Akt inhibits Myt1 in the signalling pathway that leads to meiotic G2/M-phase transition
In eukaryotes, entry into M-phase of the cell cycle is induced by activation of cyclin B–Cdc2 kinase. At G2-phase, the activity of its inactivator, a member of the Wee1 family of protein kinases, exceeds that of its activator, Cdc25C phosphatase. However, at M-phase entry the situation is reversed,...
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| Veröffentlicht in: | Nature cell biology 2002-02, Vol.4 (2), p.111-116 |
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| creator | Okumura, Eiichi Fukuhara, Takeshi Yoshida, Hitoshi Hanada, Shin-ichiro Kozutsumi, Rie Mori, Masashi Tachibana, Kazunori Kishimoto, Takeo |
| description | In eukaryotes, entry into M-phase of the cell cycle is induced by activation of cyclin B–Cdc2 kinase. At G2-phase, the activity of its inactivator, a member of the Wee1 family of protein kinases, exceeds that of its activator, Cdc25C phosphatase. However, at M-phase entry the situation is reversed, such that the activity of Cdc25C exceeds that of the Wee1 family. The mechanism of this reversal is unclear. Here we show that in oocytes from the starfish
Asterina pectinifera
, the kinase Akt (or protein kinase B (PKB)) phosphorylates and downregulates Myt1, a member of the Wee1 family. This switches the balance of regulator activities and causes the initial activation of cyclin B–Cdc2 at the meiotic G2/M-phase transition. These findings identify Myt1 as a new target of Akt, and demonstrate that Akt functions as an M-phase initiator. |
| doi_str_mv | 10.1038/ncb741 |
| format | Article |
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Asterina pectinifera
, the kinase Akt (or protein kinase B (PKB)) phosphorylates and downregulates Myt1, a member of the Wee1 family. This switches the balance of regulator activities and causes the initial activation of cyclin B–Cdc2 at the meiotic G2/M-phase transition. These findings identify Myt1 as a new target of Akt, and demonstrate that Akt functions as an M-phase initiator.</description><identifier>ISSN: 1465-7392</identifier><identifier>ISSN: 1476-4679</identifier><identifier>EISSN: 1476-4679</identifier><identifier>DOI: 10.1038/ncb741</identifier><identifier>PMID: 11802161</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Animals ; Asterina pectinifera ; Asteroidea ; Biomedical and Life Sciences ; Cancer Research ; CDC2 Protein Kinase - metabolism ; Cell Biology ; Cell cycle ; Cyclin B - metabolism ; Developmental Biology ; Enzyme Activation ; Eukaryotes ; Kinases ; Life Sciences ; Marine ; Meiosis - physiology ; Models, Biological ; Molecular Sequence Data ; Oocytes ; Oocytes - physiology ; Phase transitions ; Phosphatase ; Phosphorylation ; Physiological aspects ; Protein kinases ; Protein synthesis ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Protein-Tyrosine Kinases - genetics ; Protein-Tyrosine Kinases - metabolism ; Proteins ; Proto-Oncogene Proteins - genetics ; Proto-Oncogene Proteins - metabolism ; Proto-Oncogene Proteins c-akt ; Sequence Alignment ; Signal Transduction - physiology ; Starfish - physiology ; Stem Cells</subject><ispartof>Nature cell biology, 2002-02, Vol.4 (2), p.111-116</ispartof><rights>Springer Nature Limited 2002</rights><rights>COPYRIGHT 2002 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group Feb 2002</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4291-bd6a8edb5783f65360dec26be3cca5e21c0f336faf7db64be9d2c76160e925c43</citedby><cites>FETCH-LOGICAL-c4291-bd6a8edb5783f65360dec26be3cca5e21c0f336faf7db64be9d2c76160e925c43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/ncb741$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/ncb741$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11802161$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okumura, Eiichi</creatorcontrib><creatorcontrib>Fukuhara, Takeshi</creatorcontrib><creatorcontrib>Yoshida, Hitoshi</creatorcontrib><creatorcontrib>Hanada, Shin-ichiro</creatorcontrib><creatorcontrib>Kozutsumi, Rie</creatorcontrib><creatorcontrib>Mori, Masashi</creatorcontrib><creatorcontrib>Tachibana, Kazunori</creatorcontrib><creatorcontrib>Kishimoto, Takeo</creatorcontrib><title>Akt inhibits Myt1 in the signalling pathway that leads to meiotic G2/M-phase transition</title><title>Nature cell biology</title><addtitle>Nat Cell Biol</addtitle><addtitle>Nat Cell Biol</addtitle><description>In eukaryotes, entry into M-phase of the cell cycle is induced by activation of cyclin B–Cdc2 kinase. At G2-phase, the activity of its inactivator, a member of the Wee1 family of protein kinases, exceeds that of its activator, Cdc25C phosphatase. However, at M-phase entry the situation is reversed, such that the activity of Cdc25C exceeds that of the Wee1 family. The mechanism of this reversal is unclear. Here we show that in oocytes from the starfish
Asterina pectinifera
