FMS-like tyrosine kinase 3 interacts with the glucocorticoid receptor complex and affects glucocorticoid dependent signaling
The glucocorticoid receptor (GR) forms part of a multiprotein complex consisting of chaperones and proteins active in glucocorticoid signaling and other pathways. By immunoaffinity purification of GR, followed by Edman sequencing and Western blotting, we identified the FMS-like tyrosine kinase 3 (Fl...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2008-04, Vol.368 (3), p.569-574 |
|---|---|
| Hauptverfasser: | , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 574 |
|---|---|
| container_issue | 3 |
| container_start_page | 569 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 368 |
| creator | Asadi, Abolfazl Hedman, Erik Widén, Christina Zilliacus, Johanna Gustafsson, Jan-Åke Wikström, Ann-Charlotte |
| description | The glucocorticoid receptor (GR) forms part of a multiprotein complex consisting of chaperones and proteins active in glucocorticoid signaling and other pathways. By immunoaffinity purification of GR, followed by Edman sequencing and Western blotting, we identified the FMS-like tyrosine kinase 3 (Flt3) as a GR-interacting protein in rat liver and hepatoma cells. Flt3 interacts with both non-liganded and liganded GR. The DNA-binding domain of GR is sufficient for Flt3 interaction as shown by GST-pull down experiments. Studies of the effects of Flt3 and its ligand FL in glucocorticoid-driven reporter-gene assays in Cos7 cells, show that co-transfection with Flt3 and FL potentiates glucocorticoid effects. Treatment with FL had no effect on GR location and Dex induced translocation of GR was unaffected by FL. In summary, GR and Flt3 interact, affecting GR signaling. This novel cross-talk between GR and a hematopoietic growth factor might also imply glucocorticoid effects on Flt3-mediated signaling. |
| doi_str_mv | 10.1016/j.bbrc.2008.01.146 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_swepu</sourceid><recordid>TN_cdi_swepub_primary_oai_swepub_ki_se_565952</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X08001678</els_id><sourcerecordid>20810212</sourcerecordid><originalsourceid>FETCH-LOGICAL-c473t-4968ec871a85b17c31f9661202921b0618efc5522e48487350d58b194d4b3573</originalsourceid><addsrcrecordid>eNqFkkGL1DAUx4so7rj6BTxITt5a30ubNgEvsrgqrHhwD95Cmr7OZqbT1iR1XfDDmzKjC4J6Sgi_3-OR_z_LniMUCFi_2hVt623BAWQBWGBVP8g2CApyjlA9zDYAUOdc4Zez7EkIOwBMjHqcnaHkNapGbbIflx8_54PbE4t3fgpuJLZ3ownESubGSN7YGNitizcs3hDbDoud7OSjs5PrmCdLc5w8s9NhHug7M2PHTN_TKv3BdjTT2NEYWXDb0Qxu3D7NHvVmCPTsdJ5n15dvry_e51ef3n24eHOV26opY16pWpKVDRopWmxsib2qa-TAFccWapTUWyE4p0pWsikFdEK2qKquakvRlOdZfhwbbmleWj17dzD-Tk_G6dPTPt1Ii1oowROv_srPfurupV8iYt2AFBUk9-XRTeDXhULUBxcsDYMZaVqCbqAUshHlf0EOEoHjug0_gjblEzz1v_dB0GsP9E6vPdBrDzSgThkn6cVp-tIeqLtXTsEn4PURoPTv3xx5Hayj0VLnUqhRd5P71_yfYeDGQQ</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20810212</pqid></control><display><type>article</type><title>FMS-like tyrosine kinase 3 interacts with the glucocorticoid receptor complex and affects glucocorticoid dependent signaling</title><source>MEDLINE</source><source>Access via ScienceDirect (Elsevier)</source><creator>Asadi, Abolfazl ; Hedman, Erik ; Widén, Christina ; Zilliacus, Johanna ; Gustafsson, Jan-Åke ; Wikström, Ann-Charlotte</creator><creatorcontrib>Asadi, Abolfazl ; Hedman, Erik ; Widén, Christina ; Zilliacus, Johanna ; Gustafsson, Jan-Åke ; Wikström, Ann-Charlotte</creatorcontrib><description>The glucocorticoid receptor (GR) forms part of a multiprotein complex consisting of chaperones and proteins active in glucocorticoid signaling and other pathways. By immunoaffinity purification of GR, followed by Edman sequencing and Western blotting, we identified the FMS-like tyrosine kinase 3 (Flt3) as a GR-interacting protein in rat liver and hepatoma cells. Flt3 interacts with both non-liganded and liganded GR. The DNA-binding domain of GR is sufficient for Flt3 interaction as shown by GST-pull down experiments. Studies of the effects of Flt3 and its ligand FL in glucocorticoid-driven reporter-gene assays in Cos7 cells, show that co-transfection with Flt3 and FL potentiates glucocorticoid effects. Treatment with FL had no effect on GR location and Dex induced translocation of GR was unaffected by FL. In summary, GR and Flt3 interact, affecting GR signaling. This novel cross-talk between GR and a hematopoietic growth factor might also imply glucocorticoid effects on Flt3-mediated signaling.