Golgi apparatus casein kinase phosphorylates bioactive Ser-6 of bone morphogenetic protein 15 and growth and differentiation factor 9
Bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9 (GDF-9) are oocyte-secreted factors that play essential roles in human folliculogenesis and ovulation. Their bioactivity is tightly regulated through phosphorylation, likely to occur within the Golgi apparatus of the secr...
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| Veröffentlicht in: | FEBS letters 2010-02, Vol.584 (4), p.801-805 |
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| creator | Tibaldi, Elena Arrigoni, Giorgio Martinez, Heather M. Inagaki, Kenichi Shimasaki, Shunichi Pinna, Lorenzo A. |
| description | Bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9 (GDF-9) are oocyte-secreted factors that play essential roles in human folliculogenesis and ovulation. Their bioactivity is tightly regulated through phosphorylation, likely to occur within the Golgi apparatus of the secretory pathway. Here we show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. rhBMP-15, in particular, is an excellent substrate for G-CK. In each protein a single residue is phosphorylated by G-CK, corresponding to the serine residue at the sixth position of the mature region of both rhBMP-15 and rhGDF-9, whose phosphorylation is required for biological activity. |
| doi_str_mv | 10.1016/j.febslet.2009.12.052 |
| format | Article |
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Their bioactivity is tightly regulated through phosphorylation, likely to occur within the Golgi apparatus of the secretory pathway. Here we show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. rhBMP-15, in particular, is an excellent substrate for G-CK. In each protein a single residue is phosphorylated by G-CK, corresponding to the serine residue at the sixth position of the mature region of both rhBMP-15 and rhGDF-9, whose phosphorylation is required for biological activity.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2009.12.052</identifier><identifier>PMID: 20067794</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; BMP-15 ; Bone Morphogenetic Protein 15 - genetics ; Bone Morphogenetic Protein 15 - metabolism ; bone morphogenetic protein-15 ; Casein Kinases - metabolism ; Catalysis ; Electrophoresis, Polyacrylamide Gel ; Female ; G-CK ; GDF-9 ; Golgi Apparatus - enzymology ; Golgi apparatus casein kinase ; Golgi-casein kinase ; growth and differentiation factor-9 ; Growth Differentiation Factor 9 - genetics ; Growth Differentiation Factor 9 - metabolism ; Humans ; Kinetics ; MALDI TOF/TOF ; Mammary Glands, Animal - enzymology ; Mass Spectrometry ; matrix-assisted laser-desorption/ionization time-of-flight/time-of-flight ; MS/MS ; Oocyte-secreted factor ; Phosphorylation ; Phosphorylation - drug effects ; Rats ; Recombinant Proteins - metabolism ; Serine - metabolism ; Staurosporine - pharmacology ; tandem mass spectrometry</subject><ispartof>FEBS letters, 2010-02, Vol.584 (4), p.801-805</ispartof><rights>2010 Federation of European Biochemical Societies</rights><rights>FEBS Letters 584 (2010) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><rights>2009 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6295-5f7d21b293bd18e658dfc0a9a041445f1681cd0f77f4f49e45c8a26f1fdf67b23</citedby><cites>FETCH-LOGICAL-c6295-5f7d21b293bd18e658dfc0a9a041445f1681cd0f77f4f49e45c8a26f1fdf67b23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2009.12.052$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2009.12.052$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1417,1433,3550,27924,27925,45574,45575,45995,46409,46833</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20067794$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tibaldi, Elena</creatorcontrib><creatorcontrib>Arrigoni, Giorgio</creatorcontrib><creatorcontrib>Martinez, Heather M.</creatorcontrib><creatorcontrib>Inagaki, Kenichi</creatorcontrib><creatorcontrib>Shimasaki, Shunichi</creatorcontrib><creatorcontrib>Pinna, Lorenzo A.