The Tap42-protein phosphatase type 2A catalytic subunit complex is required for cell cycle-dependent distribution of actin in yeast.
Identifieur interne : 001919 ( Main/Exploration ); précédent : 001918; suivant : 001920The Tap42-protein phosphatase type 2A catalytic subunit complex is required for cell cycle-dependent distribution of actin in yeast.
Auteurs : Huamin Wang [États-Unis] ; Yu JiangSource :
- Molecular and cellular biology [ 0270-7306 ] ; 2003.
Descripteurs français
- KwdFr :
- Actines (métabolisme), Cycle cellulaire (physiologie), Cytosquelette (effets des médicaments et des substances chimiques), Cytosquelette (génétique), Cytosquelette (métabolisme), Domaine catalytique (MeSH), Mutation (MeSH), Phosphoprotein Phosphatases (génétique), Phosphoprotein Phosphatases (métabolisme), Polarité de la cellule (MeSH), Protéines G monomériques (MeSH), Protéines G rho (MeSH), Protéines adaptatrices de la transduction du signal (MeSH), Protéines de Saccharomyces cerevisiae (génétique), Protéines de Saccharomyces cerevisiae (métabolisme), Régulation de l'expression des gènes fongiques (MeSH), Saccharomyces cerevisiae (cytologie), Saccharomyces cerevisiae (effets des médicaments et des substances chimiques), Saccharomyces cerevisiae (métabolisme), Sirolimus (pharmacologie), Sous-unités de protéines (MeSH), Structures macromoléculaires (MeSH).
- MESH :
- cytologie : Saccharomyces cerevisiae.
- effets des médicaments et des substances chimiques : Cytosquelette, Saccharomyces cerevisiae.
- génétique : Cytosquelette, Phosphoprotein Phosphatases, Protéines de Saccharomyces cerevisiae.
- métabolisme : Actines, Cytosquelette, Phosphoprotein Phosphatases, Protéines de Saccharomyces cerevisiae, Saccharomyces cerevisiae.
- pharmacologie : Sirolimus.
- physiologie : Cycle cellulaire.
- Domaine catalytique, Mutation, Polarité de la cellule, Protéines G monomériques, Protéines G rho, Protéines adaptatrices de la transduction du signal, Régulation de l'expression des gènes fongiques, Sous-unités de protéines, Structures macromoléculaires.
English descriptors
- KwdEn :
- Actins (metabolism), Adaptor Proteins, Signal Transducing (MeSH), Catalytic Domain (MeSH), Cell Cycle (physiology), Cell Polarity (MeSH), Cytoskeleton (drug effects), Cytoskeleton (genetics), Cytoskeleton (metabolism), Gene Expression Regulation, Fungal (MeSH), Macromolecular Substances (MeSH), Monomeric GTP-Binding Proteins (MeSH), Mutation (MeSH), Phosphoprotein Phosphatases (genetics), Phosphoprotein Phosphatases (metabolism), Protein Subunits (MeSH), Saccharomyces cerevisiae (cytology), Saccharomyces cerevisiae (drug effects), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (genetics), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (pharmacology), rho GTP-Binding Proteins (MeSH).
- MESH :
- chemical , genetics : Phosphoprotein Phosphatases, Saccharomyces cerevisiae Proteins.
- chemical , metabolism : Actins, Phosphoprotein Phosphatases, Saccharomyces cerevisiae Proteins.
- chemical , pharmacology : Sirolimus.
- chemical : Adaptor Proteins, Signal Transducing, Macromolecular Substances, Monomeric GTP-Binding Proteins, Protein Subunits, rho GTP-Binding Proteins.
- cytology : Saccharomyces cerevisiae.
- drug effects : Cytoskeleton, Saccharomyces cerevisiae.
- genetics : Cytoskeleton.
- metabolism : Cytoskeleton, Saccharomyces cerevisiae.
- physiology : Cell Cycle.
- Catalytic Domain, Cell Polarity, Gene Expression Regulation, Fungal, Mutation.