</description><identifier>ISSN: 0006-291X</identifier><identifier>ISSN: 1090-2104</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2008.01.146</identifier><identifier>PMID: 18261979</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cells, Cultured ; Flt3 ; fms-Like Tyrosine Kinase 3 - metabolism ; Glucocorticoid receptor ; Glucocorticoids ; Glucocorticoids - metabolism ; GST-pull down ; Hepatocytes - metabolism ; Immunoprecipitation ; Medicin och hälsovetenskap ; Rats ; Receptors, Glucocorticoid - metabolism ; Signal Transduction - physiology</subject><ispartof>Biochemical and biophysical research communications, 2008-04, Vol.368 (3), p.569-574</ispartof><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c473t-4968ec871a85b17c31f9661202921b0618efc5522e48487350d58b194d4b3573</citedby><cites>FETCH-LOGICAL-c473t-4968ec871a85b17c31f9661202921b0618efc5522e48487350d58b194d4b3573</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2008.01.146$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18261979$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:116708540$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Asadi, Abolfazl</creatorcontrib><creatorcontrib>Hedman, Erik</creatorcontrib><creatorcontrib>Widén, Christina</creatorcontrib><creatorcontrib>Zilliacus, Johanna</creatorcontrib><creatorcontrib>Gustafsson, Jan-Åke</creatorcontrib><creatorcontrib>Wikström, Ann-Charlotte</creatorcontrib><title>FMS-like tyrosine kinase 3 interacts with the glucocorticoid receptor complex and affects glucocorticoid dependent signaling</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The glucocorticoid receptor (GR) forms part of a multiprotein complex consisting of chaperones and proteins active in glucocorticoid signaling and other pathways. By immunoaffinity purification of GR, followed by Edman sequencing and Western blotting, we identified the FMS-like tyrosine kinase 3 (Flt3) as a GR-interacting protein in rat liver and hepatoma cells. Flt3 interacts with both non-liganded and liganded GR. The DNA-binding domain of GR is sufficient for Flt3 interaction as shown by GST-pull down experiments. Studies of the effects of Flt3 and its ligand FL in glucocorticoid-driven reporter-gene assays in Cos7 cells, show that co-transfection with Flt3 and FL potentiates glucocorticoid effects. Treatment with FL had no effect on GR location and Dex induced translocation of GR was unaffected by FL. In summary, GR and Flt3 interact, affecting GR signaling. This novel cross-talk between GR and a hematopoietic growth factor might also imply glucocorticoid effects on Flt3-mediated signaling.</description><subject>Animals</subject><subject>Cells, Cultured</subject><subject>Flt3</subject><subject>fms-Like Tyrosine Kinase 3 - metabolism</subject><subject>Glucocorticoid receptor</subject><subject>Glucocorticoids</subject><subject>Glucocorticoids - metabolism</subject><subject>GST-pull down</subject><subject>Hepatocytes - metabolism</subject><subject>Immunoprecipitation</subject><subject>Medicin och hälsovetenskap</subject><subject>Rats</subject><subject>Receptors, Glucocorticoid - metabolism</subject><subject>Signal Transduction - physiology</subject><issn>0006-291X</issn><issn>1090-2104</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkkGL1DAUx4so7rj6BTxITt5a30ubNgEvsrgqrHhwD95Cmr7OZqbT1iR1XfDDmzKjC4J6Sgi_3-OR_z_LniMUCFi_2hVt623BAWQBWGBVP8g2CApyjlA9zDYAUOdc4Zez7EkIOwBMjHqcnaHkNapGbbIflx8_54PbE4t3fgpuJLZ3ownESubGSN7YGNitizcs3hDbDoud7OSjs5PrmCdLc5w8s9NhHug7M2PHTN_TKv3BdjTT2NEYWXDb0Qxu3D7NHvVmCPTsdJ5n15dvry_e51ef3n24eHOV26opY16pWpKVDRopWmxsib2qa-TAFccWapTUWyE4p0pWsikFdEK2qKquakvRlOdZfhwbbmleWj17dzD-Tk_G6dPTPt1Ii1oowROv_srPfurupV8iYt2AFBUk9-XRTeDXhULUBxcsDYMZaVqCbqAUshHlf0EOEoHjug0_gjblEzz1v_dB0GsP9E6vPdBrDzSgThkn6cVp-tIeqLtXTsEn4PURoPTv3xx5Hayj0VLnUqhRd5P71_yfYeDGQQ</recordid><startdate>20080411</startdate><enddate>20080411</enddate><creator>Asadi, Abolfazl</creator><creator>Hedman, Erik</creator><creator>Widén, Christina</creator><creator>Zilliacus, Johanna</creator><creator>Gustafsson, Jan-Åke</creator><creator>Wikström, Ann-Charlotte</creator><general>Elsevier Inc</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>7TM</scope><scope>7X8</scope><scope>ADTPV</scope><scope>AOWAS</scope></search><sort><creationdate>20080411</creationdate><title>FMS-like tyrosine kinase 3 interacts with the glucocorticoid receptor complex and affects