Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion
FKHR is phosphorylated by protein kinase B (PKB) at Thr24, Ser256 and Ser319 in response to growth factors, stimulating the nuclear exit and inactivation of this transcription factor. Here we identify two further residues, Ser322 and Ser325, that become phosphorylated in insulin‐like growth factor‐1...
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| Veröffentlicht in: | The EMBO journal 2002-05, Vol.21 (9), p.2263-2271 |
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| creator | Rena, Graham Woods, Yvonne L. Prescott, Alan R. Peggie, Mark Unterman, Terry G. Williams, Michayla R. Cohen, Philip |
| description | FKHR is phosphorylated by protein kinase B (PKB) at Thr24, Ser256 and Ser319 in response to growth factors, stimulating the nuclear exit and inactivation of this transcription factor. Here we identify two further residues, Ser322 and Ser325, that become phosphorylated in insulin‐like growth factor‐1 (IGF‐1)‐stimulated cells and which are mediated by the phosphatidylinositol 3‐kinase‐dependent PKB‐catalysed phosphorylation of Ser319. Phosphorylation of Ser319 forms a consensus sequence for phosphorylation by CK1, allowing it to phosphorylate Ser322, which in turn primes the CK1‐catalysed phosphorylation of Ser325. IGF‐1 stimulates the phosphorylation of Thr24, Ser256, Ser319, Ser322 and Ser325 in embryonic stem (ES) cells, but not in PDK1−/− ES cells, providing genetic evidence that PDK1 (the upstream activator of PKB) is required for the phosphorylation of FKHR in mammalian cells. In contrast, the phosphorylation of Ser329 is unaffected by IGF‐1 and the phosphorylation of this site is not decreased in PDK1−/− ES cells. The cluster of phosphorylation sites at Ser319, Ser322, Ser325 and Ser329 appears to accelerate nuclear export by controlling the interaction of FKHR with the Ran‐containing protein complex that mediates this process. |
| doi_str_mv | 10.1093/emboj/21.9.2263 |
| format | Article |
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Here we identify two further residues, Ser322 and Ser325, that become phosphorylated in insulin‐like growth factor‐1 (IGF‐1)‐stimulated cells and which are mediated by the phosphatidylinositol 3‐kinase‐dependent PKB‐catalysed phosphorylation of Ser319. Phosphorylation of Ser319 forms a consensus sequence for phosphorylation by CK1, allowing it to phosphorylate Ser322, which in turn primes the CK1‐catalysed phosphorylation of Ser325. IGF‐1 stimulates the phosphorylation of Thr24, Ser256, Ser319, Ser322 and Ser325 in embryonic stem (ES) cells, but not in PDK1−/− ES cells, providing genetic evidence that PDK1 (the upstream activator of PKB) is required for the phosphorylation of FKHR in mammalian cells. In contrast, the phosphorylation of Ser329 is unaffected by IGF‐1 and the phosphorylation of this site is not decreased in PDK1−/− ES cells. The cluster of phosphorylation sites at Ser319, Ser322, Ser325 and Ser329 appears to accelerate nuclear export by controlling the interaction of FKHR with the Ran‐containing protein complex that mediates this process.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/21.9.2263</identifier><identifier>PMID: 11980723</identifier><identifier>CODEN: EMJODG</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence - physiology ; Androstadienes - pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases - physiology ; Cell Line ; Cell Nucleus - physiology ; CK1 ; Conserved Sequence - physiology ; DNA-Binding Proteins - metabolism ; EMBO09 ; EMBO37 ; Enzyme Inhibitors - pharmacology ; Flavonoids - pharmacology ; forkhead ; Forkhead Box Protein O1 ; Forkhead Transcription Factors ; Glycogen Synthase Kinase 3 ; Growth factors ; Humans ; Inactivation ; nuclear export ; Phosphorylation ; PKB ; ran GTP-Binding Protein - physiology ; SGK ; Sirolimus - pharmacology ; Transcription Factors - metabolism ; Wortmannin</subject><ispartof>The EMBO journal, 2002-05, Vol.21 (9), p.2263-2271</ispartof><rights>European Molecular Biology Organization 2002</rights><rights>Copyright © 2002 European Molecular Biology Organization</rights><rights>Copyright Oxford University Press(England) May 01, 2002</rights><rights>Copyright © 2002 European Molecular Biology Organization 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5746-b77e03f4fc4df25bfd32266abe49b3a66ca25858fdda7eb5170e269b880404823</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125977/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC125977/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,724,777,781,882,1412,1428,27905,27906,45555,45556,46390,46814,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11980723$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rena, Graham</creatorcontrib><creatorcontrib>Woods, Yvonne L.</creatorcontrib><creatorcontrib>Prescott, Alan R.</creatorcontrib><creatorcontrib>Peggie, Mark</creatorcontrib><creatorcontrib>Unterman, Terry G.</creatorcontrib><creatorcontrib>Williams, Michayla R.