RapamycinFungusV1, Main, Exploration, bibRecord, 000728

TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.

Identifieur interne : 000728 ( Main/Exploration ); précédent : 000727; suivant : 000729

TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.

Auteurs : Babet Van Der Vaart [Pays-Bas] ; Josef Fischböck [Autriche] ; Christine Mieck [Autriche] ; Peter Pichler [Autriche] ; Karl Mechtler [Autriche] ; René H. Medema [Pays-Bas] ; Stefan Westermann [Allemagne]

Source :

The Journal of cell biology [ 1540-8140 ] ; 2017.

RBID : pubmed:28972103

Descripteurs français

English descriptors

Abstract

The target of rapamycin complex 1 (TORC1) is a highly conserved multiprotein complex that functions in many cellular processes, including cell growth and cell cycle progression. In this study, we define a novel role for TORC1 as a critical regulator of nuclear microtubule (MT) dynamics in the budding yeast Saccharomyces cerevisiae This activity requires interactions between EB1 and CLIP-170 plus end-tracking protein (+TIP) family members with the TORC1 subunit Kog1/Raptor, which in turn allow the TORC1 proximal kinase Sch9/S6K1 to regulate the MT polymerase Stu2/XMAP215. Sch9-dependent phosphorylation of Stu2 adjacent to a nuclear export signal prevents nuclear accumulation of Stu2 before cells enter mitosis. Mutants impaired in +TIP-TORC1 interactions or Stu2 nuclear export show increased nuclear but not cytoplasmic MT length and display nuclear fusion, spindle positioning, and elongation kinetics defects. Our results reveal key mechanisms by which TORC1 signaling controls Stu2 localization and thereby contributes to proper MT cytoskeletal organization in interphase and mitosis.

