Aurora-A and an Interacting Activator, the LIM Protein Ajuba, Are Required for Mitotic Commitment in Human Cells
Aurora family kinases contribute to regulation of mitosis. Using RNA interference in synchronized HeLa cells, we now show that Aurora-A is required for mitotic entry. We found that initial activation of Aurora-A in late G2 phase of the cell cycle is essential for recruitment of the cyclin B1-Cdk1 co...
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| Veröffentlicht in: | Cell 2003-09, Vol.114 (5), p.585-598 |
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| container_title | Cell |
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| creator | Hirota, Toru Kunitoku, Naoko Sasayama, Takashi Marumoto, Tomotoshi Zhang, Dongwei Nitta, Masayuki Hatakeyama, Katsuyoshi Saya, Hideyuki |
| description | Aurora family kinases contribute to regulation of mitosis. Using RNA interference in synchronized HeLa cells, we now show that Aurora-A is required for mitotic entry. We found that initial activation of Aurora-A in late G2 phase of the cell cycle is essential for recruitment of the cyclin B1-Cdk1 complex to centrosomes, where it becomes activated and commits cells to mitosis. A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein. Ajuba and Aurora-A interact in mitotic cells and become phosphorylated as they do so. In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A. Depletion of Ajuba prevented activation of Aurora-A at centrosomes in late G2 phase and inhibited mitotic entry. Overall, our data suggest that Ajuba is an essential activator of Aurora-A in mitotic commitment. |
| doi_str_mv | 10.1016/S0092-8674(03)00642-1 |
| format | Article |
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Using RNA interference in synchronized HeLa cells, we now show that Aurora-A is required for mitotic entry. We found that initial activation of Aurora-A in late G2 phase of the cell cycle is essential for recruitment of the cyclin B1-Cdk1 complex to centrosomes, where it becomes activated and commits cells to mitosis. A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein. Ajuba and Aurora-A interact in mitotic cells and become phosphorylated as they do so. In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A. Depletion of Ajuba prevented activation of Aurora-A at centrosomes in late G2 phase and inhibited mitotic entry. Overall, our data suggest that Ajuba is an essential activator of Aurora-A in mitotic commitment.</description><identifier>ISSN: 0092-8674</identifier><identifier>EISSN: 1097-4172</identifier><identifier>DOI: 10.1016/S0092-8674(03)00642-1</identifier><identifier>PMID: 13678582</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Aurora Kinase A ; Aurora Kinases ; CDC2 Protein Kinase - metabolism ; Cell Cycle ; Cell Cycle Proteins ; Cell Line ; Centrosome - ultrastructure ; COS Cells ; Cyclin B - metabolism ; Cyclin B1 ; G2 Phase ; Gene Deletion ; Glutathione Transferase - metabolism ; HeLa Cells ; Homeodomain Proteins - metabolism ; Homeodomain Proteins - physiology ; Humans ; LIM Domain Proteins ; Microscopy, Fluorescence ; Mitosis ; Models, Biological ; Molecular Sequence Data ; Phosphorylation ; Precipitin Tests ; Protein Binding ; Protein Kinases - metabolism ; Protein Kinases - physiology ; Protein-Serine-Threonine Kinases ; Recombinant Proteins - metabolism ; RNA Interference ; Temperature ; Time Factors ; Two-Hybrid System Techniques ; Xenopus Proteins</subject><ispartof>Cell, 2003-09, Vol.114 (5), p.585-598</ispartof><rights>2003 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-bd0526edfac91e251a61c4c3cd2813fb1bba5f1df8bc6b3e0326160ad6908aa13</citedby><cites>FETCH-LOGICAL-c505t-bd0526edfac91e251a61c4c3cd2813fb1bba5f1df8bc6b3e0326160ad6908aa13</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S0092-8674(03)00642-1$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/13678582$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hirota, Toru</creatorcontrib><creatorcontrib>Kunitoku, Naoko</creatorcontrib><creatorcontrib>Sasayama, Takashi</creatorcontrib><creatorcontrib>Marumoto, Tomotoshi</creatorcontrib><creatorcontrib>Zhang, Dongwei</creatorcontrib><creatorcontrib>Nitta, Masayuki</creatorcontrib><creatorcontrib>Hatakeyama, Katsuyoshi</creatorcontrib><creatorcontrib>Saya, Hideyuki</creatorcontrib><title>Aurora-A