</creatorcontrib><creatorcontrib>Cohen, Philip</creatorcontrib><title>Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>FKHR is phosphorylated by protein kinase B (PKB) at Thr24, Ser256 and Ser319 in response to growth factors, stimulating the nuclear exit and inactivation of this transcription factor. Here we identify two further residues, Ser322 and Ser325, that become phosphorylated in insulin‐like growth factor‐1 (IGF‐1)‐stimulated cells and which are mediated by the phosphatidylinositol 3‐kinase‐dependent PKB‐catalysed phosphorylation of Ser319. Phosphorylation of Ser319 forms a consensus sequence for phosphorylation by CK1, allowing it to phosphorylate Ser322, which in turn primes the CK1‐catalysed phosphorylation of Ser325. IGF‐1 stimulates the phosphorylation of Thr24, Ser256, Ser319, Ser322 and Ser325 in embryonic stem (ES) cells, but not in PDK1−/− ES cells, providing genetic evidence that PDK1 (the upstream activator of PKB) is required for the phosphorylation of FKHR in mammalian cells. In contrast, the phosphorylation of Ser329 is unaffected by IGF‐1 and the phosphorylation of this site is not decreased in PDK1−/− ES cells. The cluster of phosphorylation sites at Ser319, Ser322, Ser325 and Ser329 appears to accelerate nuclear export by controlling the interaction of FKHR with the Ran‐containing protein complex that mediates this process.</description><subject>Amino Acid Sequence - physiology</subject><subject>Androstadienes - pharmacology</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases - physiology</subject><subject>Cell Line</subject><subject>Cell Nucleus - physiology</subject><subject>CK1</subject><subject>Conserved Sequence - physiology</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>EMBO09</subject><subject>EMBO37</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>Flavonoids - pharmacology</subject><subject>forkhead</subject><subject>Forkhead Box Protein O1</subject><subject>Forkhead Transcription Factors</subject><subject>Glycogen Synthase Kinase 3</subject><subject>Growth factors</subject><subject>Humans</subject><subject>Inactivation</subject><subject>nuclear export</subject><subject>Phosphorylation</subject><subject>PKB</subject><subject>ran GTP-Binding Protein - 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physiology</topic><topic>Androstadienes - pharmacology</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases - physiology</topic><topic>Cell Line</topic><topic>Cell Nucleus - physiology</topic><topic>CK1</topic><topic>Conserved Sequence - physiology</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>EMBO09</topic><topic>EMBO37</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>Flavonoids - pharmacology</topic><topic>forkhead</topic><topic>Forkhead Box Protein O1</topic><topic>Forkhead Transcription Factors</topic><topic>Glycogen Synthase Kinase 3</topic><topic>Growth factors</topic><topic>Humans</topic><topic>Inactivation</topic><topic>nuclear export</topic><topic>Phosphorylation</topic><topic>PKB</topic><topic>ran GTP-Binding Protein - physiology</topic><topic>SGK</topic><topic>Sirolimus - pharmacology</topic><topic>Transcription Factors - metabolism</topic><topic>Wortmannin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rena, Graham</creatorcontrib><creatorcontrib>Woods, Yvonne L.</creatorcontrib><creatorcontrib>Prescott, Alan R.</creatorcontrib><creatorcontrib>Peggie, Mark</creatorcontrib><creatorcontrib>Unterman, Terry G.</creatorcontrib><creatorcontrib>Williams, Michayla R.</creatorcontrib><creatorcontrib>Cohen, Philip</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 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>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</fulltext></delivery><addata><au>Rena, Graham</au><au>Woods, Yvonne L.</au><au>Prescott, Alan R.</au><au>Peggie, Mark</au><au>Unterman, Terry G.</au><au>Williams, Michayla R.</au><au>Cohen, Philip</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>2002-05-01</date><risdate>2002</risdate><volume>21</volume><issue>9</issue><spage>2263</spage><epage>2271</epage><pages>2263-2271</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><coden>EMJODG</coden><abstract>FKHR is phosphorylated by protein kinase B (PKB) at Thr24, Ser256 and Ser319 in response to growth factors, stimulating the nuclear exit and inactivation of this transcription factor. Here we identify two further residues, Ser322 and Ser325, that become phosphorylated in insulin‐like growth factor‐1 (IGF‐1)‐stimulated cells and which are mediated by the phosphatidylinositol 3‐kinase‐dependent PKB‐catalysed phosphorylation of Ser319. Phosphorylation of Ser319 forms a consensus sequence for phosphorylation by CK1, allowing it to phosphorylate Ser322, which in turn primes the CK1‐catalysed phosphorylation of Ser325. IGF‐1 stimulates the phosphorylation of Thr24, Ser256, Ser319, Ser322 and Ser325 in embryonic stem (ES) cells, but not in PDK1−/− ES cells, providing genetic evidence that PDK1 (the upstream activator of PKB) is required for the phosphorylation of FKHR in mammalian cells. In contrast, the phosphorylation of Ser329 is unaffected by IGF‐1 and the phosphorylation of this site is not decreased in PDK1−/− ES cells. The cluster of phosphorylation sites at Ser319, Ser322, Ser325 and Ser329 appears to accelerate nuclear export by controlling the interaction of FKHR with the Ran‐containing protein complex that mediates this process.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>11980723</pmid><doi>10.1093/emboj/21.9.2263</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence - physiology Androstadienes - pharmacology Calcium-Calmodulin-Dependent Protein Kinases - physiology Cell Line Cell Nucleus - physiology CK1 Conserved Sequence - physiology DNA-Binding Proteins - metabolism EMBO09 EMBO37 Enzyme Inhibitors - pharmacology Flavonoids - pharmacology forkhead Forkhead Box Protein O1 Forkhead Transcription Factors Glycogen Synthase Kinase 3 Growth factors Humans Inactivation nuclear export Phosphorylation PKB ran GTP-Binding Protein - physiology SGK Sirolimus - pharmacology Transcription Factors - metabolism Wortmannin |
| title | Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion |
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