Rab5 GTPases are required for optimal TORC2 function.
Identifieur interne : 000255 ( Main/Exploration ); précédent : 000254; suivant : 000256Rab5 GTPases are required for optimal TORC2 function.
Auteurs : Melissa N. Locke [États-Unis] ; Jeremy Thorner [États-Unis]Source :
- The Journal of cell biology [ 1540-8140 ] ; 2019.
Descripteurs français
- KwdFr :
- Complexe-2 cible mécanistique de la rapamycine (génétique), Complexe-2 cible mécanistique de la rapamycine (métabolisme), Facteurs d'échange de nucléotides guanyliques (génétique), Facteurs d'échange de nucléotides guanyliques (métabolisme), Glycogen Synthase Kinase 3 (génétique), Glycogen Synthase Kinase 3 (métabolisme), Protein kinases (génétique), Protein kinases (métabolisme), Protéines G rab (génétique), Protéines G rab (métabolisme), Protéines G rab5 (génétique), Protéines G rab5 (métabolisme), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Protéines du transport vésiculaire (génétique), Protéines du transport vésiculaire (métabolisme), Saccharomyces cerevisiae (enzymologie), Saccharomyces cerevisiae (génétique).
- MESH :
- enzymologie : Saccharomyces cerevisiae.
- génétique : Complexe-2 cible mécanistique de la rapamycine, Facteurs d'échange de nucléotides guanyliques, Glycogen Synthase Kinase 3, Protein kinases, Protéines G rab, Protéines G rab5, Protéines de Saccharomyces cerevisiae, Protéines du transport vésiculaire, Saccharomyces cerevisiae.
- métabolisme : Complexe-2 cible mécanistique de la rapamycine, Facteurs d'échange de nucléotides guanyliques, Glycogen Synthase Kinase 3, Protein kinases, Protéines G rab, Protéines G rab5, Protéines de Saccharomyces cerevisiae, Protéines du transport vésiculaire.
English descriptors
- KwdEn :
- Glycogen Synthase Kinase 3 (genetics), Glycogen Synthase Kinase 3 (metabolism), Guanine Nucleotide Exchange Factors (genetics), Guanine Nucleotide Exchange Factors (metabolism), Mechanistic Target of Rapamycin Complex 2 (genetics), Mechanistic Target of Rapamycin Complex 2 (metabolism), Protein Kinases (genetics), Protein Kinases (metabolism), Saccharomyces cerevisiae (enzymology), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Vesicular Transport Proteins (genetics), Vesicular Transport Proteins (metabolism), rab GTP-Binding Proteins (genetics), rab GTP-Binding Proteins (metabolism), rab5 GTP-Binding Proteins (genetics), rab5 GTP-Binding Proteins (metabolism).
- MESH :
- chemical , genetics : Glycogen Synthase Kinase 3, Guanine Nucleotide Exchange Factors, Mechanistic Target of Rapamycin Complex 2, Protein Kinases, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, rab GTP-Binding Proteins, rab5 GTP-Binding Proteins.
- chemical , metabolism : Glycogen Synthase Kinase 3, Guanine Nucleotide Exchange Factors, Mechanistic Target of Rapamycin Complex 2, Protein Kinases, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins, rab GTP-Binding Proteins, rab5 GTP-Binding Proteins.
- enzymology : Saccharomyces cerevisiae.
- genetics : Saccharomyces cerevisiae.
Abstract
Target of rapamycin complex-2 (TORC2), a conserved protein kinase complex, is an indispensable regulator of plasma membrane homeostasis. In budding yeast (Saccharomyces cerevisiae), the essential downstream effector of TORC2 is protein kinase Ypk1 and its paralog Ypk2. Muk1, a Rab5-specific guanine nucleotide exchange factor (GEF), was identified in our prior global screen for candidate Ypk1 targets. We confirm here that Muk1 is a substrate of Ypk1 and demonstrate that Ypk1-mediated phosphorylation stimulates Muk1 function in vivo. Strikingly, yeast lacking its two Rab5 GEFs (Muk1 and Vps9) or its three Rab5 paralogs (Vps21/Ypt51, Ypt52, and Ypt53) or overexpressing Msb3, a Rab5-directed GTPase-activating protein, all exhibit pronounced reduction in TORC2-mediated phosphorylation and activation of Ypk1. Vps21 coimmunoprecipitates with TORC2, and immuno-enriched TORC2 is less active in vitro in the absence of Rab5 GTPases. Thus, TORC2-dependent and Ypk1-mediated activation of Muk1 provides a control circuit for positive (self-reinforcing) up-regulation to sustain TORC2-Ypk1 signaling.
