The spindle pole body plays a key role in controlling mitotic commitment in the fission yeast Schizosaccharomyces pombe.
Identifieur interne : 001573 ( Main/Exploration ); précédent : 001572; suivant : 001574The spindle pole body plays a key role in controlling mitotic commitment in the fission yeast Schizosaccharomyces pombe.
Auteurs : Iain M. Hagan [Royaume-Uni]Source :
- Biochemical Society transactions [ 0300-5127 ] ; 2008.
Descripteurs français
- KwdFr :
- Activation enzymatique (MeSH), Appareil du fuseau (métabolisme), Facteur de promotion de la maturation (métabolisme), Mitogen-Activated Protein Kinases (métabolisme), Mitose (physiologie), Phosphoprotéines (métabolisme), Protein kinases (métabolisme), Protein-Serine-Threonine Kinases (métabolisme), Protéines associées aux microtubules (métabolisme), Protéines de Schizosaccharomyces pombe (métabolisme), Schizosaccharomyces (cytologie), Schizosaccharomyces (physiologie), Transduction du signal (physiologie).
- MESH :
- cytologie : Schizosaccharomyces.
- métabolisme : Appareil du fuseau, Facteur de promotion de la maturation, Mitogen-Activated Protein Kinases, Phosphoprotéines, Protein kinases, Protein-Serine-Threonine Kinases, Protéines associées aux microtubules, Protéines de Schizosaccharomyces pombe.
- physiologie : Mitose, Schizosaccharomyces, Transduction du signal.
- Activation enzymatique.
English descriptors
- KwdEn :
- Enzyme Activation (MeSH), Maturation-Promoting Factor (metabolism), Microtubule-Associated Proteins (metabolism), Mitogen-Activated Protein Kinases (metabolism), Mitosis (physiology), Phosphoproteins (metabolism), Protein Kinases (metabolism), Protein-Serine-Threonine Kinases (metabolism), Schizosaccharomyces (cytology), Schizosaccharomyces (physiology), Schizosaccharomyces pombe Proteins (metabolism), Signal Transduction (physiology), Spindle Apparatus (metabolism).
- MESH :
- chemical , metabolism : Maturation-Promoting Factor, Microtubule-Associated Proteins, Mitogen-Activated Protein Kinases, Phosphoproteins, Protein Kinases, Protein-Serine-Threonine Kinases, Schizosaccharomyces pombe Proteins.
- cytology : Schizosaccharomyces.
- metabolism : Spindle Apparatus.
- physiology : Mitosis, Schizosaccharomyces, Signal Transduction.
- Enzyme Activation.
Abstract
Commitment to mitosis is regulated by a conserved protein kinase complex called MPF (mitosis-promoting factor). MPF activation triggers a positive-feedback loop that further promotes the activity of its activating phosphatase Cdc25 and is assumed to down-regulate the MPF-inhibitory kinase Wee1. Four protein kinases contribute to this amplification loop: MPF itself, Polo kinase, MAPK (mitogen-activated protein kinase) and Greatwall kinase. The fission yeast SPB (spindle pole body) component Cut12 plays a critical role in modulating mitotic commitment. In this review, I discuss the relationship between Cut12 and the fission yeast Polo kinase Plo1 in mitotic control. These results indicate that commitment to mitosis is co-ordinated by control networks on the spindle pole. I then describe how the Cut12/Plo1 control network links growth control signalling from TOR (target of rapamycin) and MAPK networks to the activation of MPF to regulate the timing of cell division.
