Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation
Aurora B regulates chromosome segregation and cytokinesis and is the first protein to be implicated as a regulator of bipolar attachment of spindle microtubules to kinetochores. Evidence from several systems suggests that Aurora B is physically associated with inner centromere protein (INCENP) in mi...
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| Veröffentlicht in: | Molecular biology of the cell 2002-09, Vol.13 (9), p.3064-3077 |
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| container_title | Molecular biology of the cell |
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| creator | Bolton, Margaret A Lan, Weijie Powers, Shannon E McCleland, Mark L Kuang, Jian Stukenberg, P Todd |
| description | Aurora B regulates chromosome segregation and cytokinesis and is the first protein to be implicated as a regulator of bipolar attachment of spindle microtubules to kinetochores. Evidence from several systems suggests that Aurora B is physically associated with inner centromere protein (INCENP) in mitosis and has genetic interactions with Survivin. It is unclear whether the Aurora B and INCENP interaction is cell cycle regulated and if Survivin physically interacts in this complex. In this study, we cloned the Xenopus Survivin gene, examined its association with Aurora B and INCENP, and determined the effect of its binding on Aurora B kinase activity. We demonstrate that in the Xenopus early embryo, all of the detectable Survivin is in a complex with both Aurora B and INCENP throughout the cell cycle. Survivin and Aurora B bind different domains on INCENP. Aurora B activity is stimulated >10-fold in mitotic extracts; this activation is phosphatase sensitive, and the binding of Survivin is required for full Aurora B activity. We also find the hydrodynamic properties of the Aurora B/Survivin/INCENP complex are cell cycle regulated. Our data indicate that Aurora B kinase activity is regulated by both Survivin binding and cell cycle-dependent phosphorylation. |
| doi_str_mv | 10.1091/mbc.E02-02-0092 |
| format | Article |
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Evidence from several systems suggests that Aurora B is physically associated with inner centromere protein (INCENP) in mitosis and has genetic interactions with Survivin. It is unclear whether the Aurora B and INCENP interaction is cell cycle regulated and if Survivin physically interacts in this complex. In this study, we cloned the Xenopus Survivin gene, examined its association with Aurora B and INCENP, and determined the effect of its binding on Aurora B kinase activity. We demonstrate that in the Xenopus early embryo, all of the detectable Survivin is in a complex with both Aurora B and INCENP throughout the cell cycle. Survivin and Aurora B bind different domains on INCENP. Aurora B activity is stimulated >10-fold in mitotic extracts; this activation is phosphatase sensitive, and the binding of Survivin is required for full Aurora B activity. We also find the hydrodynamic properties of the Aurora B/Survivin/INCENP complex are cell cycle regulated. Our data indicate that Aurora B kinase activity is regulated by both Survivin binding and cell cycle-dependent phosphorylation.</description><identifier>ISSN: 1059-1524</identifier><identifier>EISSN: 1939-4586</identifier><identifier>DOI: 10.1091/mbc.E02-02-0092</identifier><identifier>PMID: 12221116</identifier><language>eng</language><publisher>United States: The American Society for Cell Biology</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies - metabolism ; Aurora Kinase B ; Aurora Kinases ; Cell Cycle ; Cells, Cultured ; Chromatography, Gel ; Chromosomal Proteins, Non-Histone - metabolism ; Cloning, Molecular ; Dose-Response Relationship, Drug ; Glutathione Transferase - metabolism ; Humans ; Immunoblotting ; Inhibitor of Apoptosis Proteins ; Microscopy, Fluorescence ; Microtubule-Associated Proteins - chemistry ; Microtubule-Associated Proteins - genetics ; Microtubule-Associated Proteins - metabolism ; Mitosis ; Models, Molecular ; Molecular Sequence Data ; Neoplasm Proteins ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases - chemistry ; Protein-Serine-Threonine Kinases - metabolism ; Recombinant Fusion Proteins - metabolism ; Sequence Homology, Amino Acid ; Xenopus ; Xenopus