Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells
The physiological role of the prion protein is largely unknown. Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the mitogen activated protein kinases (MAPKs) extrace...
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| Veröffentlicht in: | FEBS letters 2004-10, Vol.576 (1), p.114-118 |
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| creator | Monnet, Céline Gavard, Julie Mège, René-Marc Sobel, André |
| description | The physiological role of the prion protein is largely unknown. Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the mitogen activated protein kinases (MAPKs) extracellular receptor kinases 1 and 2 (ERK1/2), and also of the microtubule-destabilizing protein stathmin at serine 16. The specificity of this antibody-mediated activation was ascertained by its inhibition by prion small interfering RNA. The phosphorylation of ERK1/2 but not that of stathmin was abolished by the MAPK/ERK kinase 1 inhibitor U0126, whereas both signaling pathways were blocked by the specific inhibitor of the epidermal growth factor receptor AG1478, suggesting the likely recruitment of this receptor upon prion clustering. |
| doi_str_mv | 10.1016/j.febslet.2004.08.076 |
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Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the mitogen activated protein kinases (MAPKs) extracellular receptor kinases 1 and 2 (ERK1/2), and also of the microtubule-destabilizing protein stathmin at serine 16. The specificity of this antibody-mediated activation was ascertained by its inhibition by prion small interfering RNA. The phosphorylation of ERK1/2 but not that of stathmin was abolished by the MAPK/ERK kinase 1 inhibitor U0126, whereas both signaling pathways were blocked by the specific inhibitor of the epidermal growth factor receptor AG1478, suggesting the likely recruitment of this receptor upon prion clustering.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2004.08.076</identifier><identifier>PMID: 15474021</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Antibodies, Monoclonal - metabolism ; Blotting, Western ; Butadienes - pharmacology ; Cells, Cultured ; Clustering ; EGF receptor ; EGFR, epidermal growth factor receptor ; Enzyme Inhibitors - pharmacology ; ERK, extracellular receptor kinase ; Fluorescent Antibody Technique, Indirect ; GPI, glycosylphosphatidylinositol ; mAb, monoclonal antibody ; MAP kinase ; MAPK, mitogen activated protein kinase ; Mice ; Microscopy, Confocal ; Microtubule Proteins - metabolism ; Mitogen-Activated Protein Kinase 1 - drug effects ; Mitogen-Activated Protein Kinase 1 - metabolism ; Mitogen-Activated Protein Kinase 3 - drug effects ; Mitogen-Activated Protein Kinase 3 - metabolism ; MKK, MAPK/ERK kinase ; Neurons - physiology ; Nitriles - pharmacology ; PBS, phosphate-buffered saline ; Phosphoproteins - metabolism ; Phosphorylation - drug effects ; Prion signaling ; PrPC Proteins - physiology ; PrPc, cellular prion protein ; PrPsc, scrapie prion protein ; Quinazolines ; RNA, Small Interfering - antagonists & inhibitors ; ROS, reactive oxygen species ; siRNA ; siRNA, small interfering RNA ; Stathmin ; Tyrphostins - pharmacology</subject><ispartof>FEBS letters, 2004-10, Vol.576 (1), p.114-118</ispartof><rights>2004 Federation of European Biochemical Societies</rights><rights>FEBS Letters 576 (2004) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright 2004 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5704-f17ffeeba4b11503247153a242386409b4ce7a22ab4b63f4601e83d052d8dbed3</citedby><cites>FETCH-LOGICAL-c5704-f17ffeeba4b11503247153a242386409b4ce7a22ab4b63f4601e83d052d8dbed3</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.2004.08.076$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2004.08.076$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,1417,1433,3549,27923,27924,45573,45574,45994,46408,46832</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15474021$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Monnet, Céline</creatorcontrib><creatorcontrib>Gavard, Julie</creatorcontrib><creatorcontrib>Mège, René-Marc</creatorcontrib><creatorcontrib>Sobel, André</creatorcontrib><title>Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The physiological role of the prion protein is largely unknown. Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the mitogen activated protein kinases (MAPKs) extracellular receptor kinases 1 and 2 (ERK1/2), and also of the microtubule-destabilizing protein stathmin at serine 16. The specificity of this antibody-mediated activation was ascertained by its inhibition by prion small interfering RNA. The phosphorylation of ERK1/2 but not that of stathmin was abolished by the MAPK/ERK kinase 1 inhibitor U0126, whereas both signaling pathways were blocked by the specific inhibitor of the epidermal growth factor receptor AG1478, suggesting the likely recruitment of this receptor upon prion clustering.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - metabolism</subject><subject>Blotting, Western</subject><subject>Butadienes - pharmacology</subject><subject>Cells, Cultured</subject><subject>Clustering</subject><subject>EGF receptor</subject><subject>EGFR, epidermal growth factor receptor</subject><subject>Enzyme Inhibitors - pharmacology</subject><subject>ERK, extracellular receptor kinase</subject><subject>Fluorescent Antibody Technique, Indirect</subject><subject>GPI, glycosylphosphatidylinositol</subject><subject>mAb, monoclonal antibody</subject><subject>MAP kinase</subject><subject>MAPK, mitogen activated protein kinase</subject><subject>Mice</subject><subject>Microscopy, Confocal</subject><subject>Microtubule Proteins - metabolism</subject><subject>Mitogen-Activated Protein Kinase 1 - drug effects</subject><subject>Mitogen-Activated Protein Kinase 1 - metabolism</subject><subject>Mitogen-Activated Protein Kinase 3 - drug effects</subject><subject>Mitogen-Activated Protein Kinase 3 - metabolism</subject><subject>MKK, MAPK/ERK kinase</subject><subject>Neurons - physiology</subject><subject>Nitriles - pharmacology</subject><subject>PBS, phosphate-buffered saline</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation - drug effects</subject><subject>Prion signaling</subject><subject>PrPC Proteins - physiology</subject><subject>PrPc, cellular prion protein</subject><subject>PrPsc, scrapie prion protein</subject><subject>Quinazolines</subject><subject>RNA, Small Interfering - antagonists & inhibitors</subject><subject>ROS, reactive oxygen species</subject><subject>siRNA</subject><subject>siRNA, small interfering RNA</subject><subject>Stathmin</subject><subject>Tyrphostins - pharmacology</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUU1v1DAUtBCoXUp_AignbkmfP2InJwSrbYuohNSWs-XEL6xXXqfYSdH-exx2JY7lYFvPnhmPZgh5T6GiQOXVrhqwSx6nigGICpoKlHxFVrRRvORCNq_JCoCKslYtPydvU9pBnhvanpFzWgslgNEV2a79nCaMLvwsxqHo0fvZm1g8RTeGvI8TulC4YOceU7G5_0avWGGCLdJkpu0-vz1tx5RXPHgzLZx8dfNIS1UEnOMYjP8rmt6RN4PxCS9P5wX5cb15XN-Wd99vvq4_35V9rUCUA1XDgNgZ0VFaA2dC0ZobJhhvpIC2Ez0qw5jpRCf5ICRQbLiFmtnGdmj5Bfl41M3ef82YJr13aXFgAo5z0lK2EmQrXgQyqAG4WoD1EdjHMaWIg87h7E08aAp66ULv9KkLvXShodG5i8z7cPpg7vZo_7FO4WfA7RHw23k8_J-qvt58YQ9LsUuvIIBSEIvHT0cpzNE-O4w69Q5Dj9ZF7CdtR_eC2z_oeLJ2</recordid><startdate>20041008</startdate><enddate>20041008</enddate><creator>Monnet, Céline</creator><creator>Gavard, Julie</creator><creator>Mège, René-Marc</creator><creator>Sobel, André</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>7TK</scope><scope>7X8</scope></search><sort><creationdate>20041008</creationdate><title>Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells</title><author>Monnet, Céline ; Gavard, Julie ; Mège, René-Marc ; Sobel, André</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5704-f17ffeeba4b11503247153a242386409b4ce7a22ab4b63f4601e83d052d8dbed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - metabolism</topic><topic>Blotting, Western</topic><topic>Butadienes - pharmacology</topic><topic>Cells, Cultured</topic><topic>Clustering</topic><topic>EGF receptor</topic><topic>EGFR, epidermal growth factor receptor</topic><topic>Enzyme Inhibitors - pharmacology</topic><topic>ERK, extracellular receptor