Glucocorticoids act within minutes to inhibit recruitment of signalling factors to activated EGF receptors through a receptor‐dependent, transcription‐independent mechanism
Recruitment to activated tyrosine kinase growth factor receptors of Grb2 and p21ras leads to downstream activation of the kinases Raf, MAPK/Erk kinase (Mek) and, subsequently, extracellular signal‐regulated kinase (Erk). Activated Erk phosphorylates specific serine residues within cytosolic phosphol...
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| creator | Croxtall, Jamie D Choudhury, Qam Flower, Rod J |
| description | Recruitment to activated tyrosine kinase growth factor receptors of Grb2 and p21ras leads to downstream activation of the kinases Raf, MAPK/Erk kinase (Mek) and, subsequently, extracellular signal‐regulated kinase (Erk). Activated Erk phosphorylates specific serine residues within cytosolic phospholipase A2 (PLA2), promoting enzyme translocation to membranes and facilitating liberation of arachidonic acid (AA).
In the A549 human adenocarcinoma cell line dexamethasone inhibited epidermal growth factor (EGF)‐stimulated cytosolic PLA2 (cPLA2) activation and AA release by blocking the recruitment of Grb2 to the activated EGF receptor (EGF‐R) through a glucocorticoid receptor (GR)‐dependent (RU486‐sensitive), transcription‐independent (actinomycin‐insensitive), mechanism.
The dexamethasone‐induced block of Grb2 recruitment was parallelled by changes in phosphorylation status and subcellular localization of lipocortin 1 (LC1) and an increase in the amount of the tyrosine phosphoprotein co‐localized with EGF‐R.
Like dexamethasone, peptides containing E‐Q‐E‐Y‐V from the N‐terminal domain of LC1 also blocked ligand‐induced association of Grb2, p21ras and Raf.
Our results point to an unsuspected rapid effect of glucocorticoids, mediated by occupation of GR but not by changes in gene transcription, which is brought about by competition between LC1 and Grb2 leading to a failure of recruitment off signalling factors to EGF‐R
British Journal of Pharmacology (2000) 130, 289–298; doi:10.1038/sj.bjp.0703272 |
| doi_str_mv | 10.1038/sj.bjp.0703272 |
| format | Article |
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In the A549 human adenocarcinoma cell line dexamethasone inhibited epidermal growth factor (EGF)‐stimulated cytosolic PLA2 (cPLA2) activation and AA release by blocking the recruitment of Grb2 to the activated EGF receptor (EGF‐R) through a glucocorticoid receptor (GR)‐dependent (RU486‐sensitive), transcription‐independent (actinomycin‐insensitive), mechanism.
The dexamethasone‐induced block of Grb2 recruitment was parallelled by changes in phosphorylation status and subcellular localization of lipocortin 1 (LC1) and an increase in the amount of the tyrosine phosphoprotein co‐localized with EGF‐R.
Like dexamethasone, peptides containing E‐Q‐E‐Y‐V from the N‐terminal domain of LC1 also blocked ligand‐induced association of Grb2, p21ras and Raf.
Our results point to an unsuspected rapid effect of glucocorticoids, mediated by occupation of GR but not by changes in gene transcription, which is brought about by competition between LC1 and Grb2 leading to a failure of recruitment off signalling factors to EGF‐R
British Journal of Pharmacology (2000) 130, 289–298; doi:10.1038/sj.bjp.0703272</description><identifier>ISSN: 0007-1188</identifier><identifier>EISSN: 1476-5381</identifier><identifier>DOI: 10.1038/sj.bjp.0703272</identifier><identifier>PMID: 10807665</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>A549 cells ; Adaptor Proteins, Signal Transducing ; annexin 1 ; Annexin A1 - biosynthesis ; Annexin A1 - metabolism ; Binding, Competitive ; Dexamethasone - pharmacology ; Enzyme Activation ; epidermal growth factor ; epidermal growth factor receptors ; glucocorticoids ; Glucocorticoids - pharmacology ; Grb2 ; GRB2 Adaptor Protein ; Humans ; Lipocortin 1 ; MAP Kinase Signaling System - physiology ; mitogen‐activated protein kinase ; phospholipase A2 ; Phospholipases A - metabolism ; Phosphorylation - drug effects ; Protein Conformation ; Proteins - chemistry ; Proteins - metabolism ; Receptor, Epidermal Growth Factor - metabolism ; Receptors, Glucocorticoid - metabolism ; Signal