RapamycinFungusV1, Main, Exploration, bibRecord, 000420

mTORC1 Controls Phase Separation and the Biophysical Properties of the Cytoplasm by Tuning Crowding.

Identifieur interne : 000420 ( Main/Exploration ); précédent : 000419; suivant : 000421

mTORC1 Controls Phase Separation and the Biophysical Properties of the Cytoplasm by Tuning Crowding.

Auteurs : M. Delarue [États-Unis] ; G P Brittingham [États-Unis] ; S. Pfeffer [Allemagne] ; I V Surovtsev [États-Unis] ; S. Pinglay [États-Unis] ; K J Kennedy [États-Unis] ; M. Schaffer [Allemagne] ; J I Gutierrez [États-Unis] ; D. Sang [États-Unis] ; G. Poterewicz [États-Unis] ; J K Chung [États-Unis] ; J M Plitzko [Allemagne] ; J T Groves [États-Unis] ; C. Jacobs-Wagner [États-Unis] ; B D Engel [Allemagne] ; L J Holt [États-Unis]

Source :

Cell [ 1097-4172 ] ; 2018.

RBID : pubmed:29937223

Descripteurs français

English descriptors

KwdEn :
- Cytoplasm (metabolism), Diffusion (MeSH), HEK293 Cells (MeSH), Humans (MeSH), Mechanistic Target of Rapamycin Complex 1 (antagonists & inhibitors), Mechanistic Target of Rapamycin Complex 1 (genetics), Mechanistic Target of Rapamycin Complex 1 (metabolism), Nanoparticles (chemistry), Nanoparticles (metabolism), Particle Size (MeSH), Plasmids (genetics), Plasmids (metabolism), RNA Interference (MeSH), RNA, Small Interfering (metabolism), Rheology (MeSH), Ribosomes (metabolism), Saccharomyces cerevisiae (metabolism), Tuberous Sclerosis Complex 1 Protein (antagonists & inhibitors), Tuberous Sclerosis Complex 1 Protein (genetics), Tuberous Sclerosis Complex 1 Protein (metabolism).
MESH :
- chemical , antagonists & inhibitors : Mechanistic Target of Rapamycin Complex 1, Tuberous Sclerosis Complex 1 Protein.
- chemical , genetics : Mechanistic Target of Rapamycin Complex 1, Tuberous Sclerosis Complex 1 Protein.
- chemistry : Nanoparticles.
- genetics : Plasmids.
- metabolism : Cytoplasm, Mechanistic Target of Rapamycin Complex 1, Nanoparticles, Plasmids, RNA, Small Interfering, Ribosomes, Saccharomyces cerevisiae, Tuberous Sclerosis Complex 1 Protein.
- Diffusion, HEK293 Cells, Humans, Particle Size, RNA Interference, Rheology.

Abstract

Macromolecular crowding has a profound impact on reaction rates and the physical properties of the cell interior, but the mechanisms that regulate crowding are poorly understood. We developed genetically encoded multimeric nanoparticles (GEMs) to dissect these mechanisms. GEMs are homomultimeric scaffolds fused to a fluorescent protein that self-assemble into bright, stable particles of defined size and shape. By combining tracking of GEMs with genetic and pharmacological approaches, we discovered that the mTORC1 pathway can modulate the effective diffusion coefficient of particles ≥20 nm in diameter more than 2-fold by tuning ribosome concentration, without any discernable effect on the motion of molecules ≤5 nm. This change in ribosome concentration affected phase separation both in vitro and in vivo. Together, these results establish a role for mTORC1 in controlling both the mesoscale biophysical properties of the cytoplasm and biomolecular condensation.

