Erythropoietin receptor-mediated Egr-1 activation: Structural requirements and functional implications
The transcription factor Egr-1 is encoded by an immediate early response gene and has been shown to be a key regulator in the induction of apoptosis, mitogenesis and differentiation. It is rapidly induced by different stimuli including the glycoprotein hormone erythropoietin. In this report, we anal...
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| Veröffentlicht in: | Cellular signalling 2008-10, Vol.20 (10), p.1848-1854 |
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| creator | Schulze, Christoph Büchse, Tom Mikkat, Stefan Bittorf, Thomas |
| description | The transcription factor Egr-1 is encoded by an immediate early response gene and has been shown to be a key regulator in the induction of apoptosis, mitogenesis and differentiation. It is rapidly induced by different stimuli including the glycoprotein hormone erythropoietin. In this report, we analyse the role of different erythropoietin receptor substructures for the activation of Egr-1 and the functional consequences of Egr-1 overexpression in the erythroleukemic cell line ELM-I-1. The investigation of receptor variants revealed that the activity of JAK2 and the phosphorylation of receptor tyrosine residues are essential preconditions for the ability to target Egr-1. Furthermore, we observed a close correlation of the abilities of receptors to activate the Ras-MAPK pathway and Egr-1. Using mass spectrometry we identified the Ras-GTPase-activating protein-SH3-domain-binding protein 1 (G3BP-1), a component of the Ras network of proteins, as an Egr-1 interacting protein in EPO stimulated ELM-I-1 cells. The overexpression of Egr-1 in these cells resulted in an enhanced rate of spontaneous erythroid differentiation. |
| doi_str_mv | 10.1016/j.cellsig.2008.06.013 |
| format | Article |
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It is rapidly induced by different stimuli including the glycoprotein hormone erythropoietin. In this report, we analyse the role of different erythropoietin receptor substructures for the activation of Egr-1 and the functional consequences of Egr-1 overexpression in the erythroleukemic cell line ELM-I-1. The investigation of receptor variants revealed that the activity of JAK2 and the phosphorylation of receptor tyrosine residues are essential preconditions for the ability to target Egr-1. Furthermore, we observed a close correlation of the abilities of receptors to activate the Ras-MAPK pathway and Egr-1. Using mass spectrometry we identified the Ras-GTPase-activating protein-SH3-domain-binding protein 1 (G3BP-1), a component of the Ras network of proteins, as an Egr-1 interacting protein in EPO stimulated ELM-I-1 cells. 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It is rapidly induced by different stimuli including the glycoprotein hormone erythropoietin. In this report, we analyse the role of different erythropoietin receptor substructures for the activation of Egr-1 and the functional consequences of Egr-1 overexpression in the erythroleukemic cell line ELM-I-1. The investigation of receptor variants revealed that the activity of JAK2 and the phosphorylation of receptor tyrosine residues are essential preconditions for the ability to target Egr-1. Furthermore, we observed a close correlation of the abilities of receptors to activate the Ras-MAPK pathway and Egr-1. Using mass spectrometry we identified the Ras-GTPase-activating protein-SH3-domain-binding protein 1 (G3BP-1), a component of the Ras network of proteins, as an Egr-1 interacting protein in EPO stimulated ELM-I-1 cells. The overexpression of Egr-1 in these cells resulted in an enhanced rate of spontaneous erythroid differentiation.</description><subject>Animals</subject><subject>Cell Differentiation - drug effects</subject><subject>Differentiation</subject><subject>DNA - metabolism</subject><subject>Early Growth Response Protein 1 - chemistry</subject><subject>Early Growth Response Protein 1 - metabolism</subject><subject>Egr-1</subject><subject>Erythroid Cells - cytology</subject><subject>Erythroid Cells - drug effects</subject><subject>Erythroid Cells - enzymology</subject><subject>Erythropoietin receptor</subject><subject>GTPase-Activating Proteins - metabolism</subject><subject>Humans</subject><subject>Immunoprecipitation</subject><subject>Interleukin-3 - pharmacology</subject><subject>Janus Kinase 2 - metabolism</subject><subject>Mice</subject><subject>Mitogen-Activated Protein Kinases - metabolism</subject><subject>Mutant Proteins - metabolism</subject><subject>Phosphotyrosine - metabolism</subject><subject>Protein Binding - drug effects</subject><subject>Ras/MAPK pathway</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>Receptors, Erythropoietin - chemistry</subject><subject>Receptors, Erythropoietin - metabolism</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Signal Transduction - drug effects</subject><subject>STAT Transcription Factors - metabolism</subject><subject>Time