Stabilization of a prokaryotic LAT transporter by random mutagenesis.
Identifieur interne : 002021 ( PubMed/Curation ); précédent : 002020; suivant : 002022Stabilization of a prokaryotic LAT transporter by random mutagenesis.
Auteurs : Arturo Rodríguez-Banqueri [Espagne] ; Ekaitz Errasti-Murugarren [Espagne] ; Paola Bartoccioni [Espagne] ; Lukasz Kowalczyk [Australie] ; Alex Perálvarez-Marín [Espagne] ; Manuel Palacín ; José Luis Vázquez-IbarSource :
- The Journal of general physiology [ 1540-7748 ] ; 2016.
Descripteurs français
- KwdFr :
- Bacillus subtilis (métabolisme), Protéines bactériennes (), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Stabilité protéique, Substitution d'acide aminé, Systèmes de transport d'acides aminés (), Systèmes de transport d'acides aminés (génétique), Systèmes de transport d'acides aminés (métabolisme).
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Amino Acid Transport Systems, Bacterial Proteins.
- chemical , genetics : Amino Acid Transport Systems, Bacterial Proteins.
- chemical , metabolism : Amino Acid Transport Systems, Bacterial Proteins.
- metabolism : Bacillus subtilis.
- Amino Acid Substitution, Protein Stability.
Abstract
The knowledge of three-dimensional structures at atomic resolution of membrane transport proteins has improved considerably our understanding of their physiological roles and pathological implications. However, most structural biology techniques require an optimal candidate within a protein family for structural determination with (a) reasonable production in heterologous hosts and (b) good stability in detergent micelles. SteT, the Bacillus subtilis L-serine/L-threonine exchanger is the best-known prokaryotic paradigm of the mammalian L-amino acid transporter (LAT) family. Unfortunately, SteT's lousy stability after extracting from the membrane prevents its structural characterization. Here, we have used an approach based on random mutagenesis to engineer stability in SteT. Using a split GFP complementation assay as reporter of protein expression and membrane insertion, we created a library of 70 SteT mutants each containing random replacements of one or two residues situated in the transmembrane domains. Analysis of expression and monodispersity in detergent of this library permitted the identification of evolved versions of SteT with a significant increase in both expression yield and stability in detergent with respect to wild type. In addition, these experiments revealed a correlation between the yield of expression and the stability in detergent micelles. Finally, and based on protein delipidation and relipidation assays together with transport experiments, possible mechanisms of SteT stabilization are discussed. Besides optimizing a member of the LAT family for structural determination, our work proposes a new approach that can be used to optimize any membrane protein of interest.
DOI: 10.1085/jgp.201511510
PubMed: 26976827
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Manuel Palacín<affiliation><nlm:affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain Spanish Biomedical Research Center in Rare Diseases (CIBERER), 08028 Barcelona, Spain Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, 08028 Barcelona, Spain jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</nlm:affiliation><wicri:noCountry code="subField">Spain jl.vazquez.ibar@gmail.com</wicri:noCountry></affiliation><affiliation><nlm:affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, French National Centre for Scientific Research (CNRS) UMR 9198, University Paris-Sud, University Paris-Saclay, F-91198 Gif-sur-Yvette, France jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</nlm:affiliation><wicri:noCountry code="subField">France jl.vazquez.ibar@gmail.com</wicri:noCountry></affiliation>Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Stabilization of a prokaryotic LAT transporter by random mutagenesis.</title><author><name sortKey="Rodriguez Banqueri, Arturo" sort="Rodriguez Banqueri, Arturo" uniqKey="Rodriguez Banqueri A" first="Arturo" last="Rodríguez-Banqueri">Arturo Rodríguez-Banqueri</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona</wicri:regionArea></affiliation></author><author><name sortKey="Errasti Murugarren, Ekaitz" sort="Errasti Murugarren, Ekaitz" uniqKey="Errasti Murugarren E" first="Ekaitz" last="Errasti-Murugarren">Ekaitz Errasti-Murugarren</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Research in Biomedicine (IRB), 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Barcelona</wicri:regionArea></affiliation></author><author><name sortKey="Kowalczyk, Lukasz" sort="Kowalczyk, Lukasz" uniqKey="Kowalczyk L" first="Lukasz" last="Kowalczyk">Lukasz Kowalczyk</name><affiliation