Analysis of the early embryonic cell cycles of Xenopus; regulation of cell cycle length by Xe-wee1 and Mos
In Xenopus, cdc2 tyrosine phosphorylation is detected in the first 60â75 minute cell cycle but not in the next eleven cell cycles (cycles 2â12) which are only 30 minutes long. Here we report that the wee1/cdc25 ratio increases before the first mitotic interphase. We show that the Xe-wee1 protein...
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Veröffentlicht in: | Development (Cambridge) 1998-01, Vol.125 (2), p.237-248 |
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description | In Xenopus, cdc2 tyrosine phosphorylation is detected in the first 60â75 minute cell cycle but not in the next eleven cell cycles (cycles 2â12) which are only 30 minutes long. Here we report that the wee1/cdc25 ratio increases before the first mitotic interphase. We show that the Xe-wee1 protein is absent in stage VI oocytes and is expressed from meiosis II until gastrulation. A dominant negative form of Xe-wee1 (KM wee1) reduced the level cdc2 tyrosine phosphorylation and length of the first cycle. However, the ratio of wee1/cdc25 did not decrease after the first cycle and therefore did not explain the lack of cdc2 tyrosine phosphorylation in, nor the rapidity of, cycles 2â12. Furthermore, there was no evidence for a wee1/myt1 inhibitor in cycles 2â12. We examined the role of Mos in the first cycle because it is present during the first 20 minutes of this cycle. We arrested the rapid embryonic cell cycle (cycle 2 or 3) with Mos and restarted the cell cycle with calcium ionophore; the 30 minute cycle was converted into a 60 minute cycle, with cdc2 tyrosine phosphorylation. In addition, the injection of a non-degradable Mos (MBP-Mos) into the first cycle resulted in a dramatic elongation of this cycle (to 140 minutes). MBP-Mos did not delay DNA replication or the translation of cyclins A or B; it did, however, result in the marked accumulation of tyrosine phosphorylated cdc2. Thus, while the wee1/cdc25 ratio changes during development, these changes may not be responsible for the variety of cell cycles observed during early Xenopus embryogenesis. Our experiments indicate that Mos/MAPK can also contribute to cell cycle length. |
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Here we report that the wee1/cdc25 ratio increases before the first mitotic interphase. We show that the Xe-wee1 protein is absent in stage VI oocytes and is expressed from meiosis II until gastrulation. A dominant negative form of Xe-wee1 (KM wee1) reduced the level cdc2 tyrosine phosphorylation and length of the first cycle. However, the ratio of wee1/cdc25 did not decrease after the first cycle and therefore did not explain the lack of cdc2 tyrosine phosphorylation in, nor the rapidity of, cycles 2â12. Furthermore, there was no evidence for a wee1/myt1 inhibitor in cycles 2â12. We examined the role of Mos in the first cycle because it is present during the first 20 minutes of this cycle. We arrested the rapid embryonic cell cycle (cycle 2 or 3) with Mos and restarted the cell cycle with calcium ionophore; the 30 minute cycle was converted into a 60 minute cycle, with cdc2 tyrosine phosphorylation. In addition, the injection of a non-degradable Mos (MBP-Mos) into the first cycle resulted in a dramatic elongation of this cycle (to 140 minutes). MBP-Mos did not delay DNA replication or the translation of cyclins A or B; it did, however, result in the marked accumulation of tyrosine phosphorylated cdc2. Thus, while the wee1/cdc25 ratio changes during development, these changes may not be responsible for the variety of cell cycles observed during early Xenopus embryogenesis. Our experiments indicate that Mos/MAPK can also contribute to cell cycle length.</description><identifier>ISSN: 0950-1991</identifier><identifier>EISSN: 1477-9129</identifier><identifier>DOI: 10.1242/dev.125.2.237</identifier><identifier>PMID: 9486797</identifier><language>eng</language><publisher>England: The Company of Biologists Limited</publisher><subject>Amino Acid Sequence ; Animals ; CDC2 Protein Kinase - metabolism ; cdc25 Phosphatases ; Cell Cycle - physiology ; Cell Cycle Proteins - metabolism ; Cyclin-Dependent Kinase Inhibitor p21 ; Cyclins - pharmacology ; Enzyme Inhibitors - pharmacology ; Freshwater ; Gastrula - metabolism ; Mitosis ; Molecular Sequence Data ; Nuclear Proteins ; Oocytes - metabolism ; Organ Specificity ; Phosphoprotein Phosphatases - metabolism ; Phosphorylation ; Protein-Tyrosine Kinases - biosynthesis ; Protein-Tyrosine Kinases - metabolism ; Proto-Oncogene Proteins c-mos - metabolism ; Recombinant Fusion Proteins ; RNA, Antisense - pharmacology ; RNA, Messenger - analysis ; Tyrosine - metabolism ; Xenopus ; Xenopus - embryology ; Xenopus Proteins</subject><ispartof>Development (Cambridge), 1998-01, Vol.125 (2), p.237-248</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-1513494d804354d4336bae7672d6576ffa986ca89a9d0a019702f992e1836e193</citedby><cites>FETCH-LOGICAL-c422t-1513494d804354d4336bae7672d6576ffa986ca89a9d0a019702f992e1836e193</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,3678,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9486797$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murakami, M S</creatorcontrib><creatorcontrib>Vande Woude, G F</creatorcontrib><title>Analysis of the early embryonic cell cycles of Xenopus; regulation of cell cycle length by Xe-wee1 and Mos</title><title>Development (Cambridge)</title><addtitle>Development</addtitle><description>In Xenopus, cdc2 tyrosine phosphorylation is detected in the first 60â75 minute cell cycle but not in the next eleven cell cycles (cycles 2â12) which are only 30 minutes long. Here we report that the wee1/cdc25 ratio increases before the first mitotic interphase. We show that the Xe-wee1 protein is absent in stage VI oocytes and is expressed from meiosis II until gastrulation. A dominant negative form of Xe-wee1 (KM wee1) reduced the level cdc2 tyrosine phosphorylation and length of the first cycle. However, the ratio of wee1/cdc25 did not decrease after the first cycle and therefore did not explain the lack of cdc2 tyrosine phosphorylation in, nor the rapidity of, cycles 2â12. Furthermore, there was no evidence for a wee1/myt1 inhibitor in cycles 2â12. We examined the role of Mos in the first cycle because it is present during the first 20 minutes of this cycle. We arrested the rapid embryonic cell cycle (cycle 2 or 3) with Mos and restarted the cell cycle with calcium ionophore; the 30 minute cycle was converted into a 60 minute cycle, with cdc2 tyrosine phosphorylation. In addition, the injection of a non-degradable Mos (MBP-Mos) into the first cycle resulted in a dramatic elongation of this cycle (to 140 minutes). MBP-Mos did not delay DNA replication or the translation of cyclins A or B; it did, however, result in the marked accumulation of tyrosine phosphorylated cdc2. Thus, while the wee1/cdc25 ratio changes during development, these changes may not be responsible for the variety of cell cycles observed during early Xenopus embryogenesis. Our experiments indicate that Mos/MAPK can also contribute to cell cycle length.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>CDC2 Protein Kinase - metabolism</subject><subject>cdc25 Phosphatases</subject><subject>Cell Cycle - physiology</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cyclin-Dependent Kinase Inhibitor p21</subject><subject>Cyclins - pharmacology</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Freshwater</subject><subject>Gastrula - metabolism</subject><subject>Mitosis</subject><subject>Molecular Sequence Data</subject><subject>Nuclear Proteins</subject><subject>Oocytes - metabolism</subject><subject>Organ Specificity</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylation</subject><subject>Protein-Tyrosine Kinases - biosynthesis</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins c-mos - metabolism</subject><subject>Recombinant Fusion Proteins</subject><subject>RNA, Antisense - pharmacology</subject><subject>RNA, Messenger - analysis</subject><subject>Tyrosine - metabolism</subject><subject>Xenopus</subject><subject>Xenopus - embryology</subject><subject>Xenopus Proteins</subject><issn>0950-1991</issn><issn>1477-9129</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1P3DAQxa0KRBfaY49IPnFqFn87Vk8rVGglEBcq9WY5yWTXK2-8tRNQ_nsSdkV762meZn56mpmH0BdKlpQJdt3A8yTkki0Z1x_QggqtC0OZOUELYiQpqDH0IzrPeUsI4UrrM3RmRKm00Qu0XXUujNlnHFvcbwCDS2HEsKvSGDtf4xpCwPVYB3hDfkMX90P-hhOsh-B6H7u5_ZfCAbp1v8HVOLHFCwDFrmvwQ8yf0GnrQobPx3qBft1-f7r5Udw_3v28Wd0XtWCsL6ikXBjRlERwKRrBuaocaKVZo6RWbetMqWpXGmca4gg1mrDWGAa05Aqo4Rfo6uC7T_HPALm3O5_nBV0Hcch2upsIKeV_Qaq4IJrPYHEA6xRzTtDaffI7l0ZLiZ1DsFMIk5CW2SmEib88Gg_VDpp3-vj1af71MN_49ebFJ7CVjyGufe7zbAUh7v-xewU_NZEf</recordid><startdate>19980101</startdate><enddate>19980101</enddate><creator>Murakami, M S</creator><creator>Vande Woude, G F</creator><general>The Company of Biologists Limited</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>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19980101</creationdate><title>Analysis of the early embryonic cell cycles of Xenopus; regulation of cell cycle length by Xe-wee1 and Mos</title><author>Murakami, M