</creatorcontrib><title>Golgi apparatus casein kinase phosphorylates bioactive Ser-6 of bone morphogenetic protein 15 and growth and differentiation factor 9</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9 (GDF-9) are oocyte-secreted factors that play essential roles in human folliculogenesis and ovulation. Their bioactivity is tightly regulated through phosphorylation, likely to occur within the Golgi apparatus of the secretory pathway. Here we show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. rhBMP-15, in particular, is an excellent substrate for G-CK. In each protein a single residue is phosphorylated by G-CK, corresponding to the serine residue at the sixth position of the mature region of both rhBMP-15 and rhGDF-9, whose phosphorylation is required for biological activity.</description><subject>Animals</subject><subject>BMP-15</subject><subject>Bone Morphogenetic Protein 15 - genetics</subject><subject>Bone Morphogenetic Protein 15 - metabolism</subject><subject>bone morphogenetic protein-15</subject><subject>Casein Kinases - metabolism</subject><subject>Catalysis</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Female</subject><subject>G-CK</subject><subject>GDF-9</subject><subject>Golgi Apparatus - enzymology</subject><subject>Golgi apparatus casein kinase</subject><subject>Golgi-casein kinase</subject><subject>growth and differentiation factor-9</subject><subject>Growth Differentiation Factor 9 - genetics</subject><subject>Growth Differentiation Factor 9 - metabolism</subject><subject>Humans</subject><subject>Kinetics</subject><subject>MALDI TOF/TOF</subject><subject>Mammary Glands, Animal - enzymology</subject><subject>Mass Spectrometry</subject><subject>matrix-assisted laser-desorption/ionization time-of-flight/time-of-flight</subject><subject>MS/MS</subject><subject>Oocyte-secreted factor</subject><subject>Phosphorylation</subject><subject>Phosphorylation - drug effects</subject><subject>Rats</subject><subject>Recombinant Proteins - metabolism</subject><subject>Serine - metabolism</subject><subject>Staurosporine - pharmacology</subject><subject>tandem mass spectrometry</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkk2P0zAQhi0EYpfCTwD5xinFdvyRXECw2g-klTgsnC3HGbcuaRxst6v-AP43Di0rOC2WrBnL7zya0TsIvaZkSQmV7zZLB10aIC8ZIe2SsiUR7Ak6p42qq5rL5ik6J4TySqi2PkMvUtqQ8m5o-xydlRKpVMvP0c_rMKw8NtNkosm7hK1J4Ef83Y8lwdM6pHLjYTAZEu58MDb7PeA7iJXEweEujIC3IRbVCkbI3uIphjwzqMBm7PEqhvu8_p323jmIMGZvsg8jdoUWIm5fomfODAleneICfbu6_HpxU91-uf588fG2spK1ohJO9Yx2rK27njYgRdM7S0xrCKecC0dlQ21PnFKOO94CF7YxTDrqeidVx-oFen_kTrtuC70tnUQz6Cn6rYkHHYzX__6Mfq1XYa9ZwxhRogDengAx_NhBynrrk4VhMCOEXdKKS8oVEc3jyrpuOZUlLJA4Km0MKUVwD_1Qomev9UafvNaz15oyXbwudW_-Huah6o-5RXBzFNz7AQ7_R9VXl5_Y3bw4895QMh82z_3hiILizt5D1Ml6GC30PoLNug_-kW5_AcY31g8</recordid><startdate>20100219</startdate><enddate>20100219</enddate><creator>Tibaldi, Elena</creator><creator>Arrigoni, Giorgio</creator><creator>Martinez, Heather M.</creator><creator>Inagaki, Kenichi</creator><creator>Shimasaki, Shunichi</creator><creator>Pinna, Lorenzo A.</creator><general>Elsevier B.V</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>7X8</scope><scope>7QP</scope><scope>5PM</scope></search><sort><creationdate>20100219</creationdate><title>Golgi apparatus casein kinase phosphorylates bioactive Ser-6 of bone morphogenetic protein 15 and growth and differentiation factor 9</title><author>Tibaldi, Elena ; Arrigoni, Giorgio ; Martinez, Heather M. ; Inagaki, Kenichi ; Shimasaki, Shunichi ; Pinna, Lorenzo A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6295-5f7d21b293bd18e658dfc0a9a041445f1681cd0f77f4f49e45c8a26f1fdf67b23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>BMP-15</topic><topic>Bone Morphogenetic Protein 15 - genetics</topic><topic>Bone Morphogenetic Protein 15 - metabolism</topic><topic>bone morphogenetic protein-15</topic><topic>Casein Kinases - metabolism</topic><topic>Catalysis</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Female</topic><topic>G-CK</topic><topic>GDF-9</topic><topic>Golgi Apparatus - enzymology</topic><topic>Golgi apparatus casein kinase</topic><topic>Golgi-casein kinase</topic><topic>growth and differentiation factor-9</topic><topic>Growth Differentiation Factor 9 - genetics</topic><topic>Growth Differentiation Factor 9 - metabolism</topic><topic>Humans</topic><topic>Kinetics</topic><topic>MALDI TOF/TOF</topic><topic>Mammary Glands, Animal - enzymology</topic><topic>Mass Spectrometry</topic><topic>matrix-assisted laser-desorption/ionization time-of-flight/time-of-flight</topic><topic>MS/MS</topic><topic>Oocyte-secreted factor</topic><topic>Phosphorylation</topic><topic>Phosphorylation - drug effects</topic><topic>Rats</topic><topic>Recombinant Proteins - metabolism</topic><topic>Serine - metabolism</topic><topic>Staurosporine - pharmacology</topic><topic>tandem mass spectrometry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tibaldi, Elena</creatorcontrib><creatorcontrib>Arrigoni, Giorgio</creatorcontrib><creatorcontrib>Martinez, Heather M.</creatorcontrib><creatorcontrib>Inagaki, Kenichi</creatorcontrib><creatorcontrib>Shimasaki, Shunichi</creatorcontrib><creatorcontrib>Pinna, Lorenzo A.</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>MEDLINE - Academic</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tibaldi, Elena</au><au>Arrigoni, Giorgio</au><au>Martinez, Heather M.</au><au>Inagaki, Kenichi</au><au>Shimasaki, Shunichi</au><au>Pinna, Lorenzo A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Golgi apparatus casein kinase phosphorylates bioactive Ser-6 of bone morphogenetic protein 15 and growth and differentiation factor 9</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2010-02-19</date><risdate>2010</risdate><volume>584</volume><issue>4</issue><spage>801</spage><epage>805</epage><pages>801-805</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Bone morphogenetic protein-15 (BMP-15) and growth and differentiation factor-9 (GDF-9) are oocyte-secreted factors that play essential roles in human folliculogenesis and ovulation. Their bioactivity is tightly regulated through phosphorylation, likely to occur within the Golgi apparatus of the secretory pathway. Here we show that Golgi apparatus casein kinase (G-CK) catalyzes the phosphorylation of rhBMP-15 and rhGDF-9. rhBMP-15, in particular, is an excellent substrate for G-CK. In each protein a single residue is phosphorylated by G-CK, corresponding to the serine residue at the sixth position of the mature region of both rhBMP-15 and rhGDF-9, whose phosphorylation is required for biological activity.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>20067794</pmid><doi>10.1016/j.febslet.2009.12.052</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 2010-02, Vol.584 (4), p.801-805 |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Wiley Online Library Free Content; Access via Wiley Online Library; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals BMP-15 Bone Morphogenetic Protein 15 - genetics Bone Morphogenetic Protein 15 - metabolism bone morphogenetic protein-15 Casein Kinases - metabolism Catalysis Electrophoresis, Polyacrylamide Gel Female G-CK GDF-9 Golgi Apparatus - enzymology Golgi apparatus casein kinase Golgi-casein kinase growth and differentiation factor-9 Growth Differentiation Factor 9 - genetics Growth Differentiation Factor 9 - metabolism Humans Kinetics MALDI TOF/TOF Mammary Glands, Animal - enzymology Mass Spectrometry matrix-assisted laser-desorption/ionization time-of-flight/time-of-flight MS/MS Oocyte-secreted factor Phosphorylation Phosphorylation - drug effects Rats Recombinant Proteins - metabolism Serine - metabolism Staurosporine - pharmacology tandem mass spectrometry |
| title | Golgi apparatus casein kinase phosphorylates bioactive Ser-6 of bone morphogenetic protein 15 and growth and differentiation factor 9 |
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