Partial inhibition of Cdk1 in G 2 phase overrides the SAC and decouples mitotic events.
Identifieur interne : 003A29 ( PubMed/Corpus ); précédent : 003A28; suivant : 003A30Partial inhibition of Cdk1 in G 2 phase overrides the SAC and decouples mitotic events.
Auteurs : Rachael A. Mccloy ; Samuel Rogers ; C Elizabeth Caldon ; Thierry Lorca ; Anna Castro ; Andrew BurgessSource :
- Cell cycle (Georgetown, Tex.) [ 1551-4005 ] ; 2014.
English descriptors
- KwdEn :
- CDC2 Protein Kinase (antagonists & inhibitors), CDC2 Protein Kinase (metabolism), Centrosome (drug effects), Centrosome (metabolism), Cytokinesis, G2 Phase, HeLa Cells, Humans, Mitosis, Okadaic Acid (pharmacology), Phosphorylation, Polyploidy, Quinolines (pharmacology), Spindle Apparatus (physiology), Spindle Apparatus (ultrastructure), Thiazoles (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : CDC2 Protein Kinase.
- chemical , metabolism : CDC2 Protein Kinase.
- drug effects : Centrosome.
- metabolism : Centrosome.
- chemical , pharmacology : Okadaic Acid, Quinolines, Thiazoles.
- physiology : Spindle Apparatus.
- ultrastructure : Spindle Apparatus.
- Cytokinesis, G2 Phase, HeLa Cells, Humans, Mitosis, Phosphorylation, Polyploidy.
Abstract
Entry and progression through mitosis has traditionally been linked directly to the activity of cyclin-dependent kinase 1 (Cdk1). In this study we utilized low doses of the Cdk1-specific inhibitor, RO3306 from early G 2 phase onwards. Addition of low doses of RO3306 in G 2 phase induced minor chromosome congression and segregation defects. In contrast, mild doses of RO3306 during G 2 phase resulted in cells entering an aberrant mitosis, with cells fragmenting centrosomes and failing to fully disassemble the nuclear envelope. Cells often underwent cytokinesis and metaphase simultaneously, despite the presence of an active spindle assembly checkpoint, which prevented degradation of cyclin B1 and securin, resulting in the random partitioning of whole chromosomes. This highly aberrant mitosis produced a significant increase in the proportion of viable polyploid cells present up to 3 days post-treatment. Furthermore, cells treated with medium doses of RO3306 were only able to reach the threshold of Cdk1 substrate phosphorylation required to initiate nuclear envelope breakdown, but failed to reach the levels of phosphorylation required to correctly complete pro-metaphase. Treatment with low doses of Okadaic acid, which primarily inhibits PP2A, rescued the mitotic defects and increased the number of cells that completed a normal mitosis. This supports the current model that PP2A is the primary phosphatase that counterbalances the activity of Cdk1 during mitosis. Taken together these results show that continuous and subtle disruption of Cdk1 activity from G 2 phase onwards has deleterious consequences on mitotic progression by disrupting the balance between Cdk1 and PP2A.
DOI: 10.4161/cc.28401
PubMed: 24626186
Links to Exploration step
pubmed:24626186Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Partial inhibition of Cdk1 in G 2 phase overrides the SAC and decouples mitotic events.</title><author><name sortKey="Mccloy, Rachael A" sort="Mccloy, Rachael A" uniqKey="Mccloy R" first="Rachael A" last="Mccloy">Rachael A. Mccloy</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Rogers, Samuel" sort="Rogers, Samuel" uniqKey="Rogers S" first="Samuel" last="Rogers">Samuel Rogers</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Caldon, C Elizabeth" sort="Caldon, C Elizabeth" uniqKey="Caldon C" first="C Elizabeth" last="Caldon">C Elizabeth Caldon</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia; St. Vincent's Clinical School; Faculty of Medicine; UNSW; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Lorca, Thierry" sort="Lorca, Thierry" uniqKey="Lorca T" first="Thierry" last="Lorca">Thierry Lorca</name><affiliation><nlm:affiliation>Universités Montpellier 2 et 1; Centre de Recherche de Biochimie Macromoléculaire; CNRS UMR 5237; Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Castro, Anna" sort="Castro, Anna" uniqKey="Castro A" first="Anna" last="Castro">Anna Castro</name><affiliation><nlm:affiliation>Universités Montpellier 2 et 1; Centre de Recherche de Biochimie Macromoléculaire; CNRS UMR 5237; Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Burgess, Andrew" sort="Burgess, Andrew" uniqKey="Burgess A" first="Andrew" last="Burgess">Andrew Burgess</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia; St. Vincent's Clinical School; Faculty of Medicine; UNSW; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:24626186</idno><idno type="pmid">24626186</idno><idno type="doi">10.4161/cc.28401</idno><idno type="wicri:Area/PubMed/Corpus">003A29</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">003A29</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Partial inhibition of Cdk1 in G 2 phase overrides the SAC and decouples mitotic events.