laevis</subject><ispartof>Molecular biology of the cell, 2002-09, Vol.13 (9), p.3064-3077</ispartof><rights>Copyright © 2002, The American Society for Cell Biology 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4112-90405db0db5e66150483bdb82baa6189350985961d2f6005b6490874d971cb743</citedby><cites>FETCH-LOGICAL-c4112-90405db0db5e66150483bdb82baa6189350985961d2f6005b6490874d971cb743</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC124143/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC124143/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12221116$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Yanagida, Mitsuhiro</contributor><creatorcontrib>Bolton, Margaret A</creatorcontrib><creatorcontrib>Lan, Weijie</creatorcontrib><creatorcontrib>Powers, Shannon E</creatorcontrib><creatorcontrib>McCleland, Mark L</creatorcontrib><creatorcontrib>Kuang, Jian</creatorcontrib><creatorcontrib>Stukenberg, P Todd</creatorcontrib><title>Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation</title><title>Molecular biology of the cell</title><addtitle>Mol Biol Cell</addtitle><description>Aurora B regulates chromosome segregation and cytokinesis and is the first protein to be implicated as a regulator of bipolar attachment of spindle microtubules to kinetochores. Evidence from several systems suggests that Aurora B is physically associated with inner centromere protein (INCENP) in mitosis and has genetic interactions with Survivin. It is unclear whether the Aurora B and INCENP interaction is cell cycle regulated and if Survivin physically interacts in this complex. In this study, we cloned the Xenopus Survivin gene, examined its association with Aurora B and INCENP, and determined the effect of its binding on Aurora B kinase activity. We demonstrate that in the Xenopus early embryo, all of the detectable Survivin is in a complex with both Aurora B and INCENP throughout the cell cycle. Survivin and Aurora B bind different domains on INCENP. Aurora B activity is stimulated >10-fold in mitotic extracts; this activation is phosphatase sensitive, and the binding of Survivin is required for full Aurora B activity. We also find the hydrodynamic properties of the Aurora B/Survivin/INCENP complex are cell cycle regulated. Our data indicate that Aurora B kinase activity is regulated by both Survivin binding and cell cycle-dependent phosphorylation.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies - metabolism</subject><subject>Aurora Kinase B</subject><subject>Aurora Kinases</subject><subject>Cell Cycle</subject><subject>Cells, Cultured</subject><subject>Chromatography, Gel</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>Cloning, Molecular</subject><subject>Dose-Response Relationship, Drug</subject><subject>Glutathione Transferase - metabolism</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Inhibitor of Apoptosis Proteins</subject><subject>Microscopy, Fluorescence</subject><subject>Microtubule-Associated Proteins - chemistry</subject><subject>Microtubule-Associated Proteins - genetics</subject><subject>Microtubule-Associated Proteins - metabolism</subject><subject>Mitosis</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Neoplasm Proteins</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Protein-Serine-Threonine Kinases - chemistry</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Xenopus</subject><subject>Xenopus laevis</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFvFCEUx4nR2Fo9ezOcvE37HgPMcPBQN2tt0lQPeiYwsF10hllhZtv9Cn7qsu3G6snkEV7g93uB_Al5i3CKoPBssN3pEli1L1DsGTlGVauKi1Y-Lz0IVaFg_Ii8yvkHAHIum5fkCBljiCiPye_zOY3J0I_0Z4gme-rvQp4yDZEa2o3Dpvd39DZMa5rntA3b_Xl09PJ6sbz--tCGQh9c002FmHY0ZJqnMMy9mbyjdvck2xBdiDcP5mY95rLSrmBhjK_Ji5Xps39z2E_I90_Lb4vP1dWXi8vF-VXVcURWKeAgnAVnhZcSBfC2ts62zBojsVW1ANUKJdGxlQQQVnIFbcOdarCzDa9PyIfHuZvZDt51Pk7J9HqTwmDSTo8m6H9vYljrm3GrkXHkdfHfH_w0_pp9nvQQcuf73kQ_zlk3DFrgDP8LMmi44IwV8OwR7NKYc_KrP49B0PucdclZe2B6XyXnYrz7-w9P_CHY-h5tLaXq</recordid><startdate>200209</startdate><enddate>200209</enddate><creator>Bolton, Margaret A</creator><creator>Lan, Weijie</creator><creator>Powers, Shannon E</creator><creator>McCleland, Mark L</creator><creator>Kuang, Jian</creator><creator>Stukenberg, P Todd</creator><general>The American Society for Cell Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200209</creationdate><title>Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation</title><author>Bolton, Margaret