DOI: 10.1083/jcb.201606080
PubMed: 28972103
PubMed Central: PMC5674874

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Active Transport, Cell Nucleus (MeSH)</term>
<term>Cell Nucleus (metabolism)</term>
<term>Interphase (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Mating Factor (genetics)</term>
<term>Mating Factor (metabolism)</term>
<term>Membrane Proteins (genetics)</term>
<term>Membrane Proteins (metabolism)</term>
<term>Microtubule-Associated Proteins (genetics)</term>
<term>Microtubule-Associated Proteins (metabolism)</term>
<term>Microtubules (genetics)</term>
<term>Microtubules (metabolism)</term>
<term>Mitosis (MeSH)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (genetics)</term>
<term>Protein-Serine-Threonine Kinases (metabolism)</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa (genetics)</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa (metabolism)</term>
<term>Saccharomyces cerevisiae (enzymology)</term>
<term>Saccharomyces cerevisiae (genetics)</term>
<term>Saccharomyces cerevisiae (growth & development)</term>
<term>Saccharomyces cerevisiae Proteins (genetics)</term>
<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
<term>Signal Transduction (MeSH)</term>
<term>Transcription Factors (genetics)</term>
<term>Transcription Factors (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term>
<term>Facteur de conjugaison (génétique)</term>
<term>Facteur de conjugaison (métabolisme)</term>
<term>Facteurs de transcription (génétique)</term>
<term>Facteurs de transcription (métabolisme)</term>
<term>Interphase (MeSH)</term>
<term>Microtubules (génétique)</term>
<term>Microtubules (métabolisme)</term>
<term>Mitose (MeSH)</term>
<term>Noyau de la cellule (métabolisme)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein-Serine-Threonine Kinases (génétique)</term>
<term>Protein-Serine-Threonine Kinases (métabolisme)</term>
<term>Protéines associées aux microtubules (génétique)</term>
<term>Protéines associées aux microtubules (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (génétique)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines membranaires (génétique)</term>
<term>Protéines membranaires (métabolisme)</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa (génétique)</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa (métabolisme)</term>
<term>Saccharomyces cerevisiae (croissance et développement)</term>
<term>Saccharomyces cerevisiae (enzymologie)</term>
<term>Saccharomyces cerevisiae (génétique)</term>
<term>Transduction du signal (MeSH)</term>
<term>Transport nucléaire actif (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Mating Factor</term>
<term>Membrane Proteins</term>
<term>Microtubule-Associated Proteins</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Microtubules</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteur de conjugaison</term>
<term>Facteurs de transcription</term>
<term>Microtubules</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines associées aux microtubules</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines membranaires</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa</term>
<term>Saccharomyces cerevisiae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term>
<term>Mating Factor</term>
<term>Membrane Proteins</term>
<term>Microtubule-Associated Proteins</term>
<term>Microtubules</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa</term>
<term>Saccharomyces cerevisiae Proteins</term>
<term>Transcription Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur de conjugaison</term>
<term>Facteurs de transcription</term>
<term>Microtubules</term>
<term>Noyau de la cellule</term>
<term>Protein-Serine-Threonine Kinases</term>
<term>Protéines associées aux microtubules</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines membranaires</term>
<term>Ribosomal Protein S6 Kinases, 70-kDa</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Active Transport, Cell Nucleus</term>
<term>Interphase</term>
<term>Kinetics</term>
<term>Mitosis</term>
<term>Phosphorylation</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term>
<term>Interphase</term>
<term>Mitose</term>
<term>Phosphorylation</term>
<term>Transduction du signal</term>
<term>Transport nucléaire actif</term>
</keywords>
</textClass>
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<front><div type="abstract" xml:lang="en">The target of rapamycin complex 1 (TORC1) is a highly conserved multiprotein complex that functions in many cellular processes, including cell growth and cell cycle progression. In this study, we define a novel role for TORC1 as a critical regulator of nuclear microtubule (MT) dynamics in the budding yeast <i>Saccharomyces cerevisiae</i>
 This activity requires interactions between EB1 and CLIP-170 plus end-tracking protein (+TIP) family members with the TORC1 subunit Kog1/Raptor, which in turn allow the TORC1 proximal kinase Sch9/S6K1 to regulate the MT polymerase Stu2/XMAP215. Sch9-dependent phosphorylation of Stu2 adjacent to a nuclear export signal prevents nuclear accumulation of Stu2 before cells enter mitosis. Mutants impaired in +TIP-TORC1 interactions or Stu2 nuclear export show increased nuclear but not cytoplasmic MT length and display nuclear fusion, spindle positioning, and elongation kinetics defects. Our results reveal key mechanisms by which TORC1 signaling controls Stu2 localization and thereby contributes to proper MT cytoskeletal organization in interphase and mitosis.</div>
</front>
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<Month>11</Month>
<Day>21</Day>
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<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<Issue>11</Issue>
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<Month>11</Month>
<Day>06</Day>
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</JournalIssue>
<Title>The Journal of cell biology</Title>
<ISOAbbreviation>J Cell Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.</ArticleTitle>
<Pagination><MedlinePgn>3471-3484</MedlinePgn>
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<Abstract><AbstractText>The target of rapamycin complex 1 (TORC1) is a highly conserved multiprotein complex that functions in many cellular processes, including cell growth and cell cycle progression. In this study, we define a novel role for TORC1 as a critical regulator of nuclear microtubule (MT) dynamics in the budding yeast <i>Saccharomyces cerevisiae</i>
 This activity requires interactions between EB1 and CLIP-170 plus end-tracking protein (+TIP) family members with the TORC1 subunit Kog1/Raptor, which in turn allow the TORC1 proximal kinase Sch9/S6K1 to regulate the MT polymerase Stu2/XMAP215. Sch9-dependent phosphorylation of Stu2 adjacent to a nuclear export signal prevents nuclear accumulation of Stu2 before cells enter mitosis. Mutants impaired in +TIP-TORC1 interactions or Stu2 nuclear export show increased nuclear but not cytoplasmic MT length and display nuclear fusion, spindle positioning, and elongation kinetics defects. Our results reveal key mechanisms by which TORC1 signaling controls Stu2 localization and thereby contributes to proper MT cytoskeletal organization in interphase and mitosis.</AbstractText>
<CopyrightInformation>© 2017 van der Vaart et al.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>van der Vaart</LastName>
<ForeName>Babet</ForeName>
<Initials>B</Initials>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
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<ForeName>Josef</ForeName>
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</AffiliationInfo>
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<ForeName>Christine</ForeName>
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</AffiliationInfo>
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<Initials>P</Initials>
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<Initials>K</Initials>
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<ForeName>René H</ForeName>
<Initials>RH</Initials>
<AffiliationInfo><Affiliation>Division of Cell Biology, The Netherlands Cancer Institute, Amsterdam, Netherlands.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Westermann</LastName>
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<Initials>S</Initials>
<Identifier Source="ORCID">0000-0001-6921-9113</Identifier>
<AffiliationInfo><Affiliation>Research Institute of Molecular Pathology, Vienna Biocenter, Vienna, Austria stefan.westermann@uni-due.de.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Molecular Genetics, Faculty of Biology, Center for Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.</Affiliation>
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   |texte=   TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.
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	Serveur d'exploration sur la rapamycine et les champignons
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TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.

TORC1 signaling exerts spatial control over microtubule dynamics by promoting nuclear export of Stu2.

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