wicri:level="1"><nlm:affiliation>Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052</wicri:regionArea></affiliation></author><author><name sortKey="Peralvarez Marin, Alex" sort="Peralvarez Marin, Alex" uniqKey="Peralvarez Marin A" first="Alex" last="Perálvarez-Marín">Alex Perálvarez-Marín</name><affiliation wicri:level="1"><nlm:affiliation>Biophysics Unit, Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, 08193 Cerdanyola del Vallés, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Biophysics Unit, Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, 08193 Cerdanyola del Vallés</wicri:regionArea></affiliation></author><author><name sortKey="Palacin, Manuel" sort="Palacin, Manuel" uniqKey="Palacin M" first="Manuel" last="Palacín">Manuel Palacín</name><affiliation><nlm:affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain Spanish Biomedical Research Center in Rare Diseases (CIBERER), 08028 Barcelona, Spain Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, 08028 Barcelona, Spain jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</nlm:affiliation><wicri:noCountry code="subField">Spain jl.vazquez.ibar@gmail.com</wicri:noCountry></affiliation></author><author><name sortKey="Vazquez Ibar, Jose Luis" sort="Vazquez Ibar, Jose Luis" uniqKey="Vazquez Ibar J" first="José Luis" last="Vázquez-Ibar">José Luis Vázquez-Ibar</name><affiliation><nlm:affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, French National Centre for Scientific Research (CNRS) UMR 9198, University Paris-Sud, University Paris-Saclay, F-91198 Gif-sur-Yvette, France jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</nlm:affiliation><wicri:noCountry code="subField">France jl.vazquez.ibar@gmail.com</wicri:noCountry></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26976827</idno><idno type="pmid">26976827</idno><idno type="doi">10.1085/jgp.201511510</idno><idno type="wicri:Area/PubMed/Corpus">002046</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002046</idno><idno type="wicri:Area/PubMed/Curation">002021</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002021</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Stabilization of a prokaryotic LAT transporter by random mutagenesis.</title><author><name sortKey="Rodriguez Banqueri, Arturo" sort="Rodriguez Banqueri, Arturo" uniqKey="Rodriguez Banqueri A" first="Arturo" last="Rodríguez-Banqueri">Arturo Rodríguez-Banqueri</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona</wicri:regionArea></affiliation></author><author><name sortKey="Errasti Murugarren, Ekaitz" sort="Errasti Murugarren, Ekaitz" uniqKey="Errasti Murugarren E" first="Ekaitz" last="Errasti-Murugarren">Ekaitz Errasti-Murugarren</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona</wicri:regionArea></affiliation></author><author><name sortKey="Bartoccioni, Paola" sort="Bartoccioni, Paola" uniqKey="Bartoccioni P" first="Paola" last="Bartoccioni">Paola Bartoccioni</name><affiliation wicri:level="1"><nlm:affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain Spanish Biomedical Research Center in Rare Diseases (CIBERER), 08028 Barcelona, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain Spanish Biomedical Research Center in Rare Diseases (CIBERER), 08028 Barcelona</wicri:regionArea></affiliation></author><author><name sortKey="Kowalczyk, Lukasz" sort="Kowalczyk, Lukasz" uniqKey="Kowalczyk L" first="Lukasz" last="Kowalczyk">Lukasz Kowalczyk</name><affiliation wicri:level="1"><nlm:affiliation>Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia.</nlm:affiliation><country xml:lang="fr">Australie</country><wicri:regionArea>Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052</wicri:regionArea></affiliation></author><author><name sortKey="Peralvarez Marin, Alex" sort="Peralvarez Marin, Alex" uniqKey="Peralvarez Marin A" first="Alex" last="Perálvarez-Marín">Alex Perálvarez-Marín</name><affiliation wicri:level="1"><nlm:affiliation>Biophysics Unit, Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, 08193 Cerdanyola del Vallés, Spain.</nlm:affiliation><country xml:lang="fr">Espagne</country><wicri:regionArea>Biophysics Unit, Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, 08193 Cerdanyola del Vallés</wicri:regionArea></affiliation></author><author><name sortKey="Palacin, Manuel" sort="Palacin, Manuel" uniqKey="Palacin M" first="Manuel" last="Palacín">Manuel Palacín</name><affiliation><nlm:affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain Spanish Biomedical Research Center in Rare Diseases (CIBERER), 08028 Barcelona, Spain Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, 08028 Barcelona, Spain jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</nlm:affiliation><wicri:noCountry code="subField">Spain