S ; Vande Woude, G F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-1513494d804354d4336bae7672d6576ffa986ca89a9d0a019702f992e1836e193</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>CDC2 Protein Kinase - metabolism</topic><topic>cdc25 Phosphatases</topic><topic>Cell Cycle - physiology</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cyclin-Dependent Kinase Inhibitor p21</topic><topic>Cyclins - pharmacology</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Freshwater</topic><topic>Gastrula - metabolism</topic><topic>Mitosis</topic><topic>Molecular Sequence Data</topic><topic>Nuclear Proteins</topic><topic>Oocytes - metabolism</topic><topic>Organ Specificity</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>Protein-Tyrosine Kinases - biosynthesis</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proto-Oncogene Proteins c-mos - metabolism</topic><topic>Recombinant Fusion Proteins</topic><topic>RNA, Antisense - pharmacology</topic><topic>RNA, Messenger - analysis</topic><topic>Tyrosine - metabolism</topic><topic>Xenopus</topic><topic>Xenopus - embryology</topic><topic>Xenopus Proteins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murakami, M S</creatorcontrib><creatorcontrib>Vande Woude, G F</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>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>Development (Cambridge)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Murakami, M S</au><au>Vande Woude, G F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of the early embryonic cell cycles of Xenopus; regulation of cell cycle length by Xe-wee1 and Mos</atitle><jtitle>Development (Cambridge)</jtitle><addtitle>Development</addtitle><date>1998-01-01</date><risdate>1998</risdate><volume>125</volume><issue>2</issue><spage>237</spage><epage>248</epage><pages>237-248</pages><issn>0950-1991</issn><eissn>1477-9129</eissn><abstract>In Xenopus, cdc2 tyrosine phosphorylation is detected in the first 60â75 minute cell cycle but not in the next eleven cell cycles (cycles 2â12) which are only 30 minutes long. Here we report that the wee1/cdc25 ratio increases before the first mitotic interphase. We show that the Xe-wee1 protein is absent in stage VI oocytes and is expressed from meiosis II until gastrulation. A dominant negative form of Xe-wee1 (KM wee1) reduced the level cdc2 tyrosine phosphorylation and length of the first cycle. However, the ratio of wee1/cdc25 did not decrease after the first cycle and therefore did not explain the lack of cdc2 tyrosine phosphorylation in, nor the rapidity of, cycles 2â12. Furthermore, there was no evidence for a wee1/myt1 inhibitor in cycles 2â12. We examined the role of Mos in the first cycle because it is present during the first 20 minutes of this cycle. We arrested the rapid embryonic cell cycle (cycle 2 or 3) with Mos and restarted the cell cycle with calcium ionophore; the 30 minute cycle was converted into a 60 minute cycle, with cdc2 tyrosine phosphorylation. In addition, the injection of a non-degradable Mos (MBP-Mos) into the first cycle resulted in a dramatic elongation of this cycle (to 140 minutes). MBP-Mos did not delay DNA replication or the translation of cyclins A or B; it did, however, result in the marked accumulation of tyrosine phosphorylated cdc2. Thus, while the wee1/cdc25 ratio changes during development, these changes may not be responsible for the variety of cell cycles observed during early Xenopus embryogenesis. Our experiments indicate that Mos/MAPK can also contribute to cell cycle length.</abstract><cop>England</cop><pub>The Company of Biologists Limited</pub><pmid>9486797</pmid><doi>10.1242/dev.125.2.237</doi><tpages>12</tpages></addata></record> |
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subjects | Amino Acid Sequence Animals CDC2 Protein Kinase - metabolism cdc25 Phosphatases Cell Cycle - physiology Cell Cycle Proteins - metabolism Cyclin-Dependent Kinase Inhibitor p21 Cyclins - pharmacology Enzyme Inhibitors - pharmacology Freshwater Gastrula - metabolism Mitosis Molecular Sequence Data Nuclear Proteins Oocytes - metabolism Organ Specificity Phosphoprotein Phosphatases - metabolism Phosphorylation Protein-Tyrosine Kinases - biosynthesis Protein-Tyrosine Kinases - metabolism Proto-Oncogene Proteins c-mos - metabolism Recombinant Fusion Proteins RNA, Antisense - pharmacology RNA, Messenger - analysis Tyrosine - metabolism Xenopus Xenopus - embryology Xenopus Proteins |
title | Analysis of the early embryonic cell cycles of Xenopus; regulation of cell cycle length by Xe-wee1 and Mos |
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