Phosphorylation by glycogen synthase kinase of inhibitor-2 does not change its structure in free state
Inhibitor-2 (I2) is a thermostable protein that specifically binds to the catalytic subunit of protein phosphatase-1 (PP1), resulting in the formation of the inactive holoenzyme, ATP-Mg-dependent phosphatase. Phosphorylation of I2 at Thr-72 by glycogen synthase kinase-3 (GSK-3) results in activation...
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| Veröffentlicht in: | FEBS letters 2003-11, Vol.554 (3), p.253-256 |
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| creator | Lin, Ta-Hsien Chen, Yi-Chen Chyan, Chia-lin Tsay, Li-huang Tang, Tzu Chun Jeng, Hao-Hsuan Lin, Fang-Min Huang, Hsien-bin |
| description | Inhibitor-2 (I2) is a thermostable protein that specifically binds to the catalytic subunit of protein phosphatase-1 (PP1), resulting in the formation of the inactive holoenzyme, ATP-Mg-dependent phosphatase. Phosphorylation of I2 at Thr-72 by glycogen synthase kinase-3 (GSK-3) results in activation of the phosphatase, suggesting that kinase action triggers conformational change in the complex. In this paper, we characterize the effect of GSK-3 phosphorylation on the structure of free state I2[1–172] by nuclear magnetic resonance and circular dichroism spectroscopy, and show that phosphorylation has no significant effect on its conformation. We conclude that the conformational changes of ATP-Mg-dependent phosphatase induced by GSK-3 phosphorylation must depend on the interactions between PP1 and I2. |
| doi_str_mv | 10.1016/S0014-5793(03)01097-4 |
| format | Article |
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Phosphorylation of I2 at Thr-72 by glycogen synthase kinase-3 (GSK-3) results in activation of the phosphatase, suggesting that kinase action triggers conformational change in the complex. In this paper, we characterize the effect of GSK-3 phosphorylation on the structure of free state I2[1–172] by nuclear magnetic resonance and circular dichroism spectroscopy, and show that phosphorylation has no significant effect on its conformation. We conclude that the conformational changes of ATP-Mg-dependent phosphatase induced by GSK-3 phosphorylation must depend on the interactions between PP1 and I2.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(03)01097-4</identifier><identifier>PMID: 14623075</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Circular Dichroism ; Escherichia coli - metabolism ; Glycogen Synthase Kinase 3 - genetics ; Glycogen Synthase Kinase 3 - metabolism ; Glycogen synthase kinase-3 ; Humans ; Inhibitor-2 ; Isoenzymes ; Nuclear magnetic resonance ; Nuclear Magnetic Resonance, Biomolecular - methods ; Phosphoprotein Phosphatases - antagonists & inhibitors ; Phosphoprotein Phosphatases - metabolism ; Phosphorylation ; Protein Conformation ; Protein Phosphatase 1 ; Proteins - chemistry ; Proteins - genetics ; Proteins - metabolism ; Rats ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Threonine - metabolism</subject><ispartof>FEBS letters, 2003-11, Vol.554 (3), p.253-256</ispartof><rights>2003 Federation of European Biochemical Societies</rights><rights>FEBS Letters 554 (2003) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4734-ba7cd43aa403421845d224bd7d7fa30218485e48dbecb681200499f167cb961c3</citedby><cites>FETCH-LOGICAL-c4734-ba7cd43aa403421845d224bd7d7fa30218485e48dbecb681200499f167cb961c3</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%2FS0014-5793%2803%2901097-4$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579303010974$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14623075$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lin, Ta-Hsien</creatorcontrib><creatorcontrib>Chen, Yi-Chen</creatorcontrib><creatorcontrib>Chyan, Chia-lin</creatorcontrib><creatorcontrib>Tsay, Li-huang</creatorcontrib><creatorcontrib>Tang, Tzu Chun</creatorcontrib><creatorcontrib>Jeng, Hao-Hsuan</creatorcontrib><creatorcontrib>Lin, Fang-Min</creatorcontrib><creatorcontrib>Huang, Hsien-bin</creatorcontrib><title>Phosphorylation by glycogen synthase kinase of inhibitor-2 does not change its structure in free state</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>Inhibitor-2 (I2) is a thermostable protein that specifically binds to the catalytic subunit of protein phosphatase-1 (PP1), resulting in the formation of the inactive holoenzyme, ATP-Mg-dependent phosphatase. Phosphorylation of I2 at Thr-72 by glycogen synthase kinase-3 (GSK-3) results in activation of the phosphatase, suggesting that kinase action triggers conformational change in the complex. In this paper, we characterize the effect of GSK-3 phosphorylation on the structure of free state I2[1–172] by nuclear magnetic resonance and circular dichroism spectroscopy, and show that phosphorylation has no significant effect on its conformation. We conclude that the conformational changes of ATP-Mg-dependent phosphatase induced by GSK-3 phosphorylation must depend on the interactions between PP1 and I2.