</title><author><name sortKey="Mccloy, Rachael A" sort="Mccloy, Rachael A" uniqKey="Mccloy R" first="Rachael A" last="Mccloy">Rachael A. Mccloy</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Rogers, Samuel" sort="Rogers, Samuel" uniqKey="Rogers S" first="Samuel" last="Rogers">Samuel Rogers</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Caldon, C Elizabeth" sort="Caldon, C Elizabeth" uniqKey="Caldon C" first="C Elizabeth" last="Caldon">C Elizabeth Caldon</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia; St. Vincent's Clinical School; Faculty of Medicine; UNSW; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author><author><name sortKey="Lorca, Thierry" sort="Lorca, Thierry" uniqKey="Lorca T" first="Thierry" last="Lorca">Thierry Lorca</name><affiliation><nlm:affiliation>Universités Montpellier 2 et 1; Centre de Recherche de Biochimie Macromoléculaire; CNRS UMR 5237; Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Castro, Anna" sort="Castro, Anna" uniqKey="Castro A" first="Anna" last="Castro">Anna Castro</name><affiliation><nlm:affiliation>Universités Montpellier 2 et 1; Centre de Recherche de Biochimie Macromoléculaire; CNRS UMR 5237; Montpellier, France.</nlm:affiliation></affiliation></author><author><name sortKey="Burgess, Andrew" sort="Burgess, Andrew" uniqKey="Burgess A" first="Andrew" last="Burgess">Andrew Burgess</name><affiliation><nlm:affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia; St. Vincent's Clinical School; Faculty of Medicine; UNSW; Sydney, New South Wales, Australia.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Cell cycle (Georgetown, Tex.)</title><idno type="eISSN">1551-4005</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>CDC2 Protein Kinase (antagonists & inhibitors)</term><term>CDC2 Protein Kinase (metabolism)</term><term>Centrosome (drug effects)</term><term>Centrosome (metabolism)</term><term>Cytokinesis</term><term>G2 Phase</term><term>HeLa Cells</term><term>Humans</term><term>Mitosis</term><term>Okadaic Acid (pharmacology)</term><term>Phosphorylation</term><term>Polyploidy</term><term>Quinolines (pharmacology)</term><term>Spindle Apparatus (physiology)</term><term>Spindle Apparatus (ultrastructure)</term><term>Thiazoles (pharmacology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>CDC2 Protein Kinase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>CDC2 Protein Kinase</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Centrosome</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Centrosome</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Okadaic Acid</term><term>Quinolines</term><term>Thiazoles</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Spindle Apparatus</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Spindle Apparatus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cytokinesis</term><term>G2 Phase</term><term>HeLa Cells</term><term>Humans</term><term>Mitosis</term><term>Phosphorylation</term><term>Polyploidy</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Entry and progression through mitosis has traditionally been linked directly to the activity of cyclin-dependent kinase 1 (Cdk1). In this study we utilized low doses of the Cdk1-specific inhibitor, RO3306 from early G 2 phase onwards. Addition of low doses of RO3306 in G 2 phase induced minor chromosome congression and segregation defects. In contrast, mild doses of RO3306 during G 2 phase resulted in cells entering an aberrant mitosis, with cells fragmenting centrosomes and failing to fully disassemble the nuclear envelope. Cells often underwent cytokinesis and metaphase simultaneously, despite the presence of an active spindle assembly checkpoint, which prevented degradation of cyclin B1 and securin, resulting in the random partitioning of whole chromosomes. This highly aberrant mitosis produced a significant increase in the proportion of viable polyploid cells present up to 3 days post-treatment. Furthermore, cells treated with medium doses of RO3306 were only able to reach the threshold of Cdk1 substrate phosphorylation required to initiate nuclear envelope breakdown, but failed to reach the levels of phosphorylation required to correctly complete pro-metaphase. Treatment with low doses of Okadaic acid, which primarily inhibits PP2A, rescued the mitotic defects and increased the number of cells that completed a normal mitosis. This supports the current model that PP2A is the primary phosphatase that counterbalances the activity of Cdk1 during mitosis. Taken together these results show that continuous and subtle disruption of Cdk1 activity from G 2 phase onwards has deleterious consequences on mitotic progression by disrupting the balance between Cdk1 and PP2A.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24626186</PMID><DateCreated><Year>2014</Year><Month>05</Month><Day>05</Day></DateCreated><DateCompleted><Year>2016</Year><Month>04</Month><Day>28</Day></DateCompleted><DateRevised><Year>2017</Year><Month>02</Month><Day>20</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1551-4005</ISSN><JournalIssue CitedMedium="Internet"><Volume>13</Volume><Issue>9</Issue><PubDate><Year>2014</Year></PubDate></JournalIssue><Title>Cell cycle (Georgetown, Tex.)</Title><ISOAbbreviation>Cell Cycle</ISOAbbreviation></Journal><ArticleTitle>Partial inhibition of Cdk1 in G 2 phase overrides the SAC and decouples mitotic events.