Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.
Identifieur interne : 000D85 ( PubMed/Curation ); précédent : 000D84; suivant : 000D86Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.
Auteurs : Susan S. Safadi [Canada] ; Gary S. ShawSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2010.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing, Amino Acid Motifs (genetics), Amino Acid Substitution, Calcium-Binding Proteins (chemistry), Calcium-Binding Proteins (genetics), Calcium-Binding Proteins (metabolism), Humans, Intracellular Signaling Peptides and Proteins (chemistry), Intracellular Signaling Peptides and Proteins (genetics), Intracellular Signaling Peptides and Proteins (metabolism), Magnetic Resonance Spectroscopy, Mutation, Missense, Parkinsonian Disorders (enzymology), Parkinsonian Disorders (genetics), Phosphoproteins (chemistry), Phosphoproteins (genetics), Phosphoproteins (metabolism), Proteasome Endopeptidase Complex (chemistry), Proteasome Endopeptidase Complex (genetics), Proteasome Endopeptidase Complex (metabolism), Signal Transduction (genetics), Ubiquitin-Protein Ligases (chemistry), Ubiquitin-Protein Ligases (genetics), Ubiquitin-Protein Ligases (metabolism), Ubiquitination.
- MESH :
- chemical , chemistry : Calcium-Binding Proteins, Intracellular Signaling Peptides and Proteins, Phosphoproteins, Proteasome Endopeptidase Complex, Ubiquitin-Protein Ligases.
- chemical , genetics : Calcium-Binding Proteins, Intracellular Signaling Peptides and Proteins, Phosphoproteins, Proteasome Endopeptidase Complex, Ubiquitin-Protein Ligases.
- chemical , metabolism : Calcium-Binding Proteins, Intracellular Signaling Peptides and Proteins, Phosphoproteins, Proteasome Endopeptidase Complex, Ubiquitin-Protein Ligases.
- chemical : Adaptor Proteins, Signal Transducing.
- enzymology : Parkinsonian Disorders.
- genetics : Amino Acid Motifs, Parkinsonian Disorders, Signal Transduction.
- Amino Acid Substitution, Humans, Magnetic Resonance Spectroscopy, Mutation, Missense, Ubiquitination.
Abstract
Parkin is a multidomain E3 ligase associated with autosomal recessive Parkinson disease. The N-terminal ubiquitin-like domain (Ubld) of parkin functions with the S5a proteasomal subunit, positioning substrate proteins for degradation. In addition the parkin Ubld recruits the endocytotic protein Eps15, allowing the E3 ligase to ubiquinate Eps15 distal from its parkin-interacting site. The recognition sequences in the S5a subunit and Eps15 for the parkin Ubld are ubiquitin-interacting motifs (UIM). Each protein has two UIM sequences separated by a 50-residue spacer in S5a, but only approximately 5 residues in Eps15. In this work we used NMR spectroscopy to determine how the parkin Ubld recognizes the proteasomal subunit S5a compared with Eps15, a substrate for ubiquitination. We show that Eps15 contains two flexible alpha-helices each encompassing a UIM sequence. The alpha-helix surrounding UIM II is longer than that for UIM I, a situation that is reversed from S5a. Furthermore, we show the parkin Ubld preferentially binds to UIM I in the S5a subunit. This interaction is strongly diminished in a K48A substitution, found near the center of the S5a interacting surface on the parkin Ubld. In contrast to S5a, parkin recruits Eps15 using both its UIM sequences resulting in a larger interaction surface that includes residues from beta1 and beta2, not typically known to interact with UIM sequences. These results show that the parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.
DOI: 10.1074/jbc.M109.041970
PubMed: 19875440
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pubmed:19875440Le document en format XML
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Shaw</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:19875440</idno><idno type="pmid">19875440</idno><idno type="doi">10.1074/jbc.M109.041970</idno><idno type="wicri:Area/PubMed/Corpus">000D85</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000D85</idno><idno type="wicri:Area/PubMed/Curation">000D85</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000D85</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.</title><author><name sortKey="Safadi, Susan S" sort="Safadi, Susan S" uniqKey="Safadi S" first="Susan S" last="Safadi">Susan S. Safadi</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada.</nlm:affiliation><country xml:lang="fr">Canada</country><wicri:regionArea>Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1</wicri:regionArea></affiliation></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">The Journal of biological chemistry</title><idno type="eISSN">1083-351X</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Amino Acid Motifs (genetics)</term><term>Amino Acid Substitution</term><term>Calcium-Binding Proteins (chemistry)</term><term>Calcium-Binding Proteins (genetics)</term><term>Calcium-Binding Proteins (metabolism)</term><term>Humans</term><term>Intracellular Signaling Peptides and Proteins (chemistry)</term><term>Intracellular Signaling Peptides and Proteins (genetics)</term><term>Intracellular Signaling Peptides and Proteins (metabolism)</term><term>Magnetic Resonance Spectroscopy</term><term>Mutation, Missense</term><term>Parkinsonian Disorders (enzymology)</term><term>Parkinsonian Disorders (genetics)</term><term>Phosphoproteins (chemistry)</term><term>Phosphoproteins (genetics)</term><term>Phosphoproteins (metabolism)</term><term>Proteasome Endopeptidase Complex (chemistry)</term><term>Proteasome Endopeptidase Complex (genetics)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Signal Transduction (genetics)</term><term>Ubiquitin-Protein Ligases (chemistry)</term><term>Ubiquitin-Protein Ligases (genetics)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Calcium-Binding Proteins</term><term>Intracellular Signaling Peptides and Proteins</term><term>Phosphoproteins</term><term>Proteasome Endopeptidase Complex</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Calcium-Binding Proteins</term><term>Intracellular Signaling Peptides and Proteins</term><term>Phosphoproteins</term><term>Proteasome Endopeptidase Complex</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium-Binding Proteins</term><term>Intracellular Signaling Peptides and Proteins</term><term>Phosphoproteins</term><term>Proteasome Endopeptidase Complex</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Parkinsonian