DOI: 10.1016/j.cell.2018.05.042
PubMed: 29937223

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<author><name sortKey="Schaffer, M" sort="Schaffer, M" uniqKey="Schaffer M" first="M" last="Schaffer">M. Schaffer</name>
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<author><name sortKey="Sang, D" sort="Sang, D" uniqKey="Sang D" first="D" last="Sang">D. Sang</name>
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<author><name sortKey="Poterewicz, G" sort="Poterewicz, G" uniqKey="Poterewicz G" first="G" last="Poterewicz">G. Poterewicz</name>
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<author><name sortKey="Chung, J K" sort="Chung, J K" uniqKey="Chung J" first="J K" last="Chung">J K Chung</name>
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<author><name sortKey="Plitzko, J M" sort="Plitzko, J M" uniqKey="Plitzko J" first="J M" last="Plitzko">J M Plitzko</name>
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<author><name sortKey="Groves, J T" sort="Groves, J T" uniqKey="Groves J" first="J T" last="Groves">J T Groves</name>
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<country xml:lang="fr">États-Unis</country>
<wicri:regionArea>Department of Chemistry, University of California, Berkeley, Berkeley, CA 95720, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815</wicri:regionArea>
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<author><name sortKey="Engel, B D" sort="Engel, B D" uniqKey="Engel B" first="B D" last="Engel">B D Engel</name>
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<country xml:lang="fr">Allemagne</country>
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<author><name sortKey="Holt, L J" sort="Holt, L J" uniqKey="Holt L" first="L J" last="Holt">L J Holt</name>
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<country xml:lang="fr">États-Unis</country>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cytoplasm (metabolism)</term>
<term>Diffusion (MeSH)</term>
<term>HEK293 Cells (MeSH)</term>
<term>Humans (MeSH)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (antagonists & inhibitors)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (genetics)</term>
<term>Mechanistic Target of Rapamycin Complex 1 (metabolism)</term>
<term>Nanoparticles (chemistry)</term>
<term>Nanoparticles (metabolism)</term>
<term>Particle Size (MeSH)</term>
<term>Plasmids (genetics)</term>
<term>Plasmids (metabolism)</term>
<term>RNA Interference (MeSH)</term>
<term>RNA, Small Interfering (metabolism)</term>
<term>Rheology (MeSH)</term>
<term>Ribosomes (metabolism)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
<term>Tuberous Sclerosis Complex 1 Protein (antagonists & inhibitors)</term>
<term>Tuberous Sclerosis Complex 1 Protein (genetics)</term>
<term>Tuberous Sclerosis Complex 1 Protein (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HEK293 (MeSH)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (antagonistes et inhibiteurs)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (génétique)</term>
<term>Complexe-1 cible mécanistique de la rapamycine (métabolisme)</term>
<term>Cytoplasme (métabolisme)</term>
<term>Diffusion (MeSH)</term>
<term>Humains (MeSH)</term>
<term>Interférence par ARN (MeSH)</term>
<term>Nanoparticules (composition chimique)</term>
<term>Nanoparticules (métabolisme)</term>
<term>Petit ARN interférent (métabolisme)</term>
<term>Plasmides (génétique)</term>
<term>Plasmides (métabolisme)</term>
<term>Protéine-1 du complexe de la sclérose tubéreuse (antagonistes et inhibiteurs)</term>
<term>Protéine-1 du complexe de la sclérose tubéreuse (génétique)</term>
<term>Protéine-1 du complexe de la sclérose tubéreuse (métabolisme)</term>
<term>Rhéologie (MeSH)</term>
<term>Ribosomes (métabolisme)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Taille de particule (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Tuberous Sclerosis Complex 1 Protein</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Tuberous Sclerosis Complex 1 Protein</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Protéine-1 du complexe de la sclérose tubéreuse</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Nanoparticles</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Nanoparticules</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Plasmids</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Plasmides</term>
<term>Protéine-1 du complexe de la sclérose tubéreuse</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoplasm</term>
