitochondrial quality control. In this pathway, PINK1 accumulates on defective mitochondria, eliciting the translocation of PARKIN from the cytosol to mediate the clearance of damaged mitochondria via autophagy (mitophagy). Throughout the different stages of mitophagy, post-translational modifications (PTMs) are critical for the regulation of PINK1 and PARKIN activity and function. Indeed, activation and recruitment of PARKIN onto damaged mitochondria involves PINK1-mediated phosphorylation of both PARKIN and Ub. Through a stepwise cascade, PARKIN is converted from an autoinhibited enzyme into an active phospho-Ub-dependent E3 ligase. Upon activation, PARKIN ubiquitinates itself in concert with many different mitochondrial substrates. The Ub conjugates attached to these substrates can in turn be phosphorylated by PINK1, which triggers further cycles of PARKIN recruitment and activation. This feed-forward amplification loop regulates both PARKIN activity and mitophagy. However, the precise steps and sequence of PTMs in this cascade are only now being uncovered. For instance, the Ub conjugates assembled by PARKIN consist predominantly of noncanonical K6-linked Ub chains. Moreover, these modifications are reversible and can be disassembled by deubiquitinating enzymes (DUBs), including Ub-specific protease 8 (USP8), USP15, and USP30. However, PINK1-mediated phosphorylation of Ub can impede the activity of these DUBs, adding a new layer of complexity to the regulation of PARKIN-mediated mitophagy by PTMs. It is therefore evident that further insight into how PTMs regulate the PINK1-PARKIN pathway will be critical for our understanding of mitochondrial quality control.</AbstractText><CopyrightInformation>© 2015 Durcan and Fon; Published by Cold Spring Harbor Laboratory Press.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Durcan</LastName><ForeName>Thomas M</ForeName><Initials>TM</Initials><AffiliationInfo><Affiliation>McGill Parkinson's Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fon</LastName><ForeName>Edward A</ForeName><Initials>EA</Initials><AffiliationInfo><Affiliation>McGill Parkinson's Program, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec H3A 2B4, Canada ted.fon@mcgill.ca.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><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><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Genes Dev</MedlineTA><NlmUniqueID>8711660</NlmUniqueID><ISSNLinking>0890-9369</ISSNLinking></MedlineJournalInfo><ChemicalList><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><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C433927">PTEN-induced putative kinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Cell. 2001 Jun 29;105(7):891-902</RefSource><PMID Version="1">11439185</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2002 Aug 1;21(15):4037-48</RefSource><PMID Version="1">12145204</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Cell. 2002 Jul;10(1):55-67</RefSource><PMID Version="1">12150907</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):4078-83</RefSource><PMID 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RefType="Cites"><RefSource>Nat Neurosci. 2000 Dec;3(12):1301-6</RefSource><PMID Version="1">11100151</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008928" MajorTopicYN="N">Mitochondria</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D063306" MajorTopicYN="N">Mitochondrial Degradation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010300" MajorTopicYN="N">Parkinson Disease</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011499" MajorTopicYN="Y">Protein Processing, Post-Translational</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054875" MajorTopicYN="N">Ubiquitination</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4441056</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">PARKIN</Keyword><Keyword MajorTopicYN="N">PINK1</Keyword><Keyword MajorTopicYN="N">deubiquitination</Keyword><Keyword MajorTopicYN="N">mitophagy</Keyword><Keyword MajorTopicYN="N">phosphorylation</Keyword><Keyword MajorTopicYN="N">ubiquitin</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>5</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>5</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>7</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25995186</ArticleId><ArticleId IdType="pii">29/10/989</ArticleId><ArticleId IdType="doi">10.1101/gad.262758.115</ArticleId><ArticleId IdType="pmc">PMC4441056</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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