Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1.
Identifieur interne : 000258 ( PubMed/Corpus ); précédent : 000257; suivant : 000259Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1.
Auteurs : Yu-Chiang Lai ; Chandana Kondapalli ; Ronny Lehneck ; James B. Procter ; Brian D. Dill ; Helen I. Woodroof ; Robert Gourlay ; Mark Peggie ; Thomas J. Macartney ; Olga Corti ; Jean-Christophe Corvol ; David G. Campbell ; Aymelt Itzen ; Matthias Trost ; Miratul Mk MuqitSource :
- The EMBO journal [ 1460-2075 ] ; 2015.
English descriptors
- KwdEn :
- Amino Acid Substitution, Enzyme Activation (genetics), HEK293 Cells, HeLa Cells, Humans, Mutation, Missense, Oncogene Proteins (genetics), Oncogene Proteins (metabolism), Parkinsonian Disorders (genetics), Parkinsonian Disorders (metabolism), Parkinsonian Disorders (pathology), Phosphorylation (genetics), Protein Kinases (genetics), Protein Kinases (metabolism), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), rab GTP-Binding Proteins (genetics), rab GTP-Binding Proteins (metabolism).
- MESH :
- chemical , genetics : Oncogene Proteins, Protein Kinases, Protein-Serine-Threonine Kinases, rab GTP-Binding Proteins.
- genetics : Enzyme Activation, Parkinsonian Disorders, Phosphorylation.
- chemical , metabolism : Oncogene Proteins, Parkinsonian Disorders, Protein Kinases, Protein-Serine-Threonine Kinases, rab GTP-Binding Proteins.
- pathology : Parkinsonian Disorders.
- Amino Acid Substitution, HEK293 Cells, HeLa Cells, Humans, Mutation, Missense.
Abstract
Mutations in the PTEN-induced kinase 1 (PINK1) are causative of autosomal recessive Parkinson's disease (PD). We have previously reported that PINK1 is activated by mitochondrial depolarisation and phosphorylates serine 65 (Ser(65)) of the ubiquitin ligase Parkin and ubiquitin to stimulate Parkin E3 ligase activity. Here, we have employed quantitative phosphoproteomics to search for novel PINK1-dependent phosphorylation targets in HEK (human embryonic kidney) 293 cells stimulated by mitochondrial depolarisation. This led to the identification of 14,213 phosphosites from 4,499 gene products. Whilst most phosphosites were unaffected, we strikingly observed three members of a sub-family of Rab GTPases namely Rab8A, 8B and 13 that are all phosphorylated at the highly conserved residue of serine 111 (Ser(111)) in response to PINK1 activation. Using phospho-specific antibodies raised against Ser(111) of each of the Rabs, we demonstrate that Rab Ser(111) phosphorylation occurs specifically in response to PINK1 activation and is abolished in HeLa PINK1 knockout cells and mutant PINK1 PD patient-derived fibroblasts stimulated by mitochondrial depolarisation. We provide evidence that Rab8A GTPase Ser(111) phosphorylation is not directly regulated by PINK1 in vitro and demonstrate in cells the time course of Ser(111) phosphorylation of Rab8A, 8B and 13 is markedly delayed compared to phosphorylation of Parkin at Ser(65). We further show mechanistically that phosphorylation at Ser(111) significantly impairs Rab8A activation by its cognate guanine nucleotide exchange factor (GEF), Rabin8 (by using the Ser111Glu phosphorylation mimic). These findings provide the first evidence that PINK1 is able to regulate the phosphorylation of Rab GTPases and indicate that monitoring phosphorylation of Rab8A/8B/13 at Ser(111) may represent novel biomarkers of PINK1 activity in vivo. Our findings also suggest that disruption of Rab GTPase-mediated signalling may represent a major mechanism in the neurodegenerative cascade of Parkinson's disease.