jl.vazquez.ibar@gmail.com</wicri:noCountry></affiliation></author><author><name sortKey="Vazquez Ibar, Jose Luis" sort="Vazquez Ibar, Jose Luis" uniqKey="Vazquez Ibar J" first="José Luis" last="Vázquez-Ibar">José Luis Vázquez-Ibar</name><affiliation><nlm:affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, French National Centre for Scientific Research (CNRS) UMR 9198, University Paris-Sud, University Paris-Saclay, F-91198 Gif-sur-Yvette, France jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</nlm:affiliation><wicri:noCountry code="subField">France jl.vazquez.ibar@gmail.com</wicri:noCountry></affiliation></author></analytic><series><title level="j">The Journal of general physiology</title><idno type="eISSN">1540-7748</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Substitution</term><term>Amino Acid Transport Systems (chemistry)</term><term>Amino Acid Transport Systems (genetics)</term><term>Amino Acid Transport Systems (metabolism)</term><term>Bacillus subtilis (metabolism)</term><term>Bacterial Proteins (chemistry)</term><term>Bacterial Proteins (genetics)</term><term>Bacterial Proteins (metabolism)</term><term>Protein Stability</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bacillus subtilis (métabolisme)</term><term>Protéines bactériennes ()</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Stabilité protéique</term><term>Substitution d'acide aminé</term><term>Systèmes de transport d'acides aminés ()</term><term>Systèmes de transport d'acides aminés (génétique)</term><term>Systèmes de transport d'acides aminés (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acid Transport Systems</term><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Amino Acid Transport Systems</term><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Amino Acid Transport Systems</term><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Protéines bactériennes</term><term>Systèmes de transport d'acides aminés</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacillus subtilis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bacillus subtilis</term><term>Protéines bactériennes</term><term>Systèmes de transport d'acides aminés</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Substitution</term><term>Protein Stability</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Protéines bactériennes</term><term>Stabilité protéique</term><term>Substitution d'acide aminé</term><term>Systèmes de transport d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The knowledge of three-dimensional structures at atomic resolution of membrane transport proteins has improved considerably our understanding of their physiological roles and pathological implications. However, most structural biology techniques require an optimal candidate within a protein family for structural determination with (a) reasonable production in heterologous hosts and (b) good stability in detergent micelles. SteT, the Bacillus subtilis L-serine/L-threonine exchanger is the best-known prokaryotic paradigm of the mammalian L-amino acid transporter (LAT) family. Unfortunately, SteT's lousy stability after extracting from the membrane prevents its structural characterization. Here, we have used an approach based on random mutagenesis to engineer stability in SteT. Using a split GFP complementation assay as reporter of protein expression and membrane insertion, we created a library of 70 SteT mutants each containing random replacements of one or two residues situated in the transmembrane domains. Analysis of expression and monodispersity in detergent of this library permitted the identification of evolved versions of SteT with a significant increase in both expression yield and stability in detergent with respect to wild type. In addition, these experiments revealed a correlation between the yield of expression and the stability in detergent micelles. Finally, and based on protein delipidation and relipidation assays together with transport experiments, possible mechanisms of SteT stabilization are discussed. Besides optimizing a member of the LAT family for structural determination, our work proposes a new approach that can be used to optimize any membrane protein of interest.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26976827</PMID><DateCreated><Year>2016</Year><Month>03</Month><Day>29</Day></DateCreated><DateCompleted><Year>2016</Year><Month>12</Month><Day>13</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1540-7748</ISSN><JournalIssue CitedMedium="Internet"><Volume>147</Volume><Issue>4</Issue><PubDate><Year>2016</Year><Month>Apr</Month></PubDate></JournalIssue><Title>The Journal of general physiology</Title><ISOAbbreviation>J. Gen. Physiol.</ISOAbbreviation></Journal><ArticleTitle>Stabilization of a prokaryotic LAT transporter by random mutagenesis.