LRRK2 localizes to endosomes and interacts with clathrin-light chains to limit Rac1 activation.
Identifieur interne : 000595 ( PubMed/Corpus ); précédent : 000594; suivant : 000596LRRK2 localizes to endosomes and interacts with clathrin-light chains to limit Rac1 activation.
Auteurs : Andrea M A. Schreij ; Mathilde Chaineau ; Wenjing Ruan ; Susan Lin ; Philip A. Barker ; Edward A. Fon ; Peter S. McphersonSource :
- EMBO reports [ 1469-3178 ] ; 2015.
English descriptors
- KwdEn :
- Animals, Animals, Genetically Modified, Base Sequence, Brain (cytology), Brain (metabolism), COS Cells, Cells, Cultured, Cercopithecus aethiops, Clathrin Light Chains (genetics), Clathrin Light Chains (metabolism), Drosophila Proteins (genetics), Drosophila Proteins (metabolism), Drosophila melanogaster (genetics), Endosomes (metabolism), Eye (metabolism), Eye (pathology), Gene Knockdown Techniques, Humans, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Molecular Sequence Data, Neurons (metabolism), Neurons (pathology), Protein Structure, Tertiary, Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Rats, rac1 GTP-Binding Protein (genetics), rac1 GTP-Binding Protein (metabolism).
- MESH :
- chemical , genetics : Clathrin Light Chains, Drosophila Proteins, Protein-Serine-Threonine Kinases, rac1 GTP-Binding Protein.
- cytology : Brain.
- genetics : Drosophila melanogaster.
- metabolism : Brain, Clathrin Light Chains, Drosophila Proteins, Endosomes, Eye, Neurons, Protein-Serine-Threonine Kinases, rac1 GTP-Binding Protein.
- pathology : Eye, Neurons.
- Animals, Animals, Genetically Modified, Base Sequence, COS Cells, Cells, Cultured, Cercopithecus aethiops, Gene Knockdown Techniques, Humans, Leucine-Rich Repeat Serine-Threonine Protein Kinase-2, Molecular Sequence Data, Protein Structure, Tertiary, Rats.
Abstract
Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of dominant-inherited Parkinson's disease (PD), and yet we do not fully understand the physiological function(s) of LRRK2. Various components of the clathrin machinery have been recently found mutated in familial forms of PD. Here, we provide molecular insight into the association of LRRK2 with the clathrin machinery. We report that through its GTPase domain, LRRK2 binds directly to clathrin-light chains (CLCs). Using genome-edited HA-LRRK2 cells, we localize LRRK2 to endosomes on the degradative pathway, where it partially co-localizes with CLCs. Knockdown of CLCs and/or LRRK2 enhances the activation of the small GTPase Rac1, leading to alterations in cell morphology, including the disruption of neuronal dendritic spines. In Drosphila, a minimal rough eye phenotype caused by overexpression of Rac1, is dramatically enhanced by loss of function of CLC and LRRK2 homologues, confirming the importance of this pathway in vivo. Our data identify a new pathway in which CLCs function with LRRK2 to control Rac1 activation on endosomes, providing a new link between the clathrin machinery, the cytoskeleton and PD.
DOI: 10.15252/embr.201438714
PubMed: 25427558
Links to Exploration step
pubmed:25427558Le document en format XML
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Schreij</name><affiliation><nlm:affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Chaineau, Mathilde" sort="Chaineau, Mathilde" uniqKey="Chaineau M" first="Mathilde" last="Chaineau">Mathilde Chaineau</name><affiliation><nlm:affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Ruan, Wenjing" sort="Ruan, Wenjing" uniqKey="Ruan W" first="Wenjing" last="Ruan">Wenjing Ruan</name><affiliation><nlm:affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Lin, Susan" sort="Lin, Susan" uniqKey="Lin S" first="Susan" last="Lin">Susan Lin</name><affiliation><nlm:affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Barker, Philip A" sort="Barker, Philip A" uniqKey="Barker P" first="Philip A" last="Barker">Philip A. 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Barker</name><affiliation><nlm:affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Fon, Edward A" sort="Fon, Edward A" uniqKey="Fon E" first="Edward A" last="Fon">Edward A. Fon</name><affiliation><nlm:affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada ted.fon@mcgill.ca peter.mcpherson@mcgill.ca.</nlm:affiliation></affiliation></author><author><name sortKey="Mcpherson, Peter S" sort="Mcpherson, Peter S" uniqKey="Mcpherson P" first="Peter S" last="Mcpherson">Peter S. Mcpherson</name><affiliation><nlm:affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada ted.fon@mcgill.ca peter.mcpherson@mcgill.ca.</nlm:affiliation></affiliation></author></analytic><series><title level="j">EMBO reports</title><idno type="eISSN">1469-3178</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Animals, Genetically Modified</term><term>Base Sequence</term><term>Brain (cytology)</term><term>Brain (metabolism)</term><term>COS Cells</term><term>Cells, Cultured</term><term>Cercopithecus aethiops</term><term>Clathrin Light Chains (genetics)</term><term>Clathrin Light Chains (metabolism)</term><term>Drosophila Proteins (genetics)</term><term>Drosophila Proteins (metabolism)</term><term>Drosophila melanogaster (genetics)</term><term>Endosomes (metabolism)</term><term>Eye (metabolism)</term><term>Eye (pathology)</term><term>Gene Knockdown Techniques</term><term>Humans</term><term>Leucine-Rich Repeat Serine-Threonine Protein Kinase-2</term><term>Molecular Sequence Data</term><term>Neurons (metabolism)</term><term>Neurons (pathology)</term><term>Protein Structure, Tertiary</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Rats</term><term>rac1 GTP-Binding Protein (genetics)</term><term>rac1 GTP-Binding Protein (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Clathrin Light Chains</term><term>Drosophila Proteins</term><term>Protein-Serine-Threonine Kinases</term><term>rac1 GTP-Binding Protein</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Brain</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Drosophila