Abstract
In Saccharomyces cerevisiae, the Tor proteins mediate a wide spectrum of growth-related cellular processes in response to nutrients. The pleiotropic role of the Tor proteins is mediated, at least in part, by type 2A protein phosphatases (PP2A) and 2A-like protein phosphatases. Tor-mediated signaling activity promotes the interaction of phosphatase-interacting protein Tap42 with PP2A and 2A-like protein phosphatases. The distinct complexes formed between Tap42 and different phosphatases mediate various cellular events and modulate phosphorylation levels of many downstream factors in the Tor pathway in a Tor-dependent and rapamycin-sensitive manner. In this study, we demonstrate that the interaction between Tap42 and the catalytic subunits of PP2A (PP2Ac) is required for cell cycle-dependent distribution of actin. We show that mutations in PP2Ac and Tap42 that perturb the interaction cause random distribution of actin during the cell cycle and that overexpression of the Rho2 GTPase suppresses the actin defects associated with the mutants. Our findings suggest that the Tap42-PP2Ac complex regulates the actin cytoskeleton via a Rho GTPase-dependent mechanism. In addition, we provide evidence that PP2A activity plays a negative role in controlling the actin cytoskeleton and, possibly, in regulation of the G(2)/M transition of the cell cycle.
DOI: 10.1128/mcb.23.9.3116-3125.2003
PubMed: 12697813
PubMed Central: PMC153200
Affiliations:
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USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmacology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213</wicri:regionArea><wicri:noRegion>Pennsylvania 15213</wicri:noRegion></affiliation></author><author><name sortKey="Jiang, Yu" sort="Jiang, Yu" uniqKey="Jiang Y" first="Yu" last="Jiang">Yu Jiang</name></author></analytic><series><title level="j">Molecular and cellular biology</title><idno type="ISSN">0270-7306</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Actins (metabolism)</term><term>Adaptor Proteins, Signal Transducing (MeSH)</term><term>Catalytic Domain (MeSH)</term><term>Cell Cycle (physiology)</term><term>Cell Polarity (MeSH)</term><term>Cytoskeleton (drug effects)</term><term>Cytoskeleton (genetics)</term><term>Cytoskeleton (metabolism)</term><term>Gene Expression Regulation, Fungal (MeSH)</term><term>Macromolecular Substances (MeSH)</term><term>Monomeric GTP-Binding Proteins (MeSH)</term><term>Mutation (MeSH)</term><term>Phosphoprotein Phosphatases (genetics)</term><term>Phosphoprotein Phosphatases (metabolism)</term><term>Protein Subunits (MeSH)</term><term>Saccharomyces cerevisiae (cytology)</term><term>Saccharomyces cerevisiae (drug effects)</term><term>Saccharomyces cerevisiae (metabolism)</term><term>Saccharomyces cerevisiae Proteins (genetics)</term><term>Saccharomyces cerevisiae Proteins (metabolism)</term><term>Sirolimus (pharmacology)</term><term>rho GTP-Binding Proteins (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Actines (métabolisme)</term><term>Cycle cellulaire (physiologie)</term><term>Cytosquelette (effets des médicaments et des substances chimiques)</term><term>Cytosquelette (génétique)</term><term>Cytosquelette (métabolisme)</term><term>Domaine catalytique (MeSH)</term><term>Mutation (MeSH)</term><term>Phosphoprotein Phosphatases (génétique)</term><term>Phosphoprotein Phosphatases (métabolisme)</term><term>Polarité de la cellule (MeSH)</term><term>Protéines G monomériques (MeSH)</term><term>Protéines G rho (MeSH)</term><term>Protéines adaptatrices de la transduction du signal (MeSH)</term><term>Protéines de Saccharomyces cerevisiae (génétique)</term><term>Protéines de Saccharomyces cerevisiae (métabolisme)</term><term>Régulation de l'expression des gènes fongiques (MeSH)</term><term>Saccharomyces cerevisiae (cytologie)</term><term>Saccharomyces cerevisiae (effets des médicaments et des substances chimiques)</term><term>Saccharomyces cerevisiae (métabolisme)</term><term>Sirolimus (pharmacologie)</term><term>Sous-unités de protéines (MeSH)</term><term>Structures macromoléculaires (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Phosphoprotein Phosphatases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Actins</term><term>Phosphoprotein Phosphatases</term><term>Saccharomyces cerevisiae Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Sirolimus</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Adaptor Proteins, Signal Transducing</term><term>Macromolecular Substances</term><term>Monomeric GTP-Binding Proteins</term><term>Protein Subunits</term><term>rho GTP-Binding Proteins</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cytoskeleton</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Cytosquelette</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cytoskeleton</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cytosquelette</term><term>Phosphoprotein Phosphatases</term><term>Protéines de Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytoskeleton</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Actines</term><term>Cytosquelette</term><term>Phosphoprotein Phosphatases</term><term>Protéines de Saccharomyces cerevisiae</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Sirolimus</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cycle cellulaire</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cell Cycle</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Catalytic Domain</term><term>Cell Polarity</term><term>Gene