DOI: 10.15252/embj.201591593
PubMed: 26471730
Links to Exploration step
pubmed:26471730Le document en format XML
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Procter</name><affiliation><nlm:affiliation>Division of Computational Biology, College of Life Sciences University of Dundee, Dundee, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Dill, Brian D" sort="Dill, Brian D" uniqKey="Dill B" first="Brian D" last="Dill">Brian D. Dill</name><affiliation><nlm:affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Woodroof, Helen I" sort="Woodroof, Helen I" uniqKey="Woodroof H" first="Helen I" last="Woodroof">Helen I. Woodroof</name><affiliation><nlm:affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Gourlay, Robert" sort="Gourlay, Robert" uniqKey="Gourlay R" first="Robert" last="Gourlay">Robert Gourlay</name><affiliation><nlm:affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Peggie, Mark" sort="Peggie, Mark" uniqKey="Peggie M" first="Mark" last="Peggie">Mark Peggie</name><affiliation><nlm:affiliation>Division of Signal Transduction Therapy, College of Life Sciences University of Dundee, Dundee, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Macartney, Thomas J" sort="Macartney, Thomas J" uniqKey="Macartney T" first="Thomas J" last="Macartney">Thomas J. Macartney</name><affiliation><nlm:affiliation>Division of Signal Transduction Therapy, College of Life Sciences University of Dundee, Dundee, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Corti, Olga" sort="Corti, Olga" uniqKey="Corti O" first="Olga" last="Corti">Olga Corti</name><affiliation><nlm:affiliation>Inserm U 1127, Paris, France CNRS UMR 7225, Paris, France Sorbonne Universités UPMC Paris 06 UMR S 1127, Paris, France Institut du Cerveau et de la Moelle épinière ICM, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Corvol, Jean Christophe" sort="Corvol, Jean Christophe" uniqKey="Corvol J" first="Jean-Christophe" last="Corvol">Jean-Christophe Corvol</name><affiliation><nlm:affiliation>Inserm U 1127, Paris, France CNRS UMR 7225, Paris, France Sorbonne Universités UPMC Paris 06 UMR S 1127, Paris, France Institut du Cerveau et de la Moelle épinière ICM, Paris, France Inserm Centre d'Investigation Clinique (CIC), Paris, France AP-HP, Département des maladies du système nerveux, Hôpital de la Pitié-Salpêtrière, Paris, France.</nlm:affiliation></affiliation></author><author><name sortKey="Campbell, David G" sort="Campbell, David G" uniqKey="Campbell D" first="David G" last="Campbell">David G. Campbell</name><affiliation><nlm:affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Itzen, Aymelt" sort="Itzen, Aymelt" uniqKey="Itzen A" first="Aymelt" last="Itzen">Aymelt Itzen</name><affiliation><nlm:affiliation>Centre for Integrated Protein Science Munich, Department Chemistry Technische Universität München, Garching, Germany.</nlm:affiliation></affiliation></author><author><name sortKey="Trost, Matthias" sort="Trost, Matthias" uniqKey="Trost M" first="Matthias" last="Trost">Matthias Trost</name><affiliation><nlm:affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK m.trost@dundee.ac.uk m.muqit@dundee.ac.uk.</nlm:affiliation></affiliation></author><author><name sortKey="Muqit, Miratul Mk" sort="Muqit, Miratul Mk" uniqKey="Muqit M" first="Miratul Mk" last="Muqit">Miratul Mk Muqit</name><affiliation><nlm:affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK College of Medicine, Dentistry & Nursing, University of Dundee, Dundee, UK m.trost@dundee.ac.uk m.muqit@dundee.ac.uk.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The EMBO journal</title><idno type="eISSN">1460-2075</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Enzyme Activation (genetics)</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Mutation, Missense</term><term>Oncogene Proteins (genetics)</term><term>Oncogene Proteins (metabolism)</term><term>Parkinsonian Disorders (genetics)</term><term>Parkinsonian Disorders (metabolism)</term><term>Parkinsonian Disorders (pathology)</term><term>Phosphorylation (genetics)</term><term>Protein Kinases (genetics)</term><term>Protein Kinases (metabolism)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>rab GTP-Binding Proteins (genetics)</term><term>rab GTP-Binding Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Oncogene Proteins</term><term>Protein Kinases</term><term>Protein-Serine-Threonine Kinases</term><term>rab GTP-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Enzyme Activation</term><term>Parkinsonian Disorders</term><term>Phosphorylation</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oncogene Proteins</term><term>Parkinsonian Disorders</term><term>Protein Kinases</term><term>Protein-Serine-Threonine Kinases</term><term>rab GTP-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Parkinsonian Disorders</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>HEK293 Cells</term><term>HeLa Cells</term><term>Humans</term><term>Mutation, Missense</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mutations in the PTEN-induced kinase 1 (PINK1) are causative of autosomal recessive Parkinson's disease (PD). We have previously reported that PINK1 is activated by mitochondrial depolarisation and phosphorylates