<term>Mechanistic Target of Rapamycin Complex 1</term>
<term>Nanoparticles</term>
<term>Plasmids</term>
<term>RNA, Small Interfering</term>
<term>Ribosomes</term>
<term>Saccharomyces cerevisiae</term>
<term>Tuberous Sclerosis Complex 1 Protein</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-1 cible mécanistique de la rapamycine</term>
<term>Cytoplasme</term>
<term>Nanoparticules</term>
<term>Petit ARN interférent</term>
<term>Plasmides</term>
<term>Protéine-1 du complexe de la sclérose tubéreuse</term>
<term>Ribosomes</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Diffusion</term>
<term>HEK293 Cells</term>
<term>Humans</term>
<term>Particle Size</term>
<term>RNA Interference</term>
<term>Rheology</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cellules HEK293</term>
<term>Diffusion</term>
<term>Humains</term>
<term>Interférence par ARN</term>
<term>Rhéologie</term>
<term>Taille de particule</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Macromolecular crowding has a profound impact on reaction rates and the physical properties of the cell interior, but the mechanisms that regulate crowding are poorly understood. We developed genetically encoded multimeric nanoparticles (GEMs) to dissect these mechanisms. GEMs are homomultimeric scaffolds fused to a fluorescent protein that self-assemble into bright, stable particles of defined size and shape. By combining tracking of GEMs with genetic and pharmacological approaches, we discovered that the mTORC1 pathway can modulate the effective diffusion coefficient of particles ≥20 nm in diameter more than 2-fold by tuning ribosome concentration, without any discernable effect on the motion of molecules ≤5 nm. This change in ribosome concentration affected phase separation both in vitro and in vivo. Together, these results establish a role for mTORC1 in controlling both the mesoscale biophysical properties of the cytoplasm and biomolecular condensation.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29937223</PMID>
<DateCompleted><Year>2019</Year>
<Month>04</Month>
<Day>03</Day>
</DateCompleted>
<DateRevised><Year>2019</Year>
<Month>04</Month>
<Day>03</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1097-4172</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>174</Volume>
<Issue>2</Issue>
<PubDate><Year>2018</Year>
<Month>07</Month>
<Day>12</Day>
</PubDate>
</JournalIssue>
<Title>Cell</Title>
<ISOAbbreviation>Cell</ISOAbbreviation>
</Journal>
<ArticleTitle>mTORC1 Controls Phase Separation and the Biophysical Properties of the Cytoplasm by Tuning Crowding.</ArticleTitle>
<Pagination><MedlinePgn>338-349.e20</MedlinePgn>
</Pagination>
<ELocationID EIdType="pii" ValidYN="Y">S0092-8674(18)30654-8</ELocationID>
<ELocationID EIdType="doi" ValidYN="Y">10.1016/j.cell.2018.05.042</ELocationID>
<Abstract><AbstractText>Macromolecular crowding has a profound impact on reaction rates and the physical properties of the cell interior, but the mechanisms that regulate crowding are poorly understood. We developed genetically encoded multimeric nanoparticles (GEMs) to dissect these mechanisms. GEMs are homomultimeric scaffolds fused to a fluorescent protein that self-assemble into bright, stable particles of defined size and shape. By combining tracking of GEMs with genetic and pharmacological approaches, we discovered that the mTORC1 pathway can modulate the effective diffusion coefficient of particles ≥20 nm in diameter more than 2-fold by tuning ribosome concentration, without any discernable effect on the motion of molecules ≤5 nm. This change in ribosome concentration affected phase separation both in vitro and in vivo. Together, these results establish a role for mTORC1 in controlling both the mesoscale biophysical properties of the cytoplasm and biomolecular condensation.</AbstractText>
<CopyrightInformation>Copyright © 2018 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Delarue</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Institute for Systems Genetics, New York University Langone Health, New York, NY 10016, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Brittingham</LastName>
<ForeName>G P</ForeName>
<Initials>GP</Initials>
<AffiliationInfo><Affiliation>Institute for Systems Genetics, New York University Langone Health, New York, NY 10016, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pfeffer</LastName>
<ForeName>S</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Surovtsev</LastName>
<ForeName>I V</ForeName>
<Initials>IV</Initials>