melanogaster</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Brain</term><term>Clathrin Light Chains</term><term>Drosophila Proteins</term><term>Endosomes</term><term>Eye</term><term>Neurons</term><term>Protein-Serine-Threonine Kinases</term><term>rac1 GTP-Binding Protein</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Eye</term><term>Neurons</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Animals, Genetically Modified</term><term>Base Sequence</term><term>COS Cells</term><term>Cells, Cultured</term><term>Cercopithecus aethiops</term><term>Gene Knockdown Techniques</term><term>Humans</term><term>Leucine-Rich Repeat Serine-Threonine Protein Kinase-2</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of dominant-inherited Parkinson's disease (PD), and yet we do not fully understand the physiological function(s) of LRRK2. Various components of the clathrin machinery have been recently found mutated in familial forms of PD. Here, we provide molecular insight into the association of LRRK2 with the clathrin machinery. We report that through its GTPase domain, LRRK2 binds directly to clathrin-light chains (CLCs). Using genome-edited HA-LRRK2 cells, we localize LRRK2 to endosomes on the degradative pathway, where it partially co-localizes with CLCs. Knockdown of CLCs and/or LRRK2 enhances the activation of the small GTPase Rac1, leading to alterations in cell morphology, including the disruption of neuronal dendritic spines. In Drosphila, a minimal rough eye phenotype caused by overexpression of Rac1, is dramatically enhanced by loss of function of CLC and LRRK2 homologues, confirming the importance of this pathway in vivo. Our data identify a new pathway in which CLCs function with LRRK2 to control Rac1 activation on endosomes, providing a new link between the clathrin machinery, the cytoskeleton and PD.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25427558</PMID><DateCreated><Year>2015</Year><Month>01</Month><Day>06</Day></DateCreated><DateCompleted><Year>2015</Year><Month>07</Month><Day>27</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-3178</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>1</Issue><PubDate><Year>2015</Year><Month>Jan</Month></PubDate></JournalIssue><Title>EMBO reports</Title><ISOAbbreviation>EMBO Rep.</ISOAbbreviation></Journal><ArticleTitle>LRRK2 localizes to endosomes and interacts with clathrin-light chains to limit Rac1 activation.</ArticleTitle><Pagination><MedlinePgn>79-86</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.15252/embr.201438714</ELocationID><Abstract><AbstractText>Mutations in leucine-rich repeat kinase 2 (LRRK2) are the most common cause of dominant-inherited Parkinson's disease (PD), and yet we do not fully understand the physiological function(s) of LRRK2. Various components of the clathrin machinery have been recently found mutated in familial forms of PD. Here, we provide molecular insight into the association of LRRK2 with the clathrin machinery. We report that through its GTPase domain, LRRK2 binds directly to clathrin-light chains (CLCs). Using genome-edited HA-LRRK2 cells, we localize LRRK2 to endosomes on the degradative pathway, where it partially co-localizes with CLCs. Knockdown of CLCs and/or LRRK2 enhances the activation of the small GTPase Rac1, leading to alterations in cell morphology, including the disruption of neuronal dendritic spines. In Drosphila, a minimal rough eye phenotype caused by overexpression of Rac1, is dramatically enhanced by loss of function of CLC and LRRK2 homologues, confirming the importance of this pathway in vivo. Our data identify a new pathway in which CLCs function with LRRK2 to control Rac1 activation on endosomes, providing a new link between the clathrin machinery, the cytoskeleton and PD.</AbstractText><CopyrightInformation>© 2014 The Authors.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Schreij</LastName><ForeName>Andrea M A</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chaineau</LastName><ForeName>Mathilde</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ruan</LastName><ForeName>Wenjing</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lin</LastName><ForeName>Susan</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barker</LastName><ForeName>Philip A</ForeName><Initials>PA</Initials><AffiliationInfo><Affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fon</LastName><ForeName>Edward A</ForeName><Initials>EA</Initials><AffiliationInfo><Affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada ted.fon@mcgill.ca peter.mcpherson@mcgill.ca.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McPherson</LastName><ForeName>Peter S</ForeName><Initials>PS</Initials><AffiliationInfo><Affiliation>Department of Neurology and Neurosurgery and McGill Parkinson Program, Montreal Neurological Institute McGill University, Montreal, Quebec, Canada ted.fon@mcgill.ca peter.mcpherson@mcgill.ca.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>MOP-13461</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. 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Repeat Serine-Threonine Protein Kinase-2</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020830" MajorTopicYN="N">rac1 GTP-Binding Protein</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4304731</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Drosophila melanogaster</Keyword><Keyword MajorTopicYN="N">Parkinson's disease</Keyword><Keyword MajorTopicYN="N">Rac1</Keyword><Keyword MajorTopicYN="N">clathrin</Keyword><Keyword MajorTopicYN="N">endosomes</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>11</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>7</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25427558</ArticleId><ArticleId IdType="pii">embr.201438714</ArticleId><ArticleId IdType="doi">10.15252/embr.201438714</ArticleId><ArticleId IdType="pmc">PMC4304731</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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