Protein kinase B/Akt phosphorylation of PDE3A and its role in mammalian oocyte maturation
cGMP‐inhibited cAMP phosphodiesterase 3A (PDE3A) is expressed in mouse oocytes, and its function is indispensable for meiotic maturation as demonstrated by genetic ablation. Moreover, PDE3 activity is required for insulin/insulin‐like growth factor‐1 stimulation of Xenopus oocyte meiotic resumption....
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| Veröffentlicht in: | The EMBO journal 2006-12, Vol.25 (24), p.5716-5725 |
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| creator | Han, Seung Jin Vaccari, Sergio Nedachi, Taku Andersen, Carsten B Kovacina, Kristina S Roth, Richard A Conti, Marco |
| description | cGMP‐inhibited cAMP phosphodiesterase 3A (PDE3A) is expressed in mouse oocytes, and its function is indispensable for meiotic maturation as demonstrated by genetic ablation. Moreover, PDE3 activity is required for insulin/insulin‐like growth factor‐1 stimulation of
Xenopus
oocyte meiotic resumption. Here, we investigated the cAMP‐dependent protein kinase B (PKB)/Akt regulation of PDE3A and its impact on oocyte maturation. Cell‐free incubation of recombinant mouse PDE3A with PKB/Akt or cAMP‐dependent protein kinase A catalytic subunits leads to phosphorylation of the PDE3A protein. Coexpression of PDE3A with constitutively activated PKB/Akt (Myr‐Akt) increases PDE activity as well as its phosphorylation state. Injection of
pde3a
mRNA potentiates insulin‐dependent maturation of
Xenopus
oocytes and rescues the phenotype of
pde3
−/−
mouse oocytes. This effect is greatly decreased by mutation of any of the PDE3A serines 290–292 to alanine in both
Xenopus
and mouse. Microinjection of myr‐Akt in mouse oocytes causes
in vitro
meiotic maturation and this effect requires PDE3A. Collectively, these data indicate that activation of PDE3A by PKB/Akt‐mediated phosphorylation plays a role in the control of PDE3A activity in mammalian oocytes. |
| doi_str_mv | 10.1038/sj.emboj.7601431 |
| format | Article |
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Xenopus
oocyte meiotic resumption. Here, we investigated the cAMP‐dependent protein kinase B (PKB)/Akt regulation of PDE3A and its impact on oocyte maturation. Cell‐free incubation of recombinant mouse PDE3A with PKB/Akt or cAMP‐dependent protein kinase A catalytic subunits leads to phosphorylation of the PDE3A protein. Coexpression of PDE3A with constitutively activated PKB/Akt (Myr‐Akt) increases PDE activity as well as its phosphorylation state. Injection of
pde3a
mRNA potentiates insulin‐dependent maturation of
Xenopus
oocytes and rescues the phenotype of
pde3
−/−
mouse oocytes. This effect is greatly decreased by mutation of any of the PDE3A serines 290–292 to alanine in both
Xenopus
and mouse. Microinjection of myr‐Akt in mouse oocytes causes
in vitro
meiotic maturation and this effect requires PDE3A. Collectively, these data indicate that activation of PDE3A by PKB/Akt‐mediated phosphorylation plays a role in the control of PDE3A activity in mammalian oocytes.</description><identifier>ISSN: 0261-4189</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1038/sj.emboj.7601431</identifier><identifier>PMID: 17124499</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>3',5'-Cyclic-AMP Phosphodiesterases - chemistry ; 3',5'-Cyclic-AMP Phosphodiesterases - deficiency ; 3',5'-Cyclic-AMP Phosphodiesterases - metabolism ; Amino Acid Sequence ; Animals ; Cyclic AMP-Dependent Protein Kinases - metabolism ; Cyclic Nucleotide Phosphodiesterases, Type 3 ; EMBO06 ; EMBO37 ; Enzyme Activation - drug effects ; Female ; Gene expression ; Genetic recombination ; Humans ; Incubation ; Injection ; Insulin - pharmacology ; Isoenzymes - metabolism ; Mammals ; Maturation-Promoting Factor - metabolism ; Mice ; Molecular biology ; Molecular Sequence Data ; Mutation ; oocyte maturation ; Oocytes - cytology ; Oocytes - drug effects ; Oogenesis - drug effects ; Oogenesis - physiology ; PDE3A ; Phenotype ; phosphorylation ; Phosphorylation - drug effects ; Phosphoserine - metabolism ; PKB/Akt ; Proteins ; Proto-Oncogene Proteins c-akt - metabolism ; Rodents ; Xenopus</subject><ispartof>The EMBO journal, 2006-12, Vol.25 (24), p.5716-5725</ispartof><rights>European Molecular Biology Organization 2006</rights><rights>Copyright © 2006 European Molecular Biology Organization</rights><rights>Copyright Nature Publishing Group Dec 13, 2006</rights><rights>Copyright © 2006, European Molecular Biology Organization 2006 European Molecular Biology