DOI: 10.1042/BST0361097
PubMed: 18793196
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Hagan</name><affiliation wicri:level="4"><nlm:affiliation>CRUK (Cancer Research UK) Cell Division Laboratory, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK. ihagan@picr.man.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>CRUK (Cancer Research UK) Cell Division Laboratory, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX</wicri:regionArea><orgName type="university">Université de Manchester</orgName><placeName><settlement type="city">Manchester</settlement><region type="nation">Angleterre</region><region nuts="2" type="region">Grand Manchester</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18793196</idno><idno type="pmid">18793196</idno><idno type="doi">10.1042/BST0361097</idno><idno type="wicri:Area/Main/Corpus">001572</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001572</idno><idno type="wicri:Area/Main/Curation">001572</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001572</idno><idno type="wicri:Area/Main/Exploration">001572</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The spindle pole body plays a key role in controlling mitotic commitment in the fission yeast Schizosaccharomyces pombe.</title><author><name sortKey="Hagan, Iain M" sort="Hagan, Iain M" uniqKey="Hagan I" first="Iain M" last="Hagan">Iain M. Hagan</name><affiliation wicri:level="4"><nlm:affiliation>CRUK (Cancer Research UK) Cell Division Laboratory, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK. ihagan@picr.man.ac.uk</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>CRUK (Cancer Research UK) Cell Division Laboratory, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX</wicri:regionArea><orgName type="university">Université de Manchester</orgName><placeName><settlement type="city">Manchester</settlement><region type="nation">Angleterre</region><region nuts="2" type="region">Grand Manchester</region></placeName></affiliation></author></analytic><series><title level="j">Biochemical Society transactions</title><idno type="ISSN">0300-5127</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Enzyme Activation (MeSH)</term><term>Maturation-Promoting Factor (metabolism)</term><term>Microtubule-Associated Proteins (metabolism)</term><term>Mitogen-Activated Protein Kinases (metabolism)</term><term>Mitosis (physiology)</term><term>Phosphoproteins (metabolism)</term><term>Protein Kinases (metabolism)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Schizosaccharomyces (cytology)</term><term>Schizosaccharomyces (physiology)</term><term>Schizosaccharomyces pombe Proteins (metabolism)</term><term>Signal Transduction (physiology)</term><term>Spindle Apparatus (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Activation enzymatique (MeSH)</term><term>Appareil du fuseau (métabolisme)</term><term>Facteur de promotion de la maturation (métabolisme)</term><term>Mitogen-Activated Protein Kinases (métabolisme)</term><term>Mitose (physiologie)</term><term>Phosphoprotéines (métabolisme)</term><term>Protein kinases (métabolisme)</term><term>Protein-Serine-Threonine Kinases (métabolisme)</term><term>Protéines associées aux microtubules (métabolisme)</term><term>Protéines de Schizosaccharomyces pombe (métabolisme)</term><term>Schizosaccharomyces (cytologie)</term><term>Schizosaccharomyces (physiologie)</term><term>Transduction du signal (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Maturation-Promoting Factor</term><term>Microtubule-Associated Proteins</term><term>Mitogen-Activated Protein Kinases</term><term>Phosphoproteins</term><term>Protein Kinases</term><term>Protein-Serine-Threonine Kinases</term><term>Schizosaccharomyces pombe Proteins</term></keywords><keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Schizosaccharomyces</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Spindle Apparatus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil du fuseau</term><term>Facteur de promotion de la maturation</term><term>Mitogen-Activated Protein Kinases</term><term>Phosphoprotéines</term><term>Protein kinases</term><term>Protein-Serine-Threonine Kinases</term><term>Protéines associées aux microtubules</term><term>Protéines de Schizosaccharomyces pombe</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Mitose</term><term>Schizosaccharomyces</term><term>Transduction du signal</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Mitosis</term><term>Schizosaccharomyces</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Enzyme Activation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Activation enzymatique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Commitment to mitosis is regulated by a conserved protein kinase complex called MPF (mitosis-promoting factor). MPF activation triggers a positive-feedback loop that further promotes the activity of its activating phosphatase Cdc25 and is assumed to down-regulate the MPF-inhibitory kinase Wee1. Four protein kinases contribute to this amplification loop: MPF itself, Polo kinase, MAPK (mitogen-activated protein kinase) and Greatwall kinase. The fission yeast SPB (spindle pole body) component Cut12 plays a critical role in modulating mitotic commitment. In this review, I discuss the relationship between Cut12 and the fission yeast Polo kinase Plo1 in mitotic control. These results indicate that commitment to mitosis is co-ordinated by control networks on the spindle pole. I then describe how the Cut12/Plo1 control network links growth control signalling from TOR (target of rapamycin) and MAPK networks to the activation of MPF to regulate the timing of cell division.