Roles of aurora‐A kinase in mitotic entry and G2 checkpoint in mammalian cells
Background: Various mitotic events are controlled by Cdc2‐cyclin B and other mitotic kinases. Aurora/Ipl1‐related mitotic kinases were proved to play key roles in mitotic progression in diverse lower organisms. Aurora‐A is a mammalian counterpart of aurora/Ipl1‐related kinases and is thought to be a...
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Veröffentlicht in: | Genes to cells : devoted to molecular & cellular mechanisms 2002-11, Vol.7 (11), p.1173-1182 |
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creator | Marumoto, Tomotoshi Hirota, Toru Morisaki, Tetsuro Kunitoku, Naoko Zhang, Dongwei Ichikawa, Yasuko Sasayama, Takashi Kuninaka, Shinji Mimori, Tatsuyuki Tamaki, Norihiko Kimura, Masashi Okano, Yukio Saya, Hideyuki |
description | Background: Various mitotic events are controlled by Cdc2‐cyclin B and other mitotic kinases. Aurora/Ipl1‐related mitotic kinases were proved to play key roles in mitotic progression in diverse lower organisms. Aurora‐A is a mammalian counterpart of aurora/Ipl1‐related kinases and is thought to be a potential oncogene. However, the regulation of aurora‐A activation and the commitment of aurora‐A in the progression of G2‐M phase are largely unknown in mammalian cells.
Results: We demonstrated that aurora‐A is activated depending on the activation of Cdc2‐cyclin B in mammalian cells. Since Cdc2‐cyclin B does not directly phosphorylate aurora‐A, indirect pathways such as the inhibition of PP1 by Cdc2‐cyclin B may act for the activation of aurora‐A kinase. Microinjection of anti‐aurora‐A antibodies into HeLa cells at late G2 phase caused a significant delay in mitotic entry. Furthermore, aurora‐A activation at G2‐M transition was inhibited by DNA damage, and the over‐expression of aurora‐A induced the abrogation of the DNA damage‐induced G2 checkpoint.
Conclusions: Aurora‐A is activated downstream of Cdc2‐cyclin B and plays crucial roles in proper mitotic entry and G2 checkpoint control. Dysregulation of aurora‐A induces abnormal G2‐M transition in mammalian cells and may lead to chromosome instability, which results in the development and progression of malignant tumours. |
doi_str_mv | 10.1046/j.1365-2443.2002.00592.x |
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Results: We demonstrated that aurora‐A is activated depending on the activation of Cdc2‐cyclin B in mammalian cells. Since Cdc2‐cyclin B does not directly phosphorylate aurora‐A, indirect pathways such as the inhibition of PP1 by Cdc2‐cyclin B may act for the activation of aurora‐A kinase. Microinjection of anti‐aurora‐A antibodies into HeLa cells at late G2 phase caused a significant delay in mitotic entry. Furthermore, aurora‐A activation at G2‐M transition was inhibited by DNA damage, and the over‐expression of aurora‐A induced the abrogation of the DNA damage‐induced G2 checkpoint.
Conclusions: Aurora‐A is activated downstream of Cdc2‐cyclin B and plays crucial roles in proper mitotic entry and G2 checkpoint control. Dysregulation of aurora‐A induces abnormal G2‐M transition in mammalian cells and may lead to chromosome instability, which results in the development and progression of malignant tumours.</description><identifier>ISSN: 1356-9597</identifier><identifier>EISSN: 1365-2443</identifier><identifier>DOI: 10.1046/j.1365-2443.2002.00592.x</identifier><identifier>PMID: 12390251</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Science Ltd</publisher><subject>Animals ; Antibodies - immunology ; Aurora Kinase A ; Aurora Kinases ; Cell Cycle Proteins ; Cyclin B1 ; Cyclin-Dependent Kinases - physiology ; Enzyme Activation - physiology ; G2 Phase - physiology ; HeLa Cells ; Humans ; Mitosis - physiology ; Phosphorylation ; Protein Kinases - immunology ; Protein Kinases - physiology ; Protein-Serine-Threonine Kinases ; Rats ; Xenopus Proteins</subject><ispartof>Genes to cells : devoted to molecular & cellular mechanisms, 2002-11, Vol.7 (11), p.1173-1182</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4632-db020d8d2b778a84f4b2f80abf3b3170cdb0f54205a4956c60a7a41008a270243</citedby><cites>FETCH-LOGICAL-c4632-db020d8d2b778a84f4b2f80abf3b3170cdb0f54205a4956c60a7a41008a270243</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1046%2Fj.1365-2443.2002.00592.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1046%2Fj.1365-2443.2002.00592.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,1427,27901,27902,45550,45551,46384,46808</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12390251$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Marumoto, Tomotoshi</creatorcontrib><creatorcontrib>Hirota, Toru</creatorcontrib><creatorcontrib>Morisaki, Tetsuro</creatorcontrib><creatorcontrib>Kunitoku, Naoko</creatorcontrib><creatorcontrib>Zhang, Dongwei</creatorcontrib><creatorcontrib>Ichikawa, Yasuko</creatorcontrib><creatorcontrib>Sasayama, Takashi</creatorcontrib><creatorcontrib>Kuninaka, Shinji</creatorcontrib><creatorcontrib>Mimori, Tatsuyuki</creatorcontrib><creatorcontrib>Tamaki, Norihiko</creatorcontrib><creatorcontrib>Kimura, Masashi</creatorcontrib><creatorcontrib>Okano, Yukio</creatorcontrib><creatorcontrib>Saya, Hideyuki</creatorcontrib><title>Roles of aurora‐A kinase in mitotic entry and G2 checkpoint in mammalian cells</title><title>Genes to cells : devoted to molecular & cellular mechanisms</title><addtitle>Genes Cells</addtitle><description>Background: Various mitotic events are controlled by Cdc2‐cyclin B and other mitotic kinases. Aurora/Ipl1‐related mitotic kinases were proved to play key roles in mitotic progression in diverse lower organisms. Aurora‐A is a mammalian counterpart of aurora/Ipl1‐related kinases and is thought to be a potential oncogene. However, the regulation of aurora‐A activation and the commitment of aurora‐A in the progression of G2‐M phase are largely unknown in mammalian cells.