Disorders</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Amino Acid Motifs</term><term>Parkinsonian Disorders</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Humans</term><term>Magnetic Resonance Spectroscopy</term><term>Mutation, Missense</term><term>Ubiquitination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Parkin is a multidomain E3 ligase associated with autosomal recessive Parkinson disease. The N-terminal ubiquitin-like domain (Ubld) of parkin functions with the S5a proteasomal subunit, positioning substrate proteins for degradation. In addition the parkin Ubld recruits the endocytotic protein Eps15, allowing the E3 ligase to ubiquinate Eps15 distal from its parkin-interacting site. The recognition sequences in the S5a subunit and Eps15 for the parkin Ubld are ubiquitin-interacting motifs (UIM). Each protein has two UIM sequences separated by a 50-residue spacer in S5a, but only approximately 5 residues in Eps15. In this work we used NMR spectroscopy to determine how the parkin Ubld recognizes the proteasomal subunit S5a compared with Eps15, a substrate for ubiquitination. We show that Eps15 contains two flexible alpha-helices each encompassing a UIM sequence. The alpha-helix surrounding UIM II is longer than that for UIM I, a situation that is reversed from S5a. Furthermore, we show the parkin Ubld preferentially binds to UIM I in the S5a subunit. This interaction is strongly diminished in a K48A substitution, found near the center of the S5a interacting surface on the parkin Ubld. In contrast to S5a, parkin recruits Eps15 using both its UIM sequences resulting in a larger interaction surface that includes residues from beta1 and beta2, not typically known to interact with UIM sequences. These results show that the parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19875440</PMID><DateCreated><Year>2010</Year><Month>01</Month><Day>04</Day></DateCreated><DateCompleted><Year>2010</Year><Month>01</Month><Day>26</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>285</Volume><Issue>2</Issue><PubDate><Year>2010</Year><Month>Jan</Month><Day>08</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. Chem.</ISOAbbreviation></Journal><ArticleTitle>Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15.</ArticleTitle><Pagination><MedlinePgn>1424-34</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1074/jbc.M109.041970</ELocationID><Abstract><AbstractText>Parkin is a multidomain E3 ligase associated with autosomal recessive Parkinson disease. The N-terminal ubiquitin-like domain (Ubld) of parkin functions with the S5a proteasomal subunit, positioning substrate proteins for degradation. In addition the parkin Ubld recruits the endocytotic protein Eps15, allowing the E3 ligase to ubiquinate Eps15 distal from its parkin-interacting site. The recognition sequences in the S5a subunit and Eps15 for the parkin Ubld are ubiquitin-interacting motifs (UIM). Each protein has two UIM sequences separated by a 50-residue spacer in S5a, but only approximately 5 residues in Eps15. In this work we used NMR spectroscopy to determine how the parkin Ubld recognizes the proteasomal subunit S5a compared with Eps15, a substrate for ubiquitination. We show that Eps15 contains two flexible alpha-helices each encompassing a UIM sequence. The alpha-helix surrounding UIM II is longer than that for UIM I, a situation that is reversed from S5a. Furthermore, we show the parkin Ubld preferentially binds to UIM I in the S5a subunit. This interaction is strongly diminished in a K48A substitution, found near the center of the S5a interacting surface on the parkin Ubld. In contrast to S5a, parkin recruits Eps15 using both its UIM sequences resulting in a larger interaction surface that includes residues from beta1 and beta2, not typically known to interact with UIM sequences. These results show that the parkin Ubld uses differential surfaces to recruit UIM regions from the S5a proteasomal subunit compared with Eps15 involved in cell signaling.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Safadi</LastName><ForeName>Susan S</ForeName><Initials>SS</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shaw</LastName><ForeName>Gary S</ForeName><Initials>GS</Initials></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></PublicationTypeList><ArticleDate 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human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010750">Phosphoproteins</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><Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber><NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Annu Rev Biochem. 1998;67:425-79</RefSource><PMID Version="1">9759494</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Methods Mol Biol. 2004;278:313-52</RefSource><PMID Version="1">15318002</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Biomol NMR. 1995 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Version="1">12970176</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D048868" MajorTopicYN="N">Adaptor Proteins, Signal Transducing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002135" MajorTopicYN="N">Calcium-Binding Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047908" MajorTopicYN="N">Intracellular Signaling Peptides and Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009682" MajorTopicYN="N">Magnetic Resonance Spectroscopy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020125" MajorTopicYN="N">Mutation, Missense</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020734" MajorTopicYN="N">Parkinsonian Disorders</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046988" MajorTopicYN="N">Proteasome Endopeptidase Complex</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054875" MajorTopicYN="Y">Ubiquitination</DescriptorName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC2801268</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2009</Year><Month>10</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2009</Year><Month>10</Month><Day>31</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2010</Year><Month>1</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">19875440</ArticleId><ArticleId IdType="pii">M109.041970</ArticleId><ArticleId IdType="doi">10.1074/jbc.M109.041970</ArticleId><ArticleId IdType="pmc">PMC2801268</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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