, the kinase Akt (or protein kinase B (PKB)) phosphorylates and downregulates Myt1, a member of the Wee1 family. This switches the balance of regulator activities and causes the initial activation of cyclin B–Cdc2 at the meiotic G2/M-phase transition. These findings identify Myt1 as a new target of Akt, and demonstrate that Akt functions as an M-phase initiator.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Asterina pectinifera</subject><subject>Asteroidea</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer Research</subject><subject>CDC2 Protein Kinase - metabolism</subject><subject>Cell Biology</subject><subject>Cell cycle</subject><subject>Cyclin B - metabolism</subject><subject>Developmental Biology</subject><subject>Enzyme Activation</subject><subject>Eukaryotes</subject><subject>Kinases</subject><subject>Life Sciences</subject><subject>Marine</subject><subject>Meiosis - physiology</subject><subject>Models, Biological</subject><subject>Molecular Sequence Data</subject><subject>Oocytes</subject><subject>Oocytes - physiology</subject><subject>Phase transitions</subject><subject>Phosphatase</subject><subject>Phosphorylation</subject><subject>Physiological aspects</subject><subject>Protein kinases</subject><subject>Protein synthesis</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Protein-Tyrosine Kinases - genetics</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins - genetics</subject><subject>Proto-Oncogene Proteins - metabolism</subject><subject>Proto-Oncogene Proteins c-akt</subject><subject>Sequence Alignment</subject><subject>Signal Transduction - physiology</subject><subject>Starfish - physiology</subject><subject>Stem Cells</subject><issn>1465-7392</issn><issn>1476-4679</issn><issn>1476-4679</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNqFkl1vFCEUhonR2Fr1JxjihcaLafkaYC43jdYmbUz8iJeEYc7MUmdgOzDR_fey2U027YXCBXB4zsnh5UXoNSXnlHB9EVyrBH2CTqlQshJSNU93e1lXijfsBL1I6Y4QKgRRz9EJpZowKukp-rn6lbEPa9_6nPDtNtNywnkNOPkh2HH0YcAbm9e_7baEbcYj2C7hHPEEPmbv8BW7uK02a5sA59mG5LOP4SV61tsxwavDeoZ-fPr4_fJzdfPl6vpydVM5wRpatZ20Grq2Vpr3suaSdOCYbIE7Z2tg1JGec9nbXnWtFC00HXNKUkmgYbUT_Ay939fdzPF-gZTN5JODcbQB4pKMlqKpGac78t0_SVXEqWum_wtSzTUXRBbw7SPwLi5zES0ZVoYWkrICne-hwY5gfOhjEcmV2cHkXQzQ-xJflaJMq_JvJeHDg4TCZPiTB7ukZK6_fX3IHlp1c0xpht5sZj_ZeWsoMTtfmL0vCvjm0OrSTtAdsYMRjjqmchUGmI9veVTqLzb-vSM</recordid><startdate>20020201</startdate><enddate>20020201</enddate><creator>Okumura, Eiichi</creator><creator>Fukuhara, Takeshi</creator><creator>Yoshida, Hitoshi</creator><creator>Hanada, Shin-ichiro</creator><creator>Kozutsumi, Rie</creator><creator>Mori, Masashi</creator><creator>Tachibana, Kazunori</creator><creator>Kishimoto, Takeo</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</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>ISR</scope><scope>3V.</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope><scope>7TN</scope><scope>F1W</scope><scope>H95</scope><scope>L.G</scope></search><sort><creationdate>20020201</creationdate><title>Akt inhibits Myt1 in the signalling pathway that leads to meiotic G2/M-phase transition</title><author>Okumura, Eiichi ; Fukuhara, Takeshi ; Yoshida, Hitoshi ; Hanada, Shin-ichiro ; Kozutsumi, Rie ; Mori, Masashi ; Tachibana, Kazunori ; Kishimoto, Takeo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4291-bd6a8edb5783f65360dec26be3cca5e21c0f336faf7db64be9d2c76160e925c43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Asterina pectinifera</topic><topic>Asteroidea</topic><topic>Biomedical and Life Sciences</topic><topic>Cancer Research</topic><topic>CDC2 Protein Kinase - 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physiology</topic><topic>Starfish - physiology</topic><topic>Stem Cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okumura, Eiichi</creatorcontrib><creatorcontrib>Fukuhara, Takeshi</creatorcontrib><creatorcontrib>Yoshida, Hitoshi</creatorcontrib><creatorcontrib>Hanada, Shin-ichiro</creatorcontrib><creatorcontrib>Kozutsumi, Rie</creatorcontrib><creatorcontrib>Mori, Masashi</creatorcontrib><creatorcontrib>Tachibana, Kazunori</creatorcontrib><creatorcontrib>Kishimoto, Takeo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - 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At G2-phase, the activity of its inactivator, a member of the Wee1 family of protein kinases, exceeds that of its activator, Cdc25C phosphatase. However, at M-phase entry the situation is reversed, such that the activity of Cdc25C exceeds that of the Wee1 family. The mechanism of this reversal is unclear. Here we show that in oocytes from the starfish
Asterina pectinifera
, the kinase Akt (or protein kinase B (PKB)) phosphorylates and downregulates Myt1, a member of the Wee1 family. This switches the balance of regulator activities and causes the initial activation of cyclin B–Cdc2 at the meiotic G2/M-phase transition. These findings identify Myt1 as a new target of Akt, and demonstrate that Akt functions as an M-phase initiator.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>11802161</pmid><doi>10.1038/ncb741</doi><tpages>6</tpages></addata></record> |
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| subjects | Amino Acid Sequence Animals Asterina pectinifera Asteroidea Biomedical and Life Sciences Cancer Research CDC2 Protein Kinase - metabolism Cell Biology Cell cycle Cyclin B - metabolism Developmental Biology Enzyme Activation Eukaryotes Kinases Life Sciences Marine Meiosis - physiology Models, Biological Molecular Sequence Data Oocytes Oocytes - physiology Phase transitions Phosphatase Phosphorylation Physiological aspects Protein kinases Protein synthesis Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Protein-Tyrosine Kinases - genetics Protein-Tyrosine Kinases - metabolism Proteins Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-akt Sequence Alignment Signal Transduction - physiology Starfish - physiology Stem Cells |
| title | Akt inhibits Myt1 in the signalling pathway that leads to meiotic G2/M-phase transition |
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