Expression Regulation, Fungal</term><term>Mutation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Domaine catalytique</term><term>Mutation</term><term>Polarité de la cellule</term><term>Protéines G monomériques</term><term>Protéines G rho</term><term>Protéines adaptatrices de la transduction du signal</term><term>Régulation de l'expression des gènes fongiques</term><term>Sous-unités de protéines</term><term>Structures macromoléculaires</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In Saccharomyces cerevisiae, the Tor proteins mediate a wide spectrum of growth-related cellular processes in response to nutrients. The pleiotropic role of the Tor proteins is mediated, at least in part, by type 2A protein phosphatases (PP2A) and 2A-like protein phosphatases. Tor-mediated signaling activity promotes the interaction of phosphatase-interacting protein Tap42 with PP2A and 2A-like protein phosphatases. The distinct complexes formed between Tap42 and different phosphatases mediate various cellular events and modulate phosphorylation levels of many downstream factors in the Tor pathway in a Tor-dependent and rapamycin-sensitive manner. In this study, we demonstrate that the interaction between Tap42 and the catalytic subunits of PP2A (PP2Ac) is required for cell cycle-dependent distribution of actin. We show that mutations in PP2Ac and Tap42 that perturb the interaction cause random distribution of actin during the cell cycle and that overexpression of the Rho2 GTPase suppresses the actin defects associated with the mutants. Our findings suggest that the Tap42-PP2Ac complex regulates the actin cytoskeleton via a Rho GTPase-dependent mechanism. In addition, we provide evidence that PP2A activity plays a negative role in controlling the actin cytoskeleton and, possibly, in regulation of the G(2)/M transition of the cell cycle.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12697813</PMID><DateCompleted><Year>2003</Year><Month>05</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0270-7306</ISSN><JournalIssue CitedMedium="Print"><Volume>23</Volume><Issue>9</Issue><PubDate><Year>2003</Year><Month>May</Month></PubDate></JournalIssue><Title>Molecular and cellular biology</Title><ISOAbbreviation>Mol Cell Biol</ISOAbbreviation></Journal><ArticleTitle>The Tap42-protein phosphatase type 2A catalytic subunit complex is required for cell cycle-dependent distribution of actin in yeast.</ArticleTitle><Pagination><MedlinePgn>3116-25</MedlinePgn></Pagination><Abstract><AbstractText>In Saccharomyces cerevisiae, the Tor proteins mediate a wide spectrum of growth-related cellular processes in response to nutrients. The pleiotropic role of the Tor proteins is mediated, at least in part, by type 2A protein phosphatases (PP2A) and 2A-like protein phosphatases. Tor-mediated signaling activity promotes the interaction of phosphatase-interacting protein Tap42 with PP2A and 2A-like protein phosphatases. The distinct complexes formed between Tap42 and different phosphatases mediate various cellular events and modulate phosphorylation levels of many downstream factors in the Tor pathway in a Tor-dependent and rapamycin-sensitive manner. In this study, we demonstrate that the interaction between Tap42 and the catalytic subunits of PP2A (PP2Ac) is required for cell cycle-dependent distribution of actin. We show that mutations in PP2Ac and Tap42 that perturb the interaction cause random distribution of actin during the cell cycle and that overexpression of the Rho2 GTPase suppresses the actin defects associated with the mutants. Our findings suggest that the Tap42-PP2Ac complex regulates the actin cytoskeleton via a Rho GTPase-dependent mechanism. In addition, we provide evidence that PP2A activity plays a negative role in controlling the actin cytoskeleton and, possibly, in regulation of the G(2)/M transition of the cell cycle.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Huamin</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Pharmacology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15213, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Yu</ForeName><Initials>Y</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Mol Cell Biol</MedlineTA><NlmUniqueID>8109087</NlmUniqueID><ISSNLinking>0270-7306</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000199">Actins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046911">Macromolecular Substances</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D021122">Protein Subunits</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029701">Saccharomyces cerevisiae Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C100984">TAP42 protein, S cerevisiae</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.3.16</RegistryNumber><NameOfSubstance UI="D010749">Phosphoprotein 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MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002453" MajorTopicYN="N">Cell Cycle</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016764" MajorTopicYN="N">Cell Polarity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003599" MajorTopicYN="N">Cytoskeleton</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015966" MajorTopicYN="N">Gene Expression Regulation, Fungal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046911" MajorTopicYN="N">Macromolecular Substances</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020559" MajorTopicYN="Y">Monomeric GTP-Binding 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