</ArticleTitle><Pagination><MedlinePgn>353-68</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1085/jgp.201511510</ELocationID><Abstract><AbstractText>The knowledge of three-dimensional structures at atomic resolution of membrane transport proteins has improved considerably our understanding of their physiological roles and pathological implications. However, most structural biology techniques require an optimal candidate within a protein family for structural determination with (a) reasonable production in heterologous hosts and (b) good stability in detergent micelles. SteT, the Bacillus subtilis L-serine/L-threonine exchanger is the best-known prokaryotic paradigm of the mammalian L-amino acid transporter (LAT) family. Unfortunately, SteT's lousy stability after extracting from the membrane prevents its structural characterization. Here, we have used an approach based on random mutagenesis to engineer stability in SteT. Using a split GFP complementation assay as reporter of protein expression and membrane insertion, we created a library of 70 SteT mutants each containing random replacements of one or two residues situated in the transmembrane domains. Analysis of expression and monodispersity in detergent of this library permitted the identification of evolved versions of SteT with a significant increase in both expression yield and stability in detergent with respect to wild type. In addition, these experiments revealed a correlation between the yield of expression and the stability in detergent micelles. Finally, and based on protein delipidation and relipidation assays together with transport experiments, possible mechanisms of SteT stabilization are discussed. Besides optimizing a member of the LAT family for structural determination, our work proposes a new approach that can be used to optimize any membrane protein of interest.</AbstractText><CopyrightInformation>© 2016 Rodríguez-Banqueri et al.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Rodríguez-Banqueri</LastName><ForeName>Arturo</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Errasti-Murugarren</LastName><ForeName>Ekaitz</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bartoccioni</LastName><ForeName>Paola</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain Spanish Biomedical Research Center in Rare Diseases (CIBERER), 08028 Barcelona, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kowalczyk</LastName><ForeName>Lukasz</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Perálvarez-Marín</LastName><ForeName>Alex</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Biophysics Unit, Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, 08193 Cerdanyola del Vallés, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Palacín</LastName><ForeName>Manuel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Institute for Research in Biomedicine (IRB), Barcelona Institute of Science and Technology, 08028 Barcelona, Spain Spanish Biomedical Research Center in Rare Diseases (CIBERER), 08028 Barcelona, Spain Department of Biochemistry and Molecular Biology, Faculty of Biology, University of Barcelona, 08028 Barcelona, Spain jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vázquez-Ibar</LastName><ForeName>José Luis</ForeName><Initials>JL</Initials><AffiliationInfo><Affiliation>Institute for Integrative Biology of the Cell (I2BC), CEA, French National Centre for Scientific Research (CNRS) UMR 9198, University Paris-Sud, University Paris-Saclay, F-91198 Gif-sur-Yvette, France jl.vazquez.ibar@gmail.com manuel.palacin@irbbarcelona.org.</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>2016</Year><Month>03</Month><Day>14</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Gen Physiol</MedlineTA><NlmUniqueID>2985110R</NlmUniqueID><ISSNLinking>0022-1295</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D026905">Amino Acid Transport Systems</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Biochim Biophys Acta. 2012 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10/01/16]</OtherID></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>09</Month><Day>04</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2016</Year><Month>02</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>3</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>3</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>12</Month><Day>15</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">26976827</ArticleId><ArticleId IdType="pii">jgp.201511510</ArticleId><ArticleId IdType="doi">10.1085/jgp.201511510</ArticleId><ArticleId IdType="pmc">PMC4810068</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix 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