RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin.
Identifieur interne : 003713 ( PubMed/Corpus ); précédent : 003712; suivant : 003714RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin.
Auteurs : Marta Truffi ; Véronique Dubreuil ; Xuan Liang ; Nathalie Vacaresse ; Fabienne Nigon ; Siew Ping Han ; Alpha S. Yap ; Guillermo A. Gomez ; Jan SapSource :
- Journal of cell science [ 1477-9137 ] ; 2014.
English descriptors
- KwdEn :
- Actins (metabolism), Adherens Junctions (genetics), Adherens Junctions (metabolism), Caco-2 Cells, Cadherins (metabolism), Cell Adhesion (genetics), Cortactin (genetics), Cortactin (metabolism), Epithelial Cells (physiology), HEK293 Cells, Humans, Mutation (genetics), Organ Culture Techniques, Organogenesis (genetics), Phosphorylation (genetics), Protein Transport, RNA, Small Interfering (genetics), Receptor-Like Protein Tyrosine Phosphatases, Class 4 (genetics), Receptor-Like Protein Tyrosine Phosphatases, Class 4 (metabolism), Signal Transduction (genetics), src-Family Kinases (metabolism).
- MESH :
- chemical , genetics : Cortactin, RNA, Small Interfering, Receptor-Like Protein Tyrosine Phosphatases, Class 4.
- chemical , metabolism : Actins, Cadherins, Cortactin, Receptor-Like Protein Tyrosine Phosphatases, Class 4, src-Family Kinases.
- genetics : Adherens Junctions, Cell Adhesion, Mutation, Organogenesis, Phosphorylation, Signal Transduction.
- metabolism : Adherens Junctions.
- physiology : Epithelial Cells.
- Caco-2 Cells, HEK293 Cells, Humans, Organ Culture Techniques, Protein Transport.
Abstract
Epithelial junctions are fundamental determinants of tissue organization, subject to regulation by tyrosine phosphorylation. Homophilic binding of E-cadherin activates tyrosine kinases, such as Src, that control junctional integrity. Protein tyrosine phosphatases (PTPs) also contribute to cadherin-based adhesion and signaling, but little is known about their specific identity or functions at epithelial junctions. Here, we report that the receptor PTP RPTPα (human gene name PTPRA) is recruited to epithelial adherens junctions at the time of cell-cell contact, where it is in molecular proximity to E-cadherin. RPTPα is required for appropriate cadherin-dependent adhesion and for cyst architecture in three-dimensional culture. Loss of RPTPα impairs adherens junction integrity, as manifested by defective E-cadherin accumulation and peri-junctional F-actin density. These effects correlate with a role for RPTPα in cellular (c)-Src activation at sites of E-cadherin engagement. Mechanistically, RPTPα is required for appropriate tyrosine phosphorylation of cortactin, a major Src substrate and a cytoskeletal actin organizer. Expression of a phosphomimetic cortactin mutant in RPTPα-depleted cells partially rescues F-actin and E-cadherin accumulation at intercellular contacts. These findings indicate that RPTPα controls cadherin-mediated signaling by linking homophilic E-cadherin engagement to cortactin tyrosine phosphorylation through c-Src.