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18793196</PMID><DateCompleted><Year>2008</Year><Month>11</Month><Day>12</Day></DateCompleted><DateRevised><Year>2013</Year><Month>11</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0300-5127</ISSN><JournalIssue CitedMedium="Print"><Volume>36</Volume><Issue>Pt 5</Issue><PubDate><Year>2008</Year><Month>Oct</Month></PubDate></JournalIssue><Title>Biochemical Society transactions</Title><ISOAbbreviation>Biochem Soc Trans</ISOAbbreviation></Journal><ArticleTitle>The spindle pole body plays a key role in controlling mitotic commitment in the fission yeast Schizosaccharomyces pombe.</ArticleTitle><Pagination><MedlinePgn>1097-101</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1042/BST0361097</ELocationID><Abstract><AbstractText>Commitment to mitosis is regulated by a conserved protein kinase complex called MPF (mitosis-promoting factor). MPF activation triggers a positive-feedback loop that further promotes the activity of its activating phosphatase Cdc25 and is assumed to down-regulate the MPF-inhibitory kinase Wee1. Four protein kinases contribute to this amplification loop: MPF itself, Polo kinase, MAPK (mitogen-activated protein kinase) and Greatwall kinase. The fission yeast SPB (spindle pole body) component Cut12 plays a critical role in modulating mitotic commitment. In this review, I discuss the relationship between Cut12 and the fission yeast Polo kinase Plo1 in mitotic control. These results indicate that commitment to mitosis is co-ordinated by control networks on the spindle pole. I then describe how the Cut12/Plo1 control network links growth control signalling from TOR (target of rapamycin) and MAPK networks to the activation of MPF to regulate the timing of cell division.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hagan</LastName><ForeName>Iain M</ForeName><Initials>IM</Initials><AffiliationInfo><Affiliation>CRUK (Cancer Research UK) Cell Division Laboratory, Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester M20 4BX, UK. ihagan@picr.man.ac.uk</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>C147/A6058</GrantID><Agency>Cancer Research UK</Agency><Country>United Kingdom</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Biochem Soc Trans</MedlineTA><NlmUniqueID>7506897</NlmUniqueID><ISSNLinking>0300-5127</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C111708">Cut12 protein, S pombe</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008869">Microtubule-Associated Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010750">Phosphoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029702">Schizosaccharomyces pombe 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="C523461">Tor1 protein, S 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UI="D008869" MajorTopicYN="N">Microtubule-Associated Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020928" MajorTopicYN="N">Mitogen-Activated Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008938" MajorTopicYN="N">Mitosis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010750" MajorTopicYN="N">Phosphoproteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011494" MajorTopicYN="N">Protein Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012568" MajorTopicYN="N">Schizosaccharomyces</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029702" MajorTopicYN="N">Schizosaccharomyces pombe Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008941" MajorTopicYN="N">Spindle Apparatus</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><NumberOfReferences>51</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2008</Year><Month>9</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2008</Year><Month>11</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2008</Year><Month>9</Month><Day>17</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">18793196</ArticleId><ArticleId IdType="pii">BST0361097</ArticleId><ArticleId IdType="doi">10.1042/BST0361097</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country><region><li>Angleterre</li><li>Grand Manchester</li></region><settlement><li>Manchester</li></settlement><orgName><li>Université de Manchester</li></orgName></list><tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Hagan, Iain M" sort="Hagan, Iain M" uniqKey="Hagan I" first="Iain M" last="Hagan">Iain M. 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