Organization</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6701-4e42ffb332a74c3b9b39e9a0a5dcd74f460672e409bbddad241b1c5bb122c31d3</citedby><cites>FETCH-LOGICAL-c6701-4e42ffb332a74c3b9b39e9a0a5dcd74f460672e409bbddad241b1c5bb122c31d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1698880/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1698880/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,41120,42189,45574,45575,46409,46833,51576,53791,53793</link.rule.ids><linktorsrc>$$Uhttps://doi.org/10.1038/sj.emboj.7601431$$EView_record_in_Springer_Nature$$FView_record_in_$$GSpringer_Nature</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17124499$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Han, Seung Jin</creatorcontrib><creatorcontrib>Vaccari, Sergio</creatorcontrib><creatorcontrib>Nedachi, Taku</creatorcontrib><creatorcontrib>Andersen, Carsten B</creatorcontrib><creatorcontrib>Kovacina, Kristina S</creatorcontrib><creatorcontrib>Roth, Richard A</creatorcontrib><creatorcontrib>Conti, Marco</creatorcontrib><title>Protein kinase B/Akt phosphorylation of PDE3A and its role in mammalian oocyte maturation</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>cGMP‐inhibited cAMP phosphodiesterase 3A (PDE3A) is expressed in mouse oocytes, and its function is indispensable for meiotic maturation as demonstrated by genetic ablation. Moreover, PDE3 activity is required for insulin/insulin‐like growth factor‐1 stimulation of
Xenopus
oocyte meiotic resumption. Here, we investigated the cAMP‐dependent protein kinase B (PKB)/Akt regulation of PDE3A and its impact on oocyte maturation. Cell‐free incubation of recombinant mouse PDE3A with PKB/Akt or cAMP‐dependent protein kinase A catalytic subunits leads to phosphorylation of the PDE3A protein. Coexpression of PDE3A with constitutively activated PKB/Akt (Myr‐Akt) increases PDE activity as well as its phosphorylation state. Injection of
pde3a
mRNA potentiates insulin‐dependent maturation of
Xenopus
oocytes and rescues the phenotype of
pde3
−/−
mouse oocytes. This effect is greatly decreased by mutation of any of the PDE3A serines 290–292 to alanine in both
Xenopus
and mouse. Microinjection of myr‐Akt in mouse oocytes causes
in vitro
meiotic maturation and this effect requires PDE3A. Collectively, these data indicate that activation of PDE3A by PKB/Akt‐mediated phosphorylation plays a role in the control of PDE3A activity in mammalian oocytes.</description><subject>3',5'-Cyclic-AMP Phosphodiesterases - chemistry</subject><subject>3',5'-Cyclic-AMP Phosphodiesterases - deficiency</subject><subject>3',5'-Cyclic-AMP Phosphodiesterases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Cyclic Nucleotide Phosphodiesterases, Type 3</subject><subject>EMBO06</subject><subject>EMBO37</subject><subject>Enzyme Activation - drug effects</subject><subject>Female</subject><subject>Gene expression</subject><subject>Genetic recombination</subject><subject>Humans</subject><subject>Incubation</subject><subject>Injection</subject><subject>Insulin - pharmacology</subject><subject>Isoenzymes - metabolism</subject><subject>Mammals</subject><subject>Maturation-Promoting Factor - metabolism</subject><subject>Mice</subject><subject>Molecular biology</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>oocyte maturation</subject><subject>Oocytes - cytology</subject><subject>Oocytes - drug effects</subject><subject>Oogenesis - drug effects</subject><subject>Oogenesis - physiology</subject><subject>PDE3A</subject><subject>Phenotype</subject><subject>phosphorylation</subject><subject>Phosphorylation - drug effects</subject><subject>Phosphoserine - metabolism</subject><subject>PKB/Akt</subject><subject>Proteins</subject><subject>Proto-Oncogene Proteins c-akt - metabolism</subject><subject>Rodents</subject><subject>Xenopus</subject><issn>0261-4189</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqFkUtv1DAUhS0EokNhzwYUsWCXqV-J4w3StEzLoy0VAgHdWHbitM4k9tROgPn3eJrRTEFCXViWfL9zfO89ADxHcIogKQ5CM9Wdcs2U5RBRgh6ACaI5TDFk2UMwgThHKUUF3wNPQmgghFnB0GOwhxjClHI-AT8uvOu1scnCWBl0cngwW_TJ8tqFePyqlb1xNnF1cvF2TmaJtFVi-pB41-okqjrZdbI1MiKuXPU6PvSDvxU9BY9q2Qb9bHPvg6_H8y9H79LTTyfvj2anaZkzGNvTFNe1IgRLRkuiuCJccwllVpUVo3UcJ2dYU8iVqipZYYoUKjOlEMYlQRXZB29G3-WgOl2V2vZetmLpTSf9SjhpxN8Va67FlfspUM6LooDR4PXGwLubQYdedCaUum2l1W4IIi9wXC3O7gURp5zCgkbw1T9g4wZv4xYik2EGi2wNwREqvQvB63rbMoJina4IjbhNV2zSjZKXd0fdCTZxRoCPwC_T6tW9hmJ-dvhhZ45GbYgye6X9nab_39CLUWPXsevth7t6OtZN6PXvbVn6hcgZYZn4dn4iLi8_npHv8Fx8Jn8A7hneTg</recordid><startdate>20061213</startdate><enddate>20061213</enddate><creator>Han, Seung Jin</creator><creator>Vaccari, Sergio</creator><creator>Nedachi, Taku</creator><creator>Andersen, Carsten B</creator><creator>Kovacina, Kristina S</creator><creator>Roth, Richard A</creator><creator>Conti, Marco</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>Nature Publishing