</ArticleTitle><Pagination><MedlinePgn>1400-12</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4161/cc.28401</ELocationID><Abstract><AbstractText>Entry and progression through mitosis has traditionally been linked directly to the activity of cyclin-dependent kinase 1 (Cdk1). In this study we utilized low doses of the Cdk1-specific inhibitor, RO3306 from early G 2 phase onwards. Addition of low doses of RO3306 in G 2 phase induced minor chromosome congression and segregation defects. In contrast, mild doses of RO3306 during G 2 phase resulted in cells entering an aberrant mitosis, with cells fragmenting centrosomes and failing to fully disassemble the nuclear envelope. Cells often underwent cytokinesis and metaphase simultaneously, despite the presence of an active spindle assembly checkpoint, which prevented degradation of cyclin B1 and securin, resulting in the random partitioning of whole chromosomes. This highly aberrant mitosis produced a significant increase in the proportion of viable polyploid cells present up to 3 days post-treatment. Furthermore, cells treated with medium doses of RO3306 were only able to reach the threshold of Cdk1 substrate phosphorylation required to initiate nuclear envelope breakdown, but failed to reach the levels of phosphorylation required to correctly complete pro-metaphase. Treatment with low doses of Okadaic acid, which primarily inhibits PP2A, rescued the mitotic defects and increased the number of cells that completed a normal mitosis. This supports the current model that PP2A is the primary phosphatase that counterbalances the activity of Cdk1 during mitosis. Taken together these results show that continuous and subtle disruption of Cdk1 activity from G 2 phase onwards has deleterious consequences on mitotic progression by disrupting the balance between Cdk1 and PP2A.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>McCloy</LastName><ForeName>Rachael A</ForeName><Initials>RA</Initials><AffiliationInfo><Affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rogers</LastName><ForeName>Samuel</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Caldon</LastName><ForeName>C Elizabeth</ForeName><Initials>CE</Initials><AffiliationInfo><Affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia; St. Vincent's Clinical School; Faculty of Medicine; UNSW; Sydney, New South Wales, Australia.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lorca</LastName><ForeName>Thierry</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Universités Montpellier 2 et 1; Centre de Recherche de Biochimie Macromoléculaire; CNRS UMR 5237; Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Castro</LastName><ForeName>Anna</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Universités Montpellier 2 et 1; Centre de Recherche de Biochimie Macromoléculaire; CNRS UMR 5237; Montpellier, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Burgess</LastName><ForeName>Andrew</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>The Kinghorn Cancer Centre; Garvan Institute of Medical Research; Sydney, New South Wales, Australia; St. Vincent's Clinical School; Faculty of Medicine; UNSW; Sydney, New South Wales, Australia.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>03</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell Cycle</MedlineTA><NlmUniqueID>101137841</NlmUniqueID><ISSNLinking>1551-4005</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011804">Quinolines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C512984">RO 3306</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013844">Thiazoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>1W21G5Q4N2</RegistryNumber><NameOfSubstance UI="D019319">Okadaic Acid</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.22</RegistryNumber><NameOfSubstance UI="D016203">CDC2 Protein Kinase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Proc Natl Acad Sci U S A. 2013 Oct 22;110(43):17374-9</RefSource><PMID Version="1">24101512</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Cell Prolif. 2011 Oct;44(5):391-400</RefSource><PMID Version="1">21951282</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>PLoS One. 2012;7(9):e45726</RefSource><PMID Version="1">23029203</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Cell Biol. 2009 Apr 20;185(2):193-202</RefSource><PMID 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Version="1">19696736</PMID></CommentsCorrections></CommentsCorrectionsList><MeshHeadingList><MeshHeading><DescriptorName UI="D016203" MajorTopicYN="N">CDC2 Protein Kinase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018385" MajorTopicYN="N">Centrosome</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D048749" MajorTopicYN="N">Cytokinesis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016195" MajorTopicYN="Y">G2 Phase</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008938" MajorTopicYN="Y">Mitosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019319" MajorTopicYN="N">Okadaic Acid</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010766" MajorTopicYN="N">Phosphorylation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011123" MajorTopicYN="N">Polyploidy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011804" MajorTopicYN="N">Quinolines</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008941" MajorTopicYN="N">Spindle Apparatus</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013844" 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IdType="pubmed">24626186</ArticleId><ArticleId IdType="pii">28401</ArticleId><ArticleId IdType="doi">10.4161/cc.28401</ArticleId><ArticleId IdType="pmc">PMC4050138</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Partial inhibition of Cdk1 in G 2 phase overrides the SAC and decouples mitotic events.
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