A ; Lan, Weijie ; Powers, Shannon E ; McCleland, Mark L ; Kuang, Jian ; Stukenberg, P Todd</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4112-90405db0db5e66150483bdb82baa6189350985961d2f6005b6490874d971cb743</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies - metabolism</topic><topic>Aurora Kinase B</topic><topic>Aurora Kinases</topic><topic>Cell Cycle</topic><topic>Cells, Cultured</topic><topic>Chromatography, Gel</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>Cloning, Molecular</topic><topic>Dose-Response Relationship, Drug</topic><topic>Glutathione Transferase - metabolism</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Inhibitor of Apoptosis Proteins</topic><topic>Microscopy, Fluorescence</topic><topic>Microtubule-Associated Proteins - chemistry</topic><topic>Microtubule-Associated Proteins - genetics</topic><topic>Microtubule-Associated Proteins - metabolism</topic><topic>Mitosis</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Neoplasm Proteins</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Protein-Serine-Threonine Kinases - chemistry</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Xenopus</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bolton, Margaret A</creatorcontrib><creatorcontrib>Lan, Weijie</creatorcontrib><creatorcontrib>Powers, Shannon E</creatorcontrib><creatorcontrib>McCleland, Mark L</creatorcontrib><creatorcontrib>Kuang, Jian</creatorcontrib><creatorcontrib>Stukenberg, P Todd</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bolton, Margaret A</au><au>Lan, Weijie</au><au>Powers, Shannon E</au><au>McCleland, Mark L</au><au>Kuang, Jian</au><au>Stukenberg, P Todd</au><au>Yanagida, Mitsuhiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>2002-09</date><risdate>2002</risdate><volume>13</volume><issue>9</issue><spage>3064</spage><epage>3077</epage><pages>3064-3077</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>Aurora B regulates chromosome segregation and cytokinesis and is the first protein to be implicated as a regulator of bipolar attachment of spindle microtubules to kinetochores. Evidence from several systems suggests that Aurora B is physically associated with inner centromere protein (INCENP) in mitosis and has genetic interactions with Survivin. It is unclear whether the Aurora B and INCENP interaction is cell cycle regulated and if Survivin physically interacts in this complex. In this study, we cloned the Xenopus Survivin gene, examined its association with Aurora B and INCENP, and determined the effect of its binding on Aurora B kinase activity. We demonstrate that in the Xenopus early embryo, all of the detectable Survivin is in a complex with both Aurora B and INCENP throughout the cell cycle. Survivin and Aurora B bind different domains on INCENP. Aurora B activity is stimulated >10-fold in mitotic extracts; this activation is phosphatase sensitive, and the binding of Survivin is required for full Aurora B activity. We also find the hydrodynamic properties of the Aurora B/Survivin/INCENP complex are cell cycle regulated. Our data indicate that Aurora B kinase activity is regulated by both Survivin binding and cell cycle-dependent phosphorylation.</abstract><cop>United States</cop><pub>The American Society for Cell Biology</pub><pmid>12221116</pmid><doi>10.1091/mbc.E02-02-0092</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Animals Antibodies - metabolism Aurora Kinase B Aurora Kinases Cell Cycle Cells, Cultured Chromatography, Gel Chromosomal Proteins, Non-Histone - metabolism Cloning, Molecular Dose-Response Relationship, Drug Glutathione Transferase - metabolism Humans Immunoblotting Inhibitor of Apoptosis Proteins Microscopy, Fluorescence Microtubule-Associated Proteins - chemistry Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Mitosis Models, Molecular Molecular Sequence Data Neoplasm Proteins Phosphorylation Protein Binding Protein Structure, Tertiary Protein-Serine-Threonine Kinases - chemistry Protein-Serine-Threonine Kinases - metabolism Recombinant Fusion Proteins - metabolism Sequence Homology, Amino Acid Xenopus Xenopus laevis |
| title | Aurora B kinase exists in a complex with survivin and INCENP and its kinase activity is stimulated by survivin binding and phosphorylation |
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