</description><subject>Animals</subject><subject>Circular Dichroism</subject><subject>Escherichia coli - metabolism</subject><subject>Glycogen Synthase Kinase 3 - genetics</subject><subject>Glycogen Synthase Kinase 3 - metabolism</subject><subject>Glycogen synthase kinase-3</subject><subject>Humans</subject><subject>Inhibitor-2</subject><subject>Isoenzymes</subject><subject>Nuclear magnetic resonance</subject><subject>Nuclear Magnetic Resonance, Biomolecular - methods</subject><subject>Phosphoprotein Phosphatases - antagonists & inhibitors</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylation</subject><subject>Protein Conformation</subject><subject>Protein Phosphatase 1</subject><subject>Proteins - chemistry</subject><subject>Proteins - genetics</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Threonine - metabolism</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFP3DAQhS1UVBbanwDyqSqHgB07cXJCgFiohARS27Pl2JONadZebKdV_j3J7qo9FsnSaN68eWN9CJ1SckEJLS-_E0J5VoiafSXsnFBSi4wfoAWtBMsYL6sPaPHXcoSOY3whU1_R-iM6orzMGRHFArXPnY-bzoexV8l6h5sRr_pR-xU4HEeXOhUB_7JuLr7F1nW2scmHLMfGQ8TOJ6w75VaAbYo4pjDoNISpc7gNAJOiEnxCh63qI3ze1xP0c3n34_Yhe3y6_3Z7_ZhpLhjPGiW04UwpThjPacULk-e8McKIVjEyK1UBvDIN6KasaE4Ir-uWlkI3dUk1O0Ffdrmb4F8HiEmubdTQ98qBH6IUlNOcCzoZi51RBx9jgFZugl2rMEpK5AxYbgHLmZ4k05sBSz7tne0PDM0azL-tPdHJ8LAz_LE9jO9Llcu7m3w7mQeEbeX51tUuCiZivy0EGbUFp8HYADpJ4-1_fvsGcEWe9w</recordid><startdate>20031120</startdate><enddate>20031120</enddate><creator>Lin, Ta-Hsien</creator><creator>Chen, Yi-Chen</creator><creator>Chyan, Chia-lin</creator><creator>Tsay, Li-huang</creator><creator>Tang, Tzu Chun</creator><creator>Jeng, Hao-Hsuan</creator><creator>Lin, Fang-Min</creator><creator>Huang, Hsien-bin</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></search><sort><creationdate>20031120</creationdate><title>Phosphorylation by glycogen synthase kinase of inhibitor-2 does not change its structure in free state</title><author>Lin, Ta-Hsien ; Chen, Yi-Chen ; Chyan, Chia-lin ; Tsay, Li-huang ; Tang, Tzu Chun ; Jeng, Hao-Hsuan ; Lin, Fang-Min ; Huang, Hsien-bin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4734-ba7cd43aa403421845d224bd7d7fa30218485e48dbecb681200499f167cb961c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Animals</topic><topic>Circular Dichroism</topic><topic>Escherichia coli - metabolism</topic><topic>Glycogen Synthase Kinase 3 - genetics</topic><topic>Glycogen Synthase Kinase 3 - metabolism</topic><topic>Glycogen synthase kinase-3</topic><topic>Humans</topic><topic>Inhibitor-2</topic><topic>Isoenzymes</topic><topic>Nuclear magnetic resonance</topic><topic>Nuclear Magnetic Resonance, Biomolecular - methods</topic><topic>Phosphoprotein Phosphatases - antagonists & inhibitors</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>Protein Conformation</topic><topic>Protein Phosphatase 1</topic><topic>Proteins - chemistry</topic><topic>Proteins - genetics</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Threonine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lin, Ta-Hsien</creatorcontrib><creatorcontrib>Chen, Yi-Chen</creatorcontrib><creatorcontrib>Chyan, Chia-lin</creatorcontrib><creatorcontrib>Tsay, Li-huang</creatorcontrib><creatorcontrib>Tang, Tzu Chun</creatorcontrib><creatorcontrib>Jeng, Hao-Hsuan</creatorcontrib><creatorcontrib>Lin, Fang-Min</creatorcontrib><creatorcontrib>Huang, Hsien-bin</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><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lin, Ta-Hsien</au><au>Chen, Yi-Chen</au><au>Chyan, Chia-lin</au><au>Tsay, Li-huang</au><au>Tang, Tzu Chun</au><au>Jeng, Hao-Hsuan</au><au>Lin, Fang-Min</au><au>Huang, Hsien-bin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation by glycogen synthase kinase of inhibitor-2 does not change its structure in free state</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2003-11-20</date><risdate>2003</risdate><volume>554</volume><issue>3</issue><spage>253</spage><epage>256</epage><pages>253-256</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>Inhibitor-2 (I2) is a thermostable protein that specifically binds to the catalytic subunit of protein phosphatase-1 (PP1), resulting in the formation of the inactive holoenzyme, ATP-Mg-dependent phosphatase. Phosphorylation of I2 at Thr-72 by glycogen synthase kinase-3 (GSK-3) results in activation of the phosphatase, suggesting that kinase action triggers conformational change in the complex. In this paper, we characterize the effect of GSK-3 phosphorylation on the structure of free state I2[1–172] by nuclear magnetic resonance and circular dichroism spectroscopy, and show that phosphorylation has no significant effect on its conformation. We conclude that the conformational changes of ATP-Mg-dependent phosphatase induced by GSK-3 phosphorylation must depend on the interactions between PP1 and I2.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>14623075</pmid><doi>10.1016/S0014-5793(03)01097-4</doi><tpages>4</tpages><oa>free_for_read</oa></addata></record> |
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| source | Wiley Free Content; MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Animals Circular Dichroism Escherichia coli - metabolism Glycogen Synthase Kinase 3 - genetics Glycogen Synthase Kinase 3 - metabolism Glycogen synthase kinase-3 Humans Inhibitor-2 Isoenzymes Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular - methods Phosphoprotein Phosphatases - antagonists & inhibitors Phosphoprotein Phosphatases - metabolism Phosphorylation Protein Conformation Protein Phosphatase 1 Proteins - chemistry Proteins - genetics Proteins - metabolism Rats Recombinant Proteins - chemistry Recombinant Proteins - genetics Recombinant Proteins - metabolism Threonine - metabolism |
| title | Phosphorylation by glycogen synthase kinase of inhibitor-2 does not change its structure in free state |
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