and an Interacting Activator, the LIM Protein Ajuba, Are Required for Mitotic Commitment in Human Cells</title><title>Cell</title><addtitle>Cell</addtitle><description>Aurora family kinases contribute to regulation of mitosis. Using RNA interference in synchronized HeLa cells, we now show that Aurora-A is required for mitotic entry. We found that initial activation of Aurora-A in late G2 phase of the cell cycle is essential for recruitment of the cyclin B1-Cdk1 complex to centrosomes, where it becomes activated and commits cells to mitosis. A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein. Ajuba and Aurora-A interact in mitotic cells and become phosphorylated as they do so. In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A. Depletion of Ajuba prevented activation of Aurora-A at centrosomes in late G2 phase and inhibited mitotic entry. Overall, our data suggest that Ajuba is an essential activator of Aurora-A in mitotic commitment.</description><subject>Animals</subject><subject>Aurora Kinase A</subject><subject>Aurora Kinases</subject><subject>CDC2 Protein Kinase - metabolism</subject><subject>Cell Cycle</subject><subject>Cell Cycle Proteins</subject><subject>Cell Line</subject><subject>Centrosome - ultrastructure</subject><subject>COS Cells</subject><subject>Cyclin B - metabolism</subject><subject>Cyclin B1</subject><subject>G2 Phase</subject><subject>Gene Deletion</subject><subject>Glutathione Transferase - metabolism</subject><subject>HeLa Cells</subject><subject>Homeodomain Proteins - metabolism</subject><subject>Homeodomain Proteins - physiology</subject><subject>Humans</subject><subject>LIM Domain Proteins</subject><subject>Microscopy, Fluorescence</subject><subject>Mitosis</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Phosphorylation</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Protein Kinases - metabolism</subject><subject>Protein Kinases - physiology</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>Recombinant Proteins - metabolism</subject><subject>RNA Interference</subject><subject>Temperature</subject><subject>Time Factors</subject><subject>Two-Hybrid System Techniques</subject><subject>Xenopus Proteins</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v1DAQxS0EotvCRwD5hEBqYGzHTnJC0YrSlbYC8edsOfYEXG3ire1U4tvj7a7g2JFGc_nNzNN7hLxi8J4BUx--A3S8alVTvwXxDkDVvGJPyIpB11Q1a_hTsvqHnJHzlG4BoJVSPidnTKimlS1fkX2_xBBN1VMzu9J0M2eMxmY__6J9Gfcmh3hJ82-k280N_RpDRj_T_nYZzCXtI9JveLf4iI6OIdIbn0P2lq7DNPk84Zxpoa-XqZxe426XXpBno9klfHmaF-Tn1acf6-tq--XzZt1vKytB5mpwILlCNxrbMeSSGcVsbYV1vGViHNgwGDkyN7aDVYNAEFwxBcapDlpjmLggb4539zHcLZiynnyyRYGZMSxJN0KV4vJRkIOQXS1FAeURtDGkFHHU--gnE_9oBvqQiX7IRB8M1yD0Qyb6oOT16cEyTOj-b51CKMDHI4DFj3uPUSfrcbboiq02axf8Iy_-Agz4mzc</recordid><startdate>20030905</startdate><enddate>20030905</enddate><creator>Hirota, Toru</creator><creator>Kunitoku, Naoko</creator><creator>Sasayama, Takashi</creator><creator>Marumoto, Tomotoshi</creator><creator>Zhang, Dongwei</creator><creator>Nitta, Masayuki</creator><creator>Hatakeyama, Katsuyoshi</creator><creator>Saya, Hideyuki</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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></search><sort><creationdate>20030905</creationdate><title>Aurora-A and an Interacting Activator, the LIM Protein Ajuba, Are Required for Mitotic Commitment in Human Cells</title><author>Hirota, Toru ; Kunitoku, Naoko ; Sasayama, Takashi ; Marumoto, Tomotoshi ; Zhang, Dongwei ; Nitta, Masayuki ; Hatakeyama, Katsuyoshi ; Saya, Hideyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-bd0526edfac91e251a61c4c3cd2813fb1bba5f1df8bc6b3e0326160ad6908aa13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Aurora Kinase