Results: We demonstrated that aurora‐A is activated depending on the activation of Cdc2‐cyclin B in mammalian cells. Since Cdc2‐cyclin B does not directly phosphorylate aurora‐A, indirect pathways such as the inhibition of PP1 by Cdc2‐cyclin B may act for the activation of aurora‐A kinase. Microinjection of anti‐aurora‐A antibodies into HeLa cells at late G2 phase caused a significant delay in mitotic entry. Furthermore, aurora‐A activation at G2‐M transition was inhibited by DNA damage, and the over‐expression of aurora‐A induced the abrogation of the DNA damage‐induced G2 checkpoint.
Conclusions: Aurora‐A is activated downstream of Cdc2‐cyclin B and plays crucial roles in proper mitotic entry and G2 checkpoint control. Dysregulation of aurora‐A induces abnormal G2‐M transition in mammalian cells and may lead to chromosome instability, which results in the development and progression of malignant tumours.</description><subject>Animals</subject><subject>Antibodies - immunology</subject><subject>Aurora Kinase A</subject><subject>Aurora Kinases</subject><subject>Cell Cycle Proteins</subject><subject>Cyclin B1</subject><subject>Cyclin-Dependent Kinases - physiology</subject><subject>Enzyme Activation - physiology</subject><subject>G2 Phase - physiology</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Mitosis - physiology</subject><subject>Phosphorylation</subject><subject>Protein Kinases - immunology</subject><subject>Protein Kinases - physiology</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>Rats</subject><subject>Xenopus Proteins</subject><issn>1356-9597</issn><issn>1365-2443</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkM1Kw0AQxxdRbK2-guzJW-Ls7G4-wEspWoWCIvW8bJINbpuPmk2xvfkIPqNPYtIWPeppBuY3M39-hFAGPgMRXC98xgPpoRDcRwD0AWSM_uaIDH8Gx30vAy-WcTggZ84tABhHkKdkwJDHgJINydNzXRhH65zqdVM3-uvjc0yXttLOUFvR0rZ1a1NqqrbZUl1ldIo0fTXpclXbqt0huix1YXVFU1MU7pyc5Lpw5uJQR-Tl7nY-ufdmj9OHyXjmpSLg6GUJIGRRhkkYRjoSuUgwj0AnOU84CyHtgFyKLq4WsQzSAHSoBQOINIaAgo_I1f7uqqnf1sa1qrSuT6ArU6-dClFyCCT-CbJISkQJHRjtwbSpnWtMrlaNLXWzVQxUr10tVG9X9XZVr13ttKtNt3p5-LFOSpP9Lh48d8DNHni3hdn--7Caziddw78BUyuPrQ</recordid><startdate>200211</startdate><enddate>200211</enddate><creator>Marumoto, Tomotoshi</creator><creator>Hirota, Toru</creator><creator>Morisaki, Tetsuro</creator><creator>Kunitoku, Naoko</creator><creator>Zhang, Dongwei</creator><creator>Ichikawa, Yasuko</creator><creator>Sasayama, Takashi</creator><creator>Kuninaka, Shinji</creator><creator>Mimori, Tatsuyuki</creator><creator>Tamaki, Norihiko</creator><creator>Kimura, Masashi</creator><creator>Okano, Yukio</creator><creator>Saya, Hideyuki</creator><general>Blackwell Science Ltd</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></search><sort><creationdate>200211</creationdate><title>Roles of aurora‐A kinase in mitotic entry and G2 checkpoint in mammalian cells</title><author>Marumoto, Tomotoshi ; Hirota, Toru ; Morisaki, Tetsuro ; Kunitoku, Naoko ; Zhang, Dongwei ; Ichikawa, Yasuko ; Sasayama, Takashi ; Kuninaka, Shinji ; Mimori, Tatsuyuki ; Tamaki, Norihiko ; Kimura, Masashi ; Okano, Yukio ; Saya, Hideyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4632-db020d8d2b778a84f4b2f80abf3b3170cdb0f54205a4956c60a7a41008a270243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Antibodies - immunology</topic><topic>Aurora Kinase A</topic><topic>Aurora Kinases</topic><topic>Cell Cycle Proteins</topic><topic>Cyclin B1</topic><topic>Cyclin-Dependent Kinases - physiology</topic><topic>Enzyme Activation - physiology</topic><topic>G2 Phase - physiology</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Mitosis - physiology</topic><topic>Phosphorylation</topic><topic>Protein Kinases - immunology</topic><topic>Protein Kinases - physiology</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>Rats</topic><topic>Xenopus Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Marumoto, Tomotoshi</creatorcontrib><creatorcontrib>Hirota, Toru</creatorcontrib><creatorcontrib>Morisaki, Tetsuro</creatorcontrib><creatorcontrib>Kunitoku, Naoko</creatorcontrib><creatorcontrib>Zhang, Dongwei</creatorcontrib><creatorcontrib>Ichikawa, Yasuko</creatorcontrib><creatorcontrib>Sasayama, Takashi</creatorcontrib><creatorcontrib>Kuninaka, Shinji</creatorcontrib><creatorcontrib>Mimori, Tatsuyuki</creatorcontrib><creatorcontrib>Tamaki, Norihiko</creatorcontrib><creatorcontrib>Kimura, Masashi</creatorcontrib><creatorcontrib>Okano, Yukio</creatorcontrib><creatorcontrib>Saya, Hideyuki</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><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Marumoto, Tomotoshi</au><au>Hirota, Toru</au><au>Morisaki, Tetsuro</au><au>Kunitoku, Naoko</au><au>Zhang, Dongwei</au><au>Ichikawa, Yasuko</au><au>Sasayama, Takashi</au><au>Kuninaka, Shinji</au><au>Mimori, Tatsuyuki</au><au>Tamaki, Norihiko</au><au>Kimura, Masashi</au><au>Okano, Yukio</au><au>Saya, Hideyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Roles of aurora‐A kinase in mitotic entry and G2 checkpoint in mammalian cells</atitle><jtitle>Genes to cells : devoted to molecular & cellular mechanisms</jtitle><addtitle>Genes Cells</addtitle><date>2002-11</date><risdate>2002</risdate><volume>7</volume><issue>11</issue><spage>1173</spage><epage>1182</epage><pages>1173-1182</pages><issn>1356-9597</issn><eissn>1365-2443</eissn><abstract>Background: Various mitotic events are controlled by Cdc2‐cyclin B and other mitotic kinases. Aurora/Ipl1‐related mitotic kinases were proved to play key roles in mitotic progression in diverse lower organisms. Aurora‐A is a mammalian counterpart of aurora/Ipl1‐related kinases and is thought to be a potential oncogene. However, the regulation of aurora‐A activation and the commitment of aurora‐A in the progression of G2‐M phase are largely unknown in mammalian cells.
Results: We demonstrated that aurora‐A is activated depending on the activation of Cdc2‐cyclin B in mammalian cells. Since Cdc2‐cyclin B does not directly phosphorylate aurora‐A, indirect pathways such as the inhibition of PP1 by Cdc2‐cyclin B may act for the activation of aurora‐A kinase. Microinjection of anti‐aurora‐A antibodies into HeLa cells at late G2 phase caused a significant delay in mitotic entry. Furthermore, aurora‐A activation at G2‐M transition was inhibited by DNA damage, and the over‐expression of aurora‐A induced the abrogation of the DNA damage‐induced G2 checkpoint.
Conclusions: Aurora‐A is activated downstream of Cdc2‐cyclin B and plays crucial roles in proper mitotic entry and G2 checkpoint control. Dysregulation of aurora‐A induces abnormal G2‐M transition in mammalian cells and may lead to chromosome instability, which results in the development and progression of malignant tumours.</abstract><cop>Oxford, UK</cop><pub>Blackwell Science Ltd</pub><pmid>12390251</pmid><doi>10.1046/j.1365-2443.2002.00592.x</doi><tpages>10</tpages></addata></record> |
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source | Freely Accessible Japanese Titles - check A-Z of ejournals; Wiley-Blackwell Journals; MEDLINE; Wiley Free Archive; EZB Electronic Journals Library |
subjects | Animals Antibodies - immunology Aurora Kinase A Aurora Kinases Cell Cycle Proteins Cyclin B1 Cyclin-Dependent Kinases - physiology Enzyme Activation - physiology G2 Phase - physiology HeLa Cells Humans Mitosis - physiology Phosphorylation Protein Kinases - immunology Protein Kinases - physiology Protein-Serine-Threonine Kinases Rats Xenopus Proteins |
title | Roles of aurora‐A kinase in mitotic entry and G2 checkpoint in mammalian cells |
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