DOI: 10.1083/jcb.201807154
PubMed: 30578283
PubMed Central: PMC6400565
Affiliations:
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xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term><term>Facteurs d'échange de nucléotides guanyliques</term><term>Glycogen Synthase Kinase 3</term><term>Protein kinases</term><term>Protéines G rab</term><term>Protéines G rab5</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du transport vésiculaire</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Complexe-2 cible mécanistique de la rapamycine</term><term>Facteurs d'échange de nucléotides guanyliques</term><term>Glycogen Synthase Kinase 3</term><term>Protein kinases</term><term>Protéines G rab</term><term>Protéines G rab5</term><term>Protéines de Saccharomyces cerevisiae</term><term>Protéines du transport vésiculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Target of rapamycin complex-2 (TORC2), a conserved protein kinase complex, is an indispensable regulator of plasma membrane homeostasis. In budding yeast (<i>Saccharomyces cerevisiae</i>), the essential downstream effector of TORC2 is protein kinase Ypk1 and its paralog Ypk2. Muk1, a Rab5-specific guanine nucleotide exchange factor (GEF), was identified in our prior global screen for candidate Ypk1 targets. We confirm here that Muk1 is a substrate of Ypk1 and demonstrate that Ypk1-mediated phosphorylation stimulates Muk1 function in vivo. Strikingly, yeast lacking its two Rab5 GEFs (Muk1 and Vps9) or its three Rab5 paralogs (Vps21/Ypt51, Ypt52, and Ypt53) or overexpressing Msb3, a Rab5-directed GTPase-activating protein, all exhibit pronounced reduction in TORC2-mediated phosphorylation and activation of Ypk1. Vps21 coimmunoprecipitates with TORC2, and immuno-enriched TORC2 is less active in vitro in the absence of Rab5 GTPases. Thus, TORC2-dependent and Ypk1-mediated activation of Muk1 provides a control circuit for positive (self-reinforcing) up-regulation to sustain TORC2-Ypk1 signaling.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30578283</PMID><DateCompleted><Year>2020</Year><Month>02</Month><Day>26</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>09</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1540-8140</ISSN><JournalIssue CitedMedium="Internet"><Volume>218</Volume><Issue>3</Issue><PubDate><Year>2019</Year><Month>03</Month><Day>04</Day></PubDate></JournalIssue><Title>The Journal of cell biology</Title><ISOAbbreviation>J Cell Biol</ISOAbbreviation></Journal><ArticleTitle>Rab5 GTPases are required for optimal TORC2 function.</ArticleTitle><Pagination><MedlinePgn>961-976</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1083/jcb.201807154</ELocationID><Abstract><AbstractText>Target of rapamycin complex-2 (TORC2), a conserved protein kinase complex, is an indispensable regulator of plasma membrane homeostasis. In budding yeast (<i>Saccharomyces cerevisiae</i>), the essential downstream effector of TORC2 is protein kinase Ypk1 and its paralog Ypk2. Muk1, a Rab5-specific guanine nucleotide exchange factor (GEF), was identified in our prior global screen for candidate Ypk1 targets. We confirm here that Muk1 is a substrate of Ypk1 and demonstrate that Ypk1-mediated phosphorylation stimulates Muk1 function in vivo. Strikingly, yeast lacking its two Rab5 GEFs (Muk1 and Vps9) or its three Rab5 paralogs (Vps21/Ypt51, Ypt52, and Ypt53) or overexpressing Msb3, a Rab5-directed GTPase-activating protein, all exhibit pronounced reduction in TORC2-mediated phosphorylation and activation of Ypk1. Vps21 coimmunoprecipitates with TORC2, and immuno-enriched TORC2 is less active in vitro in the absence of Rab5 GTPases. Thus, TORC2-dependent and Ypk1-mediated activation of Muk1 provides a control circuit for positive (self-reinforcing) up-regulation to sustain TORC2-Ypk1 signaling.</AbstractText><CopyrightInformation>© 2019 Locke and Thorner.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Locke</LastName><ForeName>Melissa N</ForeName><Initials>MN</Initials><Identifier Source="ORCID">0000-0001-8162-1471</Identifier><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics, and Structural Biology and Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Thorner</LastName><ForeName>Jeremy</ForeName><Initials>J</Initials><Identifier Source="ORCID">0000-0002-2583-500X</Identifier><AffiliationInfo><Affiliation>Division of Biochemistry, Biophysics, and Structural Biology and Division of Cell and Developmental Biology, Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA jthorner@berkeley.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM021841</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>12</Month><Day>21</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Cell Biol</MedlineTA><NlmUniqueID>0375356</NlmUniqueID><ISSNLinking>0021-9525</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D020662">Guanine Nucleotide Exchange Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C583270">Muk1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C099285">VPS9 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D033921">Vesicular Transport Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.-</RegistryNumber><NameOfSubstance UI="D011494">Protein Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.1.-</RegistryNumber><NameOfSubstance UI="C060388">YPK2 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D000076225">Mechanistic Target of Rapamycin Complex 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.26</RegistryNumber><NameOfSubstance UI="D038362">Glycogen Synthase Kinase 3</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.12.1</RegistryNumber><NameOfSubstance UI="C068124">MCK1 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="C086866">VPS21 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020691">rab GTP-Binding Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.5.2</RegistryNumber><NameOfSubstance UI="D020696">rab5 GTP-Binding Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName 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