Group</general><scope>BSCLL</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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</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>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7N</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PCBAR</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20061213</creationdate><title>Protein kinase B/Akt phosphorylation of PDE3A and its role in mammalian oocyte maturation</title><author>Han, Seung Jin ; Vaccari, Sergio ; Nedachi, Taku ; Andersen, Carsten B ; Kovacina, Kristina S ; Roth, Richard A ; Conti, Marco</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6701-4e42ffb332a74c3b9b39e9a0a5dcd74f460672e409bbddad241b1c5bb122c31d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>3',5'-Cyclic-AMP Phosphodiesterases - 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drug effects</topic><topic>Phosphoserine - metabolism</topic><topic>PKB/Akt</topic><topic>Proteins</topic><topic>Proto-Oncogene Proteins c-akt - metabolism</topic><topic>Rodents</topic><topic>Xenopus</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Han, Seung Jin</creatorcontrib><creatorcontrib>Vaccari, Sergio</creatorcontrib><creatorcontrib>Nedachi, Taku</creatorcontrib><creatorcontrib>Andersen, Carsten B</creatorcontrib><creatorcontrib>Kovacina, Kristina S</creatorcontrib><creatorcontrib>Roth, Richard A</creatorcontrib><creatorcontrib>Conti, Marco</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue 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>Public Health Database</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>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</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>Earth, Atmospheric & Aquatic 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>Research Library Prep</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>Research Library</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Han, Seung Jin</au><au>Vaccari, Sergio</au><au>Nedachi, Taku</au><au>Andersen, Carsten B</au><au>Kovacina, Kristina S</au><au>Roth, Richard A</au><au>Conti, Marco</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein kinase B/Akt phosphorylation of PDE3A and its role in mammalian oocyte maturation</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2006-12-13</date><risdate>2006</risdate><volume>25</volume><issue>24</issue><spage>5716</spage><epage>5725</epage><pages>5716-5725</pages><issn>0261-4189</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>cGMP‐inhibited cAMP phosphodiesterase 3A (PDE3A) is expressed in mouse oocytes, and its function is indispensable for meiotic maturation as demonstrated by genetic ablation. Moreover, PDE3 activity is required for insulin/insulin‐like growth factor‐1 stimulation of
Xenopus
oocyte meiotic resumption. Here, we investigated the cAMP‐dependent protein kinase B (PKB)/Akt regulation of PDE3A and its impact on oocyte maturation. Cell‐free incubation of recombinant mouse PDE3A with PKB/Akt or cAMP‐dependent protein kinase A catalytic subunits leads to phosphorylation of the PDE3A protein. Coexpression of PDE3A with constitutively activated PKB/Akt (Myr‐Akt) increases PDE activity as well as its phosphorylation state. Injection of
pde3a
mRNA potentiates insulin‐dependent maturation of
Xenopus
oocytes and rescues the phenotype of
pde3
−/−
mouse oocytes. This effect is greatly decreased by mutation of any of the PDE3A serines 290–292 to alanine in both
Xenopus
and mouse. Microinjection of myr‐Akt in mouse oocytes causes
in vitro
meiotic maturation and this effect requires PDE3A. Collectively, these data indicate that activation of PDE3A by PKB/Akt‐mediated phosphorylation plays a role in the control of PDE3A activity in mammalian oocytes.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>17124499</pmid><doi>10.1038/sj.emboj.7601431</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| source | Springer Nature OA Free Journals |
| subjects | 3',5'-Cyclic-AMP Phosphodiesterases - chemistry 3',5'-Cyclic-AMP Phosphodiesterases - deficiency 3',5'-Cyclic-AMP Phosphodiesterases - metabolism Amino Acid Sequence Animals Cyclic AMP-Dependent Protein Kinases - metabolism Cyclic Nucleotide Phosphodiesterases, Type 3 EMBO06 EMBO37 Enzyme Activation - drug effects Female Gene expression Genetic recombination Humans Incubation Injection Insulin - pharmacology Isoenzymes - metabolism Mammals Maturation-Promoting Factor - metabolism Mice Molecular biology Molecular Sequence Data Mutation oocyte maturation Oocytes - cytology Oocytes - drug effects Oogenesis - drug effects Oogenesis - physiology PDE3A Phenotype phosphorylation Phosphorylation - drug effects Phosphoserine - metabolism PKB/Akt Proteins Proto-Oncogene Proteins c-akt - metabolism Rodents Xenopus |
| title | Protein kinase B/Akt phosphorylation of PDE3A and its role in mammalian oocyte maturation |
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