DOI: 10.1242/jcs.134379
PubMed: 24652832
Links to Exploration step
pubmed:24652832Le document en format XML
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Yap</name><affiliation><nlm:affiliation>Division of Molecular Cell Biology, Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Gomez, Guillermo A" sort="Gomez, Guillermo A" uniqKey="Gomez G" first="Guillermo A" last="Gomez">Guillermo A. Gomez</name><affiliation><nlm:affiliation>Division of Molecular Cell Biology, Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Sap, Jan" sort="Sap, Jan" uniqKey="Sap J" first="Jan" last="Sap">Jan Sap</name><affiliation><nlm:affiliation>Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR 7216 CNRS, Bâtiment Lamarck, Case 7042, 35 Rue Hélène Brion, F-75205 Paris Cedex 13, France Biotech Research and Innovation Centre and Department of Biomedical Sciences, Faculty of Health Sciences, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark veronique.dubrueil@univ-paris-diderot.fr jansap@fastmail.fm.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of cell science</title><idno type="eISSN">1477-9137</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actins (metabolism)</term><term>Adherens Junctions (genetics)</term><term>Adherens Junctions (metabolism)</term><term>Caco-2 Cells</term><term>Cadherins (metabolism)</term><term>Cell Adhesion (genetics)</term><term>Cortactin (genetics)</term><term>Cortactin (metabolism)</term><term>Epithelial Cells (physiology)</term><term>HEK293 Cells</term><term>Humans</term><term>Mutation (genetics)</term><term>Organ Culture Techniques</term><term>Organogenesis (genetics)</term><term>Phosphorylation (genetics)</term><term>Protein Transport</term><term>RNA, Small Interfering (genetics)</term><term>Receptor-Like Protein Tyrosine Phosphatases, Class 4 (genetics)</term><term>Receptor-Like Protein Tyrosine Phosphatases, Class 4 (metabolism)</term><term>Signal Transduction (genetics)</term><term>src-Family Kinases (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cortactin</term><term>RNA, Small Interfering</term><term>Receptor-Like Protein Tyrosine Phosphatases, Class 4</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Actins</term><term>Cadherins</term><term>Cortactin</term><term>Receptor-Like Protein Tyrosine Phosphatases, Class 4</term><term>src-Family Kinases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Adherens Junctions</term><term>Cell Adhesion</term><term>Mutation</term><term>Organogenesis</term><term>Phosphorylation</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Adherens Junctions</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Epithelial Cells</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Caco-2 Cells</term><term>HEK293 Cells</term><term>Humans</term><term>Organ Culture Techniques</term><term>Protein Transport</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Epithelial junctions are fundamental determinants of tissue organization, subject to regulation by tyrosine phosphorylation. Homophilic binding of E-cadherin activates tyrosine kinases, such as Src, that control junctional integrity. Protein tyrosine phosphatases (PTPs) also contribute to cadherin-based adhesion and signaling, but little is known about their specific identity or functions at epithelial junctions. Here, we report that the receptor PTP RPTPα (human gene name PTPRA) is recruited to epithelial adherens junctions at the time of cell-cell contact, where it is in molecular proximity to E-cadherin. RPTPα is required for appropriate cadherin-dependent adhesion and for cyst architecture in three-dimensional culture. Loss of RPTPα impairs adherens junction integrity, as manifested by defective E-cadherin accumulation and peri-junctional F-actin density. These effects correlate with a role for RPTPα in cellular (c)-Src activation at sites of E-cadherin engagement. Mechanistically, RPTPα is required for appropriate tyrosine phosphorylation of cortactin, a major Src substrate and a cytoskeletal actin organizer. Expression of a phosphomimetic cortactin mutant in RPTPα-depleted cells partially rescues F-actin and E-cadherin accumulation at intercellular contacts. These findings indicate that RPTPα controls cadherin-mediated signaling by linking homophilic E-cadherin engagement to cortactin tyrosine phosphorylation through c-Src.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24652832</PMID><DateCreated><Year>2014</Year><Month>06</Month><Day>02</Day></DateCreated><DateCompleted><Year>2015</Year><Month>05</Month><Day>11</Day></DateCompleted><DateRevised><Year>2014</Year><Month>06</Month><Day>02</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1477-9137</ISSN><JournalIssue CitedMedium="Internet"><Volume>127</Volume><Issue>Pt 11</Issue><PubDate><Year>2014</Year><Month>Jun</Month><Day>01</Day></PubDate></JournalIssue><Title>Journal of cell science</Title><ISOAbbreviation>J. Cell. Sci.</ISOAbbreviation></Journal><ArticleTitle>RPTPα controls epithelial adherens junctions, linking E-cadherin engagement to c-Src-mediated phosphorylation of cortactin.</ArticleTitle><Pagination><MedlinePgn>2420-32</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1242/jcs.134379</ELocationID><Abstract><AbstractText>Epithelial junctions are fundamental determinants of tissue organization, subject to regulation by tyrosine phosphorylation. Homophilic binding of E-cadherin activates tyrosine kinases, such as Src, that control junctional integrity. Protein tyrosine phosphatases (PTPs) also contribute to cadherin-based adhesion and signaling, but little is known about their specific identity or functions at epithelial junctions. Here, we report that the receptor PTP RPTPα (human gene name PTPRA) is recruited to epithelial adherens junctions at the time of cell-cell contact, where it is in molecular proximity to E-cadherin. RPTPα is required for appropriate cadherin-dependent adhesion and for cyst architecture in three-dimensional culture. Loss of RPTPα impairs adherens junction integrity, as manifested by defective E-cadherin accumulation and peri-junctional F-actin density. These effects correlate with a role for RPTPα in cellular (c)-Src activation at sites of E-cadherin engagement. Mechanistically, RPTPα is required for appropriate tyrosine phosphorylation of cortactin, a major Src substrate and a cytoskeletal actin organizer. Expression of a phosphomimetic cortactin mutant in RPTPα-depleted cells partially rescues F-actin and E-cadherin accumulation at intercellular contacts. These findings indicate that RPTPα controls cadherin-mediated signaling by linking homophilic E-cadherin engagement to cortactin tyrosine phosphorylation through c-Src.