A</topic><topic>Aurora Kinases</topic><topic>CDC2 Protein Kinase - metabolism</topic><topic>Cell Cycle</topic><topic>Cell Cycle Proteins</topic><topic>Cell Line</topic><topic>Centrosome - ultrastructure</topic><topic>COS Cells</topic><topic>Cyclin B - metabolism</topic><topic>Cyclin B1</topic><topic>G2 Phase</topic><topic>Gene Deletion</topic><topic>Glutathione Transferase - metabolism</topic><topic>HeLa Cells</topic><topic>Homeodomain Proteins - metabolism</topic><topic>Homeodomain Proteins - physiology</topic><topic>Humans</topic><topic>LIM Domain Proteins</topic><topic>Microscopy, Fluorescence</topic><topic>Mitosis</topic><topic>Models, Biological</topic><topic>Molecular Sequence Data</topic><topic>Phosphorylation</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Protein Kinases - metabolism</topic><topic>Protein Kinases - physiology</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>Recombinant Proteins - metabolism</topic><topic>RNA Interference</topic><topic>Temperature</topic><topic>Time Factors</topic><topic>Two-Hybrid System Techniques</topic><topic>Xenopus Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hirota, Toru</creatorcontrib><creatorcontrib>Kunitoku, Naoko</creatorcontrib><creatorcontrib>Sasayama, Takashi</creatorcontrib><creatorcontrib>Marumoto, Tomotoshi</creatorcontrib><creatorcontrib>Zhang, Dongwei</creatorcontrib><creatorcontrib>Nitta, Masayuki</creatorcontrib><creatorcontrib>Hatakeyama, Katsuyoshi</creatorcontrib><creatorcontrib>Saya, Hideyuki</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hirota, Toru</au><au>Kunitoku, Naoko</au><au>Sasayama, Takashi</au><au>Marumoto, Tomotoshi</au><au>Zhang, Dongwei</au><au>Nitta, Masayuki</au><au>Hatakeyama, Katsuyoshi</au><au>Saya, Hideyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Aurora-A and an Interacting Activator, the LIM Protein Ajuba, Are Required for Mitotic Commitment in Human Cells</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>2003-09-05</date><risdate>2003</risdate><volume>114</volume><issue>5</issue><spage>585</spage><epage>598</epage><pages>585-598</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>Aurora family kinases contribute to regulation of mitosis. Using RNA interference in synchronized HeLa cells, we now show that Aurora-A is required for mitotic entry. We found that initial activation of Aurora-A in late G2 phase of the cell cycle is essential for recruitment of the cyclin B1-Cdk1 complex to centrosomes, where it becomes activated and commits cells to mitosis. A two-hybrid screen identified the LIM protein Ajuba as an Aurora-A binding protein. Ajuba and Aurora-A interact in mitotic cells and become phosphorylated as they do so. In vitro analyses revealed that Ajuba induces the autophosphorylation and consequent activation of Aurora-A. Depletion of Ajuba prevented activation of Aurora-A at centrosomes in late G2 phase and inhibited mitotic entry. Overall, our data suggest that Ajuba is an essential activator of Aurora-A in mitotic commitment.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>13678582</pmid><doi>10.1016/S0092-8674(03)00642-1</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Aurora Kinase A Aurora Kinases CDC2 Protein Kinase - metabolism Cell Cycle Cell Cycle Proteins Cell Line Centrosome - ultrastructure COS Cells Cyclin B - metabolism Cyclin B1 G2 Phase Gene Deletion Glutathione Transferase - metabolism HeLa Cells Homeodomain Proteins - metabolism Homeodomain Proteins - physiology Humans LIM Domain Proteins Microscopy, Fluorescence Mitosis Models, Biological Molecular Sequence Data Phosphorylation Precipitin Tests Protein Binding Protein Kinases - metabolism Protein Kinases - physiology Protein-Serine-Threonine Kinases Recombinant Proteins - metabolism RNA Interference Temperature Time Factors Two-Hybrid System Techniques Xenopus Proteins |
| title | Aurora-A and an Interacting Activator, the LIM Protein Ajuba, Are Required for Mitotic Commitment in Human Cells |
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