<AffiliationInfo><Affiliation>Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA; Microbial Sciences Institute, Yale West Campus, West Haven, CT 06516, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Pinglay</LastName>
<ForeName>S</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Institute for Systems Genetics, New York University Langone Health, New York, NY 10016, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kennedy</LastName>
<ForeName>K J</ForeName>
<Initials>KJ</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 95720, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Schaffer</LastName>
<ForeName>M</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gutierrez</LastName>
<ForeName>J I</ForeName>
<Initials>JI</Initials>
<AffiliationInfo><Affiliation>Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 95720, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Sang</LastName>
<ForeName>D</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>Institute for Systems Genetics, New York University Langone Health, New York, NY 10016, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Poterewicz</LastName>
<ForeName>G</ForeName>
<Initials>G</Initials>
<AffiliationInfo><Affiliation>Institute for Systems Genetics, New York University Langone Health, New York, NY 10016, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chung</LastName>
<ForeName>J K</ForeName>
<Initials>JK</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, University of California, Berkeley, Berkeley, CA 95720, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Plitzko</LastName>
<ForeName>J M</ForeName>
<Initials>JM</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Groves</LastName>
<ForeName>J T</ForeName>
<Initials>JT</Initials>
<AffiliationInfo><Affiliation>Department of Chemistry, University of California, Berkeley, Berkeley, CA 95720, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Jacobs-Wagner</LastName>
<ForeName>C</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06511, USA; Howard Hughes Medical Institute, Chevy Chase, MD 20815, USA; Microbial Sciences Institute, Yale West Campus, West Haven, CT 06516, USA; Department of Microbial Pathogenesis, Yale School of Medicine, New Haven, CT 06511, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Engel</LastName>
<ForeName>B D</ForeName>
<Initials>BD</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany. Electronic address: engelben@biochem.mpg.de.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Holt</LastName>
<ForeName>L J</ForeName>
<Initials>LJ</Initials>
<AffiliationInfo><Affiliation>Institute for Systems Genetics, New York University Langone Health, New York, NY 10016, USA. Electronic address: liam.holt@nyumc.org.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><Acronym>HHMI</Acronym>
<Agency>Howard Hughes Medical Institute</Agency>
<Country>United States</Country>
</Grant>
</GrantList>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2018</Year>
<Month>06</Month>
<Day>21</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Cell</MedlineTA>
<NlmUniqueID>0413066</NlmUniqueID>
<ISSNLinking>0092-8674</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D034741">RNA, Small Interfering</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C000624650">TSC1 protein, human</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D000077004">Tuberous Sclerosis Complex 1 Protein</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber>
<NameOfSubstance UI="D000076222">Mechanistic Target of Rapamycin Complex 1</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Cell. 2018 Jul 12;174(2):253-255</RefSource>
<PMID Version="1">30007414</PMID>
</CommentsCorrections>
<CommentsCorrections RefType="CommentIn"><RefSource>Nat Chem Biol. 2018 Aug;14(8):745</RefSource>
<PMID Version="1">30018416</PMID>
</CommentsCorrections>
</CommentsCorrectionsList>
<MeshHeadingList><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D004058" MajorTopicYN="N">Diffusion</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D057809" MajorTopicYN="N">HEK293 Cells</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000076222" MajorTopicYN="N">Mechanistic Target of Rapamycin Complex 1</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D053758" MajorTopicYN="N">Nanoparticles</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010316" MajorTopicYN="N">Particle Size</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010957" MajorTopicYN="N">Plasmids</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D034622" MajorTopicYN="N">RNA Interference</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D034741" MajorTopicYN="N">RNA, Small Interfering</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012212" MajorTopicYN="N">Rheology</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012270" MajorTopicYN="N">Ribosomes</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000077004" MajorTopicYN="N">Tuberous Sclerosis Complex 1 Protein</DescriptorName>
<QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">biophysics</Keyword>
<Keyword MajorTopicYN="Y">cytoplasm</Keyword>
<Keyword MajorTopicYN="Y">electron tomography</Keyword>
<Keyword MajorTopicYN="Y">mTORC1</Keyword>
<Keyword MajorTopicYN="Y">microrheology</Keyword>
<Keyword MajorTopicYN="Y">molecular crowding</Keyword>
<Keyword MajorTopicYN="Y">nanoparticles</Keyword>
<Keyword MajorTopicYN="Y">phase separation</Keyword>
<Keyword MajorTopicYN="Y">ribosomes</Keyword>
<Keyword MajorTopicYN="Y">systems biology</Keyword>
</KeywordList>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year>
<Month>12</Month>
<Day>19</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised"><Year>2018</Year>
<Month>03</Month>
<Day>26</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2018</Year>
<Month>05</Month>
<Day>17</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2018</Year>
<Month>6</Month>
<Day>26</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2019</Year>
<Month>4</Month>
<Day>4</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2018</Year>
<Month>6</Month>
<Day>26</Day>
<Hour>6</Hour>
<Minute>0</Minute>
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</History>
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<ArticleId IdType="doi">10.1016/j.cell.2018.05.042</ArticleId>
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</pubmed>
<affiliations><list><country><li>Allemagne</li>
<li>États-Unis</li>
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<region><li>Californie</li>
<li>Connecticut</li>
<li>Maryland</li>
<li>État de New York</li>
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<tree><country name="États-Unis"><region name="État de New York"><name sortKey="Delarue, M" sort="Delarue, M" uniqKey="Delarue M" first="M" last="Delarue">M. Delarue</name>
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<name sortKey="Brittingham, G P" sort="Brittingham, G P" uniqKey="Brittingham G" first="G P" last="Brittingham">G P Brittingham</name>
<name sortKey="Chung, J K" sort="Chung, J K" uniqKey="Chung J" first="J K" last="Chung">J K Chung</name>
<name sortKey="Groves, J T" sort="Groves, J T" uniqKey="Groves J" first="J T" last="Groves">J T Groves</name>
<name sortKey="Gutierrez, J I" sort="Gutierrez, J I" uniqKey="Gutierrez J" first="J I" last="Gutierrez">J I Gutierrez</name>
<name sortKey="Holt, L J" sort="Holt, L J" uniqKey="Holt L" first="L J" last="Holt">L J Holt</name>
<name sortKey="Jacobs Wagner, C" sort="Jacobs Wagner, C" uniqKey="Jacobs Wagner C" first="C" last="Jacobs-Wagner">C. Jacobs-Wagner</name>
<name sortKey="Kennedy, K J" sort="Kennedy, K J" uniqKey="Kennedy K" first="K J" last="Kennedy">K J Kennedy</name>
<name sortKey="Pinglay, S" sort="Pinglay, S" uniqKey="Pinglay S" first="S" last="Pinglay">S. Pinglay</name>
<name sortKey="Poterewicz, G" sort="Poterewicz, G" uniqKey="Poterewicz G" first="G" last="Poterewicz">G. Poterewicz</name>
<name sortKey="Sang, D" sort="Sang, D" uniqKey="Sang D" first="D" last="Sang">D. Sang</name>
<name sortKey="Surovtsev, I V" sort="Surovtsev, I V" uniqKey="Surovtsev I" first="I V" last="Surovtsev">I V Surovtsev</name>
</country>
<country name="Allemagne"><noRegion><name sortKey="Pfeffer, S" sort="Pfeffer, S" uniqKey="Pfeffer S" first="S" last="Pfeffer">S. Pfeffer</name>
</noRegion>
<name sortKey="Engel, B D" sort="Engel, B D" uniqKey="Engel B" first="B D" last="Engel">B D Engel</name>
<name sortKey="Plitzko, J M" sort="Plitzko, J M" uniqKey="Plitzko J" first="J M" last="Plitzko">J M Plitzko</name>
<name sortKey="Schaffer, M" sort="Schaffer, M" uniqKey="Schaffer M" first="M" last="Schaffer">M. Schaffer</name>
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	Serveur d'exploration sur la rapamycine et les champignons
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mTORC1 Controls Phase Separation and the Biophysical Properties of the Cytoplasm by Tuning Crowding.

mTORC1 Controls Phase Separation and the Biophysical Properties of the Cytoplasm by Tuning Crowding.

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