kinase</topic><topic>Fluorescent Antibody Technique, Indirect</topic><topic>GPI, glycosylphosphatidylinositol</topic><topic>mAb, monoclonal antibody</topic><topic>MAP kinase</topic><topic>MAPK, mitogen activated protein kinase</topic><topic>Mice</topic><topic>Microscopy, Confocal</topic><topic>Microtubule Proteins - metabolism</topic><topic>Mitogen-Activated Protein Kinase 1 - drug effects</topic><topic>Mitogen-Activated Protein Kinase 1 - metabolism</topic><topic>Mitogen-Activated Protein Kinase 3 - drug effects</topic><topic>Mitogen-Activated Protein Kinase 3 - metabolism</topic><topic>MKK, MAPK/ERK kinase</topic><topic>Neurons - physiology</topic><topic>Nitriles - pharmacology</topic><topic>PBS, phosphate-buffered saline</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation - drug effects</topic><topic>Prion signaling</topic><topic>PrPC Proteins - physiology</topic><topic>PrPc, cellular prion protein</topic><topic>PrPsc, scrapie prion protein</topic><topic>Quinazolines</topic><topic>RNA, Small Interfering - antagonists & inhibitors</topic><topic>ROS, reactive oxygen species</topic><topic>siRNA</topic><topic>siRNA, small interfering RNA</topic><topic>Stathmin</topic><topic>Tyrphostins - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Monnet, Céline</creatorcontrib><creatorcontrib>Gavard, Julie</creatorcontrib><creatorcontrib>Mège, René-Marc</creatorcontrib><creatorcontrib>Sobel, André</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>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Monnet, Céline</au><au>Gavard, Julie</au><au>Mège, René-Marc</au><au>Sobel, André</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2004-10-08</date><risdate>2004</risdate><volume>576</volume><issue>1</issue><spage>114</spage><epage>118</epage><pages>114-118</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>The physiological role of the prion protein is largely unknown. Here, clustering of prion at the surface of GT1-7 cells was observed upon anti-prion antibody treatments. This clustering was associated with a rapid and transient phosphorylation of the mitogen activated protein kinases (MAPKs) extracellular receptor kinases 1 and 2 (ERK1/2), and also of the microtubule-destabilizing protein stathmin at serine 16. The specificity of this antibody-mediated activation was ascertained by its inhibition by prion small interfering RNA. The phosphorylation of ERK1/2 but not that of stathmin was abolished by the MAPK/ERK kinase 1 inhibitor U0126, whereas both signaling pathways were blocked by the specific inhibitor of the epidermal growth factor receptor AG1478, suggesting the likely recruitment of this receptor upon prion clustering.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>15474021</pmid><doi>10.1016/j.febslet.2004.08.076</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Free Content; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Antibodies, Monoclonal - metabolism Blotting, Western Butadienes - pharmacology Cells, Cultured Clustering EGF receptor EGFR, epidermal growth factor receptor Enzyme Inhibitors - pharmacology ERK, extracellular receptor kinase Fluorescent Antibody Technique, Indirect GPI, glycosylphosphatidylinositol mAb, monoclonal antibody MAP kinase MAPK, mitogen activated protein kinase Mice Microscopy, Confocal Microtubule Proteins - metabolism Mitogen-Activated Protein Kinase 1 - drug effects Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinase 3 - drug effects Mitogen-Activated Protein Kinase 3 - metabolism MKK, MAPK/ERK kinase Neurons - physiology Nitriles - pharmacology PBS, phosphate-buffered saline Phosphoproteins - metabolism Phosphorylation - drug effects Prion signaling PrPC Proteins - physiology PrPc, cellular prion protein PrPsc, scrapie prion protein Quinazolines RNA, Small Interfering - antagonists & inhibitors ROS, reactive oxygen species siRNA siRNA, small interfering RNA Stathmin Tyrphostins - pharmacology |
| title | Clustering of cellular prion protein induces ERK1/2 and stathmin phosphorylation in GT1-7 neuronal cells |
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