serine 65 (Ser(65)) of the ubiquitin ligase Parkin and ubiquitin to stimulate Parkin E3 ligase activity. Here, we have employed quantitative phosphoproteomics to search for novel PINK1-dependent phosphorylation targets in HEK (human embryonic kidney) 293 cells stimulated by mitochondrial depolarisation. This led to the identification of 14,213 phosphosites from 4,499 gene products. Whilst most phosphosites were unaffected, we strikingly observed three members of a sub-family of Rab GTPases namely Rab8A, 8B and 13 that are all phosphorylated at the highly conserved residue of serine 111 (Ser(111)) in response to PINK1 activation. Using phospho-specific antibodies raised against Ser(111) of each of the Rabs, we demonstrate that Rab Ser(111) phosphorylation occurs specifically in response to PINK1 activation and is abolished in HeLa PINK1 knockout cells and mutant PINK1 PD patient-derived fibroblasts stimulated by mitochondrial depolarisation. We provide evidence that Rab8A GTPase Ser(111) phosphorylation is not directly regulated by PINK1 in vitro and demonstrate in cells the time course of Ser(111) phosphorylation of Rab8A, 8B and 13 is markedly delayed compared to phosphorylation of Parkin at Ser(65). We further show mechanistically that phosphorylation at Ser(111) significantly impairs Rab8A activation by its cognate guanine nucleotide exchange factor (GEF), Rabin8 (by using the Ser111Glu phosphorylation mimic). These findings provide the first evidence that PINK1 is able to regulate the phosphorylation of Rab GTPases and indicate that monitoring phosphorylation of Rab8A/8B/13 at Ser(111) may represent novel biomarkers of PINK1 activity in vivo. Our findings also suggest that disruption of Rab GTPase-mediated signalling may represent a major mechanism in the neurodegenerative cascade of Parkinson's disease.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26471730</PMID><DateCreated><Year>2015</Year><Month>11</Month><Day>13</Day></DateCreated><DateCompleted><Year>2016</Year><Month>02</Month><Day>22</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1460-2075</ISSN><JournalIssue CitedMedium="Internet"><Volume>34</Volume><Issue>22</Issue><PubDate><Year>2015</Year><Month>Nov</Month><Day>12</Day></PubDate></JournalIssue><Title>The EMBO journal</Title><ISOAbbreviation>EMBO J.</ISOAbbreviation></Journal><ArticleTitle>Phosphoproteomic screening identifies Rab GTPases as novel downstream targets of PINK1.</ArticleTitle><Pagination><MedlinePgn>2840-61</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.15252/embj.201591593</ELocationID><Abstract><AbstractText>Mutations in the PTEN-induced kinase 1 (PINK1) are causative of autosomal recessive Parkinson's disease (PD). We have previously reported that PINK1 is activated by mitochondrial depolarisation and phosphorylates serine 65 (Ser(65)) of the ubiquitin ligase Parkin and ubiquitin to stimulate Parkin E3 ligase activity. Here, we have employed quantitative phosphoproteomics to search for novel PINK1-dependent phosphorylation targets in HEK (human embryonic kidney) 293 cells stimulated by mitochondrial depolarisation. This led to the identification of 14,213 phosphosites from 4,499 gene products. Whilst most phosphosites were unaffected, we strikingly observed three members of a sub-family of Rab GTPases namely Rab8A, 8B and 13 that are all phosphorylated at the highly conserved residue of serine 111 (Ser(111)) in response to PINK1 activation. Using phospho-specific antibodies raised against Ser(111) of each of the Rabs, we demonstrate that Rab Ser(111) phosphorylation occurs specifically in response to PINK1 activation and is abolished in HeLa PINK1 knockout cells and mutant PINK1 PD patient-derived fibroblasts stimulated by mitochondrial depolarisation. We provide evidence that Rab8A GTPase Ser(111) phosphorylation is not directly regulated by PINK1 in vitro and demonstrate in cells the time course of Ser(111) phosphorylation of Rab8A, 8B and 13 is markedly delayed compared to phosphorylation of Parkin at Ser(65). We further show mechanistically that phosphorylation at Ser(111) significantly impairs Rab8A activation by its cognate guanine nucleotide exchange factor (GEF), Rabin8 (by using the Ser111Glu phosphorylation mimic). These findings provide the first evidence that PINK1 is able to regulate the phosphorylation of Rab GTPases and indicate that monitoring phosphorylation of Rab8A/8B/13 at Ser(111) may represent novel biomarkers of PINK1 activity in vivo. Our findings also suggest that disruption of Rab GTPase-mediated signalling may represent a major mechanism in the neurodegenerative cascade of Parkinson's disease.</AbstractText><CopyrightInformation>© 2015 The Authors. Published under the terms of the CC BY 4.0 license.