</AbstractText><CopyrightInformation>© 2014. Published by The Company of Biologists Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Truffi</LastName><ForeName>Marta</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR 7216 CNRS, Bâtiment Lamarck, Case 7042, 35 Rue Hélène Brion, F-75205 Paris Cedex 13, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dubreuil</LastName><ForeName>Véronique</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR 7216 CNRS, Bâtiment Lamarck, Case 7042, 35 Rue Hélène Brion, F-75205 Paris Cedex 13, France veronique.dubrueil@univ-paris-diderot.fr jansap@fastmail.fm.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Liang</LastName><ForeName>Xuan</ForeName><Initials>X</Initials><AffiliationInfo><Affiliation>Division of Molecular Cell Biology, Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vacaresse</LastName><ForeName>Nathalie</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Biotech Research and Innovation Centre and Department of Biomedical Sciences, Faculty of Health Sciences, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nigon</LastName><ForeName>Fabienne</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR 7216 CNRS, Bâtiment Lamarck, Case 7042, 35 Rue Hélène Brion, F-75205 Paris Cedex 13, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Han</LastName><ForeName>Siew Ping</ForeName><Initials>SP</Initials><AffiliationInfo><Affiliation>Division of Molecular Cell Biology, Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yap</LastName><ForeName>Alpha S</ForeName><Initials>AS</Initials><AffiliationInfo><Affiliation>Division of Molecular Cell Biology, Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Gomez</LastName><ForeName>Guillermo A</ForeName><Initials>GA</Initials><AffiliationInfo><Affiliation>Division of Molecular Cell Biology, Institute for Molecular Bioscience, University of Queensland, St. Lucia, Brisbane 4072, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sap</LastName><ForeName>Jan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Université Paris Diderot, Sorbonne Paris Cité, Epigenetics and Cell Fate, UMR 7216 CNRS, Bâtiment Lamarck, Case 7042, 35 Rue Hélène Brion, F-75205 Paris Cedex 13, France Biotech Research and Innovation Centre and Department of Biomedical Sciences, Faculty of Health Sciences, University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen N, Denmark veronique.dubrueil@univ-paris-diderot.fr jansap@fastmail.fm.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>03</Month><Day>20</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>J Cell Sci</MedlineTA><NlmUniqueID>0052457</NlmUniqueID><ISSNLinking>0021-9533</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000199">Actins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015820">Cadherins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051356">Cortactin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D034741">RNA, Small Interfering</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.10.2</RegistryNumber><NameOfSubstance UI="C073097">CSK tyrosine-protein kinase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.10.2</RegistryNumber><NameOfSubstance UI="D019061">src-Family Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.48</RegistryNumber><NameOfSubstance UI="C516841">PTPRA protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.48</RegistryNumber><NameOfSubstance UI="D054630">Receptor-Like Protein Tyrosine Phosphatases, Class 4</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000199" MajorTopicYN="N">Actins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D022005" MajorTopicYN="N">Adherens Junctions</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018938" MajorTopicYN="N">Caco-2 Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015820" MajorTopicYN="N">Cadherins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002448" MajorTopicYN="N">Cell Adhesion</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051356" MajorTopicYN="N">Cortactin</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" 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UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D034741" MajorTopicYN="N">RNA, Small Interfering</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054630" MajorTopicYN="N">Receptor-Like Protein Tyrosine Phosphatases, Class 4</DescriptorName><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="D019061" MajorTopicYN="N">src-Family Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Adherens junctions</Keyword><Keyword MajorTopicYN="N">Cortactin</Keyword><Keyword MajorTopicYN="N">E-cadherin</Keyword><Keyword MajorTopicYN="N">Tyrosine phosphatase</Keyword><Keyword MajorTopicYN="N">c-Src</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>3</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>3</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>5</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24652832</ArticleId><ArticleId IdType="pii">jcs.134379</ArticleId><ArticleId 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