Greatwall Kinase Participates in the Cdc2 Autoregulatory Loop in Xenopus Egg Extracts
Mutations in the Drosophila gene encoding the serine-threonine protein kinase Greatwall have previously been shown to disrupt mitotic progression. To investigate Greatwall's mitotic function, we examined its behavior in Xenopus egg extracts. Greatwall is activated during mitosis by phosphorylat...
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| Veröffentlicht in: | Molecular cell 2006-04, Vol.22 (1), p.83-91 |
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| creator | Yu, Jiangtao Zhao, Yong Li, ZeXiao Galas, Simon Goldberg, Michael L. |
| description | Mutations in the
Drosophila gene encoding the serine-threonine protein kinase Greatwall have previously been shown to disrupt mitotic progression. To investigate Greatwall's mitotic function, we examined its behavior in
Xenopus egg extracts. Greatwall is activated during mitosis by phosphorylation; in vitro evidence indicates that maturation promoting factor (MPF) is an upstream kinase. Conversely, depletion of Greatwall from mitotic extracts rapidly lowers MPF activity due to the accumulation of inhibitory phosphorylations on Cdc2 kinase. Greatwall depletion similarly prevents cycling extracts from entering M phase. The effects of Greatwall depletion can be rescued by the addition of either wild-type (wt) Greatwall or a noninhibitable form of Cdc2 kinase. These results demonstrate that Greatwall participates in an autoregulatory loop that generates and maintains sufficiently high MPF activity levels to support mitosis. |
| doi_str_mv | 10.1016/j.molcel.2006.02.022 |
| format | Article |
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Drosophila gene encoding the serine-threonine protein kinase Greatwall have previously been shown to disrupt mitotic progression. To investigate Greatwall's mitotic function, we examined its behavior in
Xenopus egg extracts. Greatwall is activated during mitosis by phosphorylation; in vitro evidence indicates that maturation promoting factor (MPF) is an upstream kinase. Conversely, depletion of Greatwall from mitotic extracts rapidly lowers MPF activity due to the accumulation of inhibitory phosphorylations on Cdc2 kinase. Greatwall depletion similarly prevents cycling extracts from entering M phase. The effects of Greatwall depletion can be rescued by the addition of either wild-type (wt) Greatwall or a noninhibitable form of Cdc2 kinase. These results demonstrate that Greatwall participates in an autoregulatory loop that generates and maintains sufficiently high MPF activity levels to support mitosis.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/j.molcel.2006.02.022</identifier><identifier>PMID: 16600872</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; CDC2 Protein Kinase - genetics ; CDC2 Protein Kinase - metabolism ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - immunology ; Cell Cycle Proteins - metabolism ; Cell Division ; CELLCYLCE ; Drosophila ; Drosophila Proteins ; Gene Expression Regulation ; Maturation-Promoting Factor - metabolism ; Mitosis ; Ovum - metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases ; SIGNALING ; Xenopus ; Xenopus laevis</subject><ispartof>Molecular cell, 2006-04, Vol.22 (1), p.83-91</ispartof><rights>2006 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-fe3f78a95f5e45a7c735ac32df0dbb0cfd4d3de3ca402eb435a8717a52d551993</citedby><cites>FETCH-LOGICAL-c503t-fe3f78a95f5e45a7c735ac32df0dbb0cfd4d3de3ca402eb435a8717a52d551993</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1097276506001766$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16600872$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yu, Jiangtao</creatorcontrib><creatorcontrib>Zhao, Yong</creatorcontrib><creatorcontrib>Li, ZeXiao</creatorcontrib><creatorcontrib>Galas, Simon</creatorcontrib><creatorcontrib>Goldberg, Michael L.</creatorcontrib><title>Greatwall Kinase Participates in the Cdc2 Autoregulatory Loop in Xenopus Egg Extracts</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>Mutations in the
Drosophila gene encoding the serine-threonine protein kinase Greatwall have previously been shown to disrupt mitotic progression. To investigate Greatwall's mitotic function, we examined its behavior in