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lai</LastName><ForeName>Yu-Chiang</ForeName><Initials>YC</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kondapalli</LastName><ForeName>Chandana</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lehneck</LastName><ForeName>Ronny</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Centre for Integrated Protein Science Munich, Department Chemistry Technische Universität München, Garching, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Procter</LastName><ForeName>James B</ForeName><Initials>JB</Initials><AffiliationInfo><Affiliation>Division of Computational Biology, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dill</LastName><ForeName>Brian D</ForeName><Initials>BD</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Woodroof</LastName><ForeName>Helen I</ForeName><Initials>HI</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gourlay</LastName><ForeName>Robert</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Peggie</LastName><ForeName>Mark</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Division of Signal Transduction Therapy, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Macartney</LastName><ForeName>Thomas J</ForeName><Initials>TJ</Initials><AffiliationInfo><Affiliation>Division of Signal Transduction Therapy, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Corti</LastName><ForeName>Olga</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Inserm U 1127, Paris, France CNRS UMR 7225, Paris, France Sorbonne Universités UPMC Paris 06 UMR S 1127, Paris, France Institut du Cerveau et de la Moelle épinière ICM, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Corvol</LastName><ForeName>Jean-Christophe</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>Inserm U 1127, Paris, France CNRS UMR 7225, Paris, France Sorbonne Universités UPMC Paris 06 UMR S 1127, Paris, France Institut du Cerveau et de la Moelle épinière ICM, Paris, France Inserm Centre d'Investigation Clinique (CIC), Paris, France AP-HP, Département des maladies du système nerveux, Hôpital de la Pitié-Salpêtrière, Paris, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Campbell</LastName><ForeName>David G</ForeName><Initials>DG</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Itzen</LastName><ForeName>Aymelt</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Centre for Integrated Protein Science Munich, Department Chemistry Technische Universität München, Garching, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Trost</LastName><ForeName>Matthias</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK m.trost@dundee.ac.uk m.muqit@dundee.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Muqit</LastName><ForeName>Miratul Mk</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences University of Dundee, Dundee, UK College of Medicine, Dentistry & Nursing, University of Dundee, Dundee, UK m.trost@dundee.ac.uk m.muqit@dundee.ac.uk.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>101022/Z/13/Z</GrantID><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>BB/L020742/1</GrantID><Agency>Biotechnology and Biological Sciences Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>101022</GrantID><Agency>Wellcome Trust</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>MC_UP_A500_1020</GrantID><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>G1100713</GrantID><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>MC_UU_12016/5</GrantID><Agency>Medical Research Council</Agency><Country>United Kingdom</Country></Grant><Grant><GrantID>P41-GM103311</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>10</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>EMBO J</MedlineTA><NlmUniqueID>8208664</NlmUniqueID><ISSNLinking>0261-4189</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015513">Oncogene Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C529761">Rab8b protein, human</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><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine 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Version="1">24297252</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D019943" MajorTopicYN="N">Amino Acid Substitution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004789" MajorTopicYN="N">Enzyme Activation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020125" MajorTopicYN="N">Mutation, Missense</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015513" MajorTopicYN="N">Oncogene Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020734" MajorTopicYN="N">Parkinsonian Disorders</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></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="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020691" MajorTopicYN="N">rab GTP-Binding Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4654935</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">PINK1</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">Rab GTPases</Keyword><Keyword MajorTopicYN="N">phosphoproteomics</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>03</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>09</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>10</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>10</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>2</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26471730</ArticleId><ArticleId IdType="pii">embj.201591593</ArticleId><ArticleId IdType="doi">10.15252/embj.201591593</ArticleId><ArticleId IdType="pmc">PMC4654935</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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