Factors</subject><issn>0898-6568</issn><issn>1873-3913</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1P3DAQhi1EBQvtT2iVE7eEcRI7NhdUoS0gIXFoe7a89ph6lS9sB4l_X6e7Uo-c5jDPOyO9DyFfKVQUKL_eVwb7PvqXqgYQFfAKaHNCNlR0TdlI2pySDQgpSs64OCcXMe4BKANen5FzKnjddRI2xG3De_oTpnnymPxYBDQ4pymUA1qvE9pi-xJKWmiT_JtOfhpvip8pLCYtQfcZf118wAHHFAs92sIto1mpvPPD3HvzLxM_k09O9xG_HOcl-f1j--vuoXx6vn-8-_5Umka2qWQMm5ZxZ1jrsMaOUzQ7Z6GlwgKTLWoAZ1FK0e1AN7zNhOXaUWtFp8WuuSRXh7tzmF4XjEkNPq5F6RGnJSouW8akEB-CVDKoO76C7ACaMMUY0Kk5-EGHd0VBrSbUXh1NqNWEAq6yiZz7dnyw7HKX_1PH6jNwewAw9_HmMahoPI4m954lJGUn_8GLvyB8n3c</recordid><startdate>20081001</startdate><enddate>20081001</enddate><creator>Schulze, Christoph</creator><creator>Büchse, Tom</creator><creator>Mikkat, Stefan</creator><creator>Bittorf, Thomas</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></search><sort><creationdate>20081001</creationdate><title>Erythropoietin receptor-mediated Egr-1 activation: Structural requirements and functional implications</title><author>Schulze, Christoph ; Büchse, Tom ; Mikkat, Stefan ; Bittorf, Thomas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c394t-55e3456fc54fe2e761ecbfd0418d0594ea00fde9987b0a364761d6af1dd87a8b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Animals</topic><topic>Cell Differentiation - drug effects</topic><topic>Differentiation</topic><topic>DNA - metabolism</topic><topic>Early Growth Response Protein 1 - chemistry</topic><topic>Early Growth Response Protein 1 - metabolism</topic><topic>Egr-1</topic><topic>Erythroid Cells - cytology</topic><topic>Erythroid Cells - drug effects</topic><topic>Erythroid Cells - enzymology</topic><topic>Erythropoietin receptor</topic><topic>GTPase-Activating Proteins - metabolism</topic><topic>Humans</topic><topic>Immunoprecipitation</topic><topic>Interleukin-3 - pharmacology</topic><topic>Janus Kinase 2 - metabolism</topic><topic>Mice</topic><topic>Mitogen-Activated Protein Kinases - metabolism</topic><topic>Mutant Proteins - metabolism</topic><topic>Phosphotyrosine - metabolism</topic><topic>Protein Binding - drug effects</topic><topic>Ras/MAPK pathway</topic><topic>Receptor, Epidermal Growth Factor - metabolism</topic><topic>Receptors, Erythropoietin - chemistry</topic><topic>Receptors, Erythropoietin - metabolism</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Signal Transduction - drug effects</topic><topic>STAT Transcription Factors - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schulze, Christoph</creatorcontrib><creatorcontrib>Büchse, Tom</creatorcontrib><creatorcontrib>Mikkat, Stefan</creatorcontrib><creatorcontrib>Bittorf, Thomas</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><jtitle>Cellular signalling</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schulze, Christoph</au><au>Büchse, Tom</au><au>Mikkat, Stefan</au><au>Bittorf, Thomas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Erythropoietin receptor-mediated Egr-1 activation: Structural requirements and functional implications</atitle><jtitle>Cellular signalling</jtitle><addtitle>Cell Signal</addtitle><date>2008-10-01</date><risdate>2008</risdate><volume>20</volume><issue>10</issue><spage>1848</spage><epage>1854</epage><pages>1848-1854</pages><issn>0898-6568</issn><eissn>1873-3913</eissn><abstract>The transcription factor Egr-1 is encoded by an immediate early response gene and has been shown to be a key regulator in the induction of apoptosis, mitogenesis and differentiation. It is rapidly induced by different stimuli including the glycoprotein hormone erythropoietin. In this report, we analyse the role of different erythropoietin receptor substructures for the activation of Egr-1 and the functional consequences of Egr-1 overexpression in the erythroleukemic cell line ELM-I-1. The investigation of receptor variants revealed that the activity of JAK2 and the phosphorylation of receptor tyrosine residues are essential preconditions for the ability to target Egr-1. Furthermore, we observed a close correlation of the abilities of receptors to activate the Ras-MAPK pathway and Egr-1. Using mass spectrometry we identified the Ras-GTPase-activating protein-SH3-domain-binding protein 1 (G3BP-1), a component of the Ras network of proteins, as an Egr-1 interacting protein in EPO stimulated ELM-I-1 cells. The overexpression of Egr-1 in these cells resulted in an enhanced rate of spontaneous erythroid differentiation.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>18627790</pmid><doi>10.1016/j.cellsig.2008.06.013</doi><tpages>7</tpages></addata></record> |
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| subjects | Animals Cell Differentiation - drug effects Differentiation DNA - metabolism Early Growth Response Protein 1 - chemistry Early Growth Response Protein 1 - metabolism Egr-1 Erythroid Cells - cytology Erythroid Cells - drug effects Erythroid Cells - enzymology Erythropoietin receptor GTPase-Activating Proteins - metabolism Humans Immunoprecipitation Interleukin-3 - pharmacology Janus Kinase 2 - metabolism Mice Mitogen-Activated Protein Kinases - metabolism Mutant Proteins - metabolism Phosphotyrosine - metabolism Protein Binding - drug effects Ras/MAPK pathway Receptor, Epidermal Growth Factor - metabolism Receptors, Erythropoietin - chemistry Receptors, Erythropoietin - metabolism Recombinant Fusion Proteins - metabolism Signal Transduction - drug effects STAT Transcription Factors - metabolism Time Factors |
| title | Erythropoietin receptor-mediated Egr-1 activation: Structural requirements and functional implications |
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