Xenopus egg extracts. Greatwall is activated during mitosis by phosphorylation; in vitro evidence indicates that maturation promoting factor (MPF) is an upstream kinase. Conversely, depletion of Greatwall from mitotic extracts rapidly lowers MPF activity due to the accumulation of inhibitory phosphorylations on Cdc2 kinase. Greatwall depletion similarly prevents cycling extracts from entering M phase. The effects of Greatwall depletion can be rescued by the addition of either wild-type (wt) Greatwall or a noninhibitable form of Cdc2 kinase. These results demonstrate that Greatwall participates in an autoregulatory loop that generates and maintains sufficiently high MPF activity levels to support mitosis.</description><subject>Animals</subject><subject>CDC2 Protein Kinase - genetics</subject><subject>CDC2 Protein Kinase - metabolism</subject><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - immunology</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Division</subject><subject>CELLCYLCE</subject><subject>Drosophila</subject><subject>Drosophila Proteins</subject><subject>Gene Expression Regulation</subject><subject>Maturation-Promoting Factor - metabolism</subject><subject>Mitosis</subject><subject>Ovum - metabolism</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases</subject><subject>SIGNALING</subject><subject>Xenopus</subject><subject>Xenopus laevis</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkMFqGzEQhkVoSNI0bxCKTr3ZHWml1e6lEIyblBiSQwK9CVmadWXWq62kTZq3j4wNvbUwMAPzzT_wEXLNYM6A1V-3813oLfZzDlDPgZfiJ-SCQatmgtXiw3Hmqpbn5GNKWwAmZNOekXNW1wCN4hfk-Taiya-m7-m9H0xC-mhi9taPJmOifqD5F9KFs5zeTDlE3Ey9Kf2NrkIY9_ufOIRxSnS52dDlnxyNzekTOe1Mn_Dq2C_J8_fl0-Jutnq4_bG4Wc2shCrPOqw61ZhWdhKFNMqqShpbcdeBW6_Bdk64ymFljQCOa1G2jWLKSO6kZG1bXZIvh9wxht8Tpqx3PhUnvRkwTEnXqhEcxP9BVmJZ3coCigNoY0gpYqfH6HcmvmkGeu9db_XBu95718BL8XL2-Zg_rXfo_h4dRRfg2wHAouPFY9TJehwsOh_RZu2C__eHd6C_lho</recordid><startdate>20060407</startdate><enddate>20060407</enddate><creator>Yu, Jiangtao</creator><creator>Zhao, Yong</creator><creator>Li, ZeXiao</creator><creator>Galas, Simon</creator><creator>Goldberg, Michael L.</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>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060407</creationdate><title>Greatwall Kinase Participates in the Cdc2 Autoregulatory Loop in Xenopus Egg Extracts</title><author>Yu, Jiangtao ; Zhao, Yong ; Li, ZeXiao ; Galas, Simon ; Goldberg, Michael L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-fe3f78a95f5e45a7c735ac32df0dbb0cfd4d3de3ca402eb435a8717a52d551993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>CDC2 Protein Kinase - genetics</topic><topic>CDC2 Protein Kinase - metabolism</topic><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Cycle Proteins - immunology</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cell Division</topic><topic>CELLCYLCE</topic><topic>Drosophila</topic><topic>Drosophila Proteins</topic><topic>Gene Expression Regulation</topic><topic>Maturation-Promoting Factor - metabolism</topic><topic>Mitosis</topic><topic>Ovum - metabolism</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases</topic><topic>SIGNALING</topic><topic>Xenopus</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yu, Jiangtao</creatorcontrib><creatorcontrib>Zhao, Yong</creatorcontrib><creatorcontrib>Li, ZeXiao</creatorcontrib><creatorcontrib>Galas, Simon</creatorcontrib><creatorcontrib>Goldberg, Michael L.</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>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yu, Jiangtao</au><au>Zhao, Yong</au><au>Li, ZeXiao</au><au>Galas, Simon</au><au>Goldberg, Michael L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Greatwall Kinase Participates in the Cdc2 Autoregulatory Loop in Xenopus Egg Extracts</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2006-04-07</date><risdate>2006</risdate><volume>22</volume><issue>1</issue><spage>83</spage><epage>91</epage><pages>83-91</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>Mutations in the
Drosophila gene encoding the serine-threonine protein kinase Greatwall have previously been shown to disrupt mitotic progression. To investigate Greatwall's mitotic function, we examined its behavior in
Xenopus egg extracts. Greatwall is activated during mitosis by phosphorylation; in vitro evidence indicates that maturation promoting factor (MPF) is an upstream kinase. Conversely, depletion of Greatwall from mitotic extracts rapidly lowers MPF activity due to the accumulation of inhibitory phosphorylations on Cdc2 kinase. Greatwall depletion similarly prevents cycling extracts from entering M phase. The effects of Greatwall depletion can be rescued by the addition of either wild-type (wt) Greatwall or a noninhibitable form of Cdc2 kinase. These results demonstrate that Greatwall participates in an autoregulatory loop that generates and maintains sufficiently high MPF activity levels to support mitosis.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16600872</pmid><doi>10.1016/j.molcel.2006.02.022</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Animals CDC2 Protein Kinase - genetics CDC2 Protein Kinase - metabolism Cell Cycle Proteins - genetics Cell Cycle Proteins - immunology Cell Cycle Proteins - metabolism Cell Division CELLCYLCE Drosophila Drosophila Proteins Gene Expression Regulation Maturation-Promoting Factor - metabolism Mitosis Ovum - metabolism Phosphorylation Protein-Serine-Threonine Kinases SIGNALING Xenopus Xenopus laevis |
| title | Greatwall Kinase Participates in the Cdc2 Autoregulatory Loop in Xenopus Egg Extracts |
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