glucocorticoid dependent signaling</title><author>Asadi, Abolfazl ; Hedman, Erik ; Widén, Christina ; Zilliacus, Johanna ; Gustafsson, Jan-Åke ; Wikström, Ann-Charlotte</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c473t-4968ec871a85b17c31f9661202921b0618efc5522e48487350d58b194d4b3573</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Cells, Cultured</topic><topic>Flt3</topic><topic>fms-Like Tyrosine Kinase 3 - metabolism</topic><topic>Glucocorticoid receptor</topic><topic>Glucocorticoids</topic><topic>Glucocorticoids - metabolism</topic><topic>GST-pull down</topic><topic>Hepatocytes - metabolism</topic><topic>Immunoprecipitation</topic><topic>Medicin och hälsovetenskap</topic><topic>Rats</topic><topic>Receptors, Glucocorticoid - metabolism</topic><topic>Signal Transduction - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Asadi, Abolfazl</creatorcontrib><creatorcontrib>Hedman, Erik</creatorcontrib><creatorcontrib>Widén, Christina</creatorcontrib><creatorcontrib>Zilliacus, Johanna</creatorcontrib><creatorcontrib>Gustafsson, Jan-Åke</creatorcontrib><creatorcontrib>Wikström, Ann-Charlotte</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>SwePub</collection><collection>SwePub Articles</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Asadi, Abolfazl</au><au>Hedman, Erik</au><au>Widén, Christina</au><au>Zilliacus, Johanna</au><au>Gustafsson, Jan-Åke</au><au>Wikström, Ann-Charlotte</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>FMS-like tyrosine kinase 3 interacts with the glucocorticoid receptor complex and affects glucocorticoid dependent signaling</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2008-04-11</date><risdate>2008</risdate><volume>368</volume><issue>3</issue><spage>569</spage><epage>574</epage><pages>569-574</pages><issn>0006-291X</issn><issn>1090-2104</issn><eissn>1090-2104</eissn><abstract>The glucocorticoid receptor (GR) forms part of a multiprotein complex consisting of chaperones and proteins active in glucocorticoid signaling and other pathways. By immunoaffinity purification of GR, followed by Edman sequencing and Western blotting, we identified the FMS-like tyrosine kinase 3 (Flt3) as a GR-interacting protein in rat liver and hepatoma cells. Flt3 interacts with both non-liganded and liganded GR. The DNA-binding domain of GR is sufficient for Flt3 interaction as shown by GST-pull down experiments. Studies of the effects of Flt3 and its ligand FL in glucocorticoid-driven reporter-gene assays in Cos7 cells, show that co-transfection with Flt3 and FL potentiates glucocorticoid effects. Treatment with FL had no effect on GR location and Dex induced translocation of GR was unaffected by FL. In summary, GR and Flt3 interact, affecting GR signaling. This novel cross-talk between GR and a hematopoietic growth factor might also imply glucocorticoid effects on Flt3-mediated signaling.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18261979</pmid><doi>10.1016/j.bbrc.2008.01.146</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2008-04, Vol.368 (3), p.569-574 |
| issn | 0006-291X 1090-2104 1090-2104 |
| language | eng |
| recordid | cdi_swepub_primary_oai_swepub_ki_se_565952 |
| source | MEDLINE; Access via ScienceDirect (Elsevier) |
| subjects | Animals Cells, Cultured Flt3 fms-Like Tyrosine Kinase 3 - metabolism Glucocorticoid receptor Glucocorticoids Glucocorticoids - metabolism GST-pull down Hepatocytes - metabolism Immunoprecipitation Medicin och hälsovetenskap Rats Receptors, Glucocorticoid - metabolism Signal Transduction - physiology |
| title | FMS-like tyrosine kinase 3 interacts with the glucocorticoid receptor complex and affects glucocorticoid dependent signaling |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-03T07%3A38%3A22IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_swepu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=FMS-like%20tyrosine%20kinase%203%20interacts%20with%20the%20glucocorticoid%20receptor%20complex%20and%20affects%20glucocorticoid%20dependent%20signaling&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Asadi,%20Abolfazl&rft.date=2008-04-11&rft.volume=368&rft.issue=3&rft.spage=569&rft.epage=574&rft.pages=569-574&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2008.01.146&rft_dat=%3Cproquest_swepu%3E20810212%3C/proquest_swepu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20810212&rft_id=info:pmid/18261979&rft_els_id=S0006291X08001678&rfr_iscdi=true |