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
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :000D85
Links to Exploration step
pubmed:19875440Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><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>
</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 DateType="Electronic"><Year>2009</Year>
<Month>10</Month>
<Day>29</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>J Biol Chem</MedlineTA>
<NlmUniqueID>2985121R</NlmUniqueID>
<ISSNLinking>0021-9258</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D002135">Calcium-Binding Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C486206">EPS15 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D047908">Intracellular Signaling Peptides and Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C498506">PSMD4 protein, 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 Nov;6(3):277-93</RefSource>
<PMID Version="1">8520220</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Genet. 2000 Jul;25(3):302-5</RefSource>
<PMID Version="1">10888878</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Neuron. 2003 Mar 6;37(5):735-49</RefSource>
<PMID Version="1">12628165</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Neurochem. 2005 Jan;92(1):114-22</RefSource>
<PMID Version="1">15606901</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 1996 Jun;133(6):1331-46</RefSource>
<PMID Version="1">8682868</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Am J Hum Genet. 1997 Mar;60(3):588-96</RefSource>
<PMID Version="1">9042918</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO Rep. 2003 Mar;4(3):301-6</RefSource>
<PMID Version="1">12634850</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Trends Biochem Sci. 1996 May;21(5):172-3</RefSource>
<PMID Version="1">8871400</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Cell. 2009 Mar 27;33(6):775-83</RefSource>
<PMID Version="1">19328070</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Neuropharmacology. 2003 Jul;45(1):1-13</RefSource>
<PMID Version="1">12814656</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2003 Aug 1;278(31):28976-84</RefSource>
<PMID Version="1">12750381</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochem J. 2006 Nov 1;399(3):361-72</RefSource>
<PMID Version="1">17034365</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Med. 2001 Oct;7(10):1144-50</RefSource>
<PMID Version="1">11590439</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 1998 Apr 9;392(6676):605-8</RefSource>
<PMID Version="1">9560156</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Solid State Nucl Magn Reson. 2002 Dec;22(4):458-483</RefSource>
<PMID Version="1">12637147</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2003 Sep 15;22(18):4597-606</RefSource>
<PMID Version="1">12970172</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1985 Oct 15;260(23):12464-73</RefSource>
<PMID Version="1">2995377</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Cell Sci. 2005 Oct 1;118(Pt 19):4437-50</RefSource>
<PMID Version="1">16159959</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2009 May 29;284(22):14978-86</RefSource>
<PMID Version="1">19339245</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biomol NMR. 2003 Feb;25(2):153-6</RefSource>
<PMID Version="1">12652124</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Science. 2001 Jul 13;293(5528):263-9</RefSource>
<PMID Version="1">11431533</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Methods Enzymol. 1990;182:50-68</RefSource>
<PMID Version="1">2314256</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>FEBS Lett. 2004 May 21;566(1-3):110-4</RefSource>
<PMID Version="1">15147878</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 1992 Feb 18;31(6):1647-51</RefSource>
<PMID Version="1">1737021</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nature. 2002 Mar 28;416(6879):451-5</RefSource>
<PMID Version="1">11919637</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 2009 May 8;284(19):12622-32</RefSource>
<PMID Version="1">19240029</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2006 Jan 11;25(1):211-21</RefSource>
<PMID Version="1">16096643</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 2007 Dec 11;46(49):14162-9</RefSource>
<PMID Version="1">18004887</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13354-9</RefSource>
<PMID Version="1">11078524</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>FASEB J. 1997 Nov;11(13):1055-66</RefSource>
<PMID Version="1">9367341</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Trends Biochem Sci. 1999 Jun;24(6):229-31</RefSource>
<PMID Version="1">10366851</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Hum Mol Genet. 2003 Jun 15;12(12):1427-37</RefSource>
<PMID Version="1">12783850</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Trends Biochem Sci. 2001 Jun;26(6):347-50</RefSource>
<PMID Version="1">11406394</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biomol NMR. 2004 Oct;30(2):231-2</RefSource>
<PMID Version="1">15704274</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1996 Nov 15;271(46):28766-71</RefSource>
<PMID Version="1">8910518</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Biochemistry. 2002 Feb 12;41(6):1767-77</RefSource>
<PMID Version="1">11827521</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1999 Sep 24;274(39):28019-25</RefSource>
<PMID Version="1">10488153</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Rev Mol Cell Biol. 2005 Aug;6(8):610-21</RefSource>
<PMID Version="1">16064137</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Mol Cell Biol. 1997 Dec;17(12):6915-23</RefSource>
<PMID Version="1">9372923</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Physiol Rev. 2002 Apr;82(2):373-428</RefSource>
<PMID Version="1">11917093</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Cell. 2001 Jun 29;105(7):891-902</RefSource>
<PMID Version="1">11439185</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Biol Chem. 1998 Mar 6;273(10):5461-7</RefSource>
<PMID Version="1">9488668</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Semin Cell Dev Biol. 2004 Apr;15(2):247-59</RefSource>
<PMID Version="1">15209385</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>Nat Cell Biol. 2006 Aug;8(8):834-42</RefSource>
<PMID Version="1">16862145</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>J Mol Biol. 2005 May 6;348(3):727-39</RefSource>
<PMID Version="1">15826667</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="Cites"><RefSource>EMBO J. 2003 Sep 15;22(18):4634-45</RefSource>
<PMID 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)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Canada/explor/ParkinsonCanadaV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000D85 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 000D85 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Canada |area= ParkinsonCanadaV1 |flux= PubMed |étape= Curation |type= RBID |clé= pubmed:19875440 |texte= Differential interaction of the E3 ligase parkin with the proteasomal subunit S5a and the endocytic protein Eps15. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:19875440" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \ | NlmPubMed2Wicri -a ParkinsonCanadaV1
![]() | This area was generated with Dilib version V0.6.29. | ![]() |