Transduction - drug effects ; Signal Transduction - physiology ; Transcription, Genetic ; Tumor Cells, Cultured</subject><ispartof>British journal of pharmacology, 2000-05, Vol.130 (2), p.289-298</ispartof><rights>2000 Nature Publishing Group</rights><rights>Copyright Nature Publishing Group May 2000</rights><rights>Copyright 2000, Nature Publishing Group 2000 Nature Publishing Group</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4578-e7555f475b624554cdb0c65053e7f8068da5cdb3e5f671a884892d6361e2f9a83</citedby><cites>FETCH-LOGICAL-c4578-e7555f475b624554cdb0c65053e7f8068da5cdb3e5f671a884892d6361e2f9a83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1572055/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1572055/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10807665$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Croxtall, Jamie D</creatorcontrib><creatorcontrib>Choudhury, Qam</creatorcontrib><creatorcontrib>Flower, Rod J</creatorcontrib><title>Glucocorticoids act within minutes to inhibit recruitment of signalling factors to activated EGF receptors through a receptor‐dependent, transcription‐independent mechanism</title><title>British journal of pharmacology</title><addtitle>Br J Pharmacol</addtitle><description>Recruitment to activated tyrosine kinase growth factor receptors of Grb2 and p21ras leads to downstream activation of the kinases Raf, MAPK/Erk kinase (Mek) and, subsequently, extracellular signal‐regulated kinase (Erk). Activated Erk phosphorylates specific serine residues within cytosolic phospholipase A2 (PLA2), promoting enzyme translocation to membranes and facilitating liberation of arachidonic acid (AA).
In the A549 human adenocarcinoma cell line dexamethasone inhibited epidermal growth factor (EGF)‐stimulated cytosolic PLA2 (cPLA2) activation and AA release by blocking the recruitment of Grb2 to the activated EGF receptor (EGF‐R) through a glucocorticoid receptor (GR)‐dependent (RU486‐sensitive), transcription‐independent (actinomycin‐insensitive), mechanism.
The dexamethasone‐induced block of Grb2 recruitment was parallelled by changes in phosphorylation status and subcellular localization of lipocortin 1 (LC1) and an increase in the amount of the tyrosine phosphoprotein co‐localized with EGF‐R.
Like dexamethasone, peptides containing E‐Q‐E‐Y‐V from the N‐terminal domain of LC1 also blocked ligand‐induced association of Grb2, p21ras and Raf.
Our results point to an unsuspected rapid effect of glucocorticoids, mediated by occupation of GR but not by changes in gene transcription, which is brought about by competition between LC1 and Grb2 leading to a failure of recruitment off signalling factors to EGF‐R
British Journal of Pharmacology (2000) 130, 289–298; doi:10.1038/sj.bjp.0703272</description><subject>A549 cells</subject><subject>Adaptor Proteins, Signal Transducing</subject><subject>annexin 1</subject><subject>Annexin A1 - biosynthesis</subject><subject>Annexin A1 - metabolism</subject><subject>Binding, Competitive</subject><subject>Dexamethasone - pharmacology</subject><subject>Enzyme Activation</subject><subject>epidermal growth factor</subject><subject>epidermal growth factor receptors</subject><subject>glucocorticoids</subject><subject>Glucocorticoids - pharmacology</subject><subject>Grb2</subject><subject>GRB2 Adaptor Protein</subject><subject>Humans</subject><subject>Lipocortin 1</subject><subject>MAP Kinase Signaling System - physiology</subject><subject>mitogen‐activated protein kinase</subject><subject>phospholipase A2</subject><subject>Phospholipases A - metabolism</subject><subject>Phosphorylation - drug effects</subject><subject>Protein Conformation</subject><subject>Proteins - chemistry</subject><subject>Proteins - metabolism</subject><subject>Receptor, Epidermal Growth Factor - metabolism</subject><subject>Receptors, Glucocorticoid - metabolism</subject><subject>Signal Transduction - drug effects</subject><subject>Signal Transduction - physiology</subject><subject>Transcription, Genetic</subject><subject>Tumor Cells, Cultured</subject><issn>0007-1188</issn><issn>1476-5381</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFksFu1DAQhiMEokvhyhFZHDg1ix3HsfeCVKp2i1QJDnC2HMfZTJTYwXZa9cYj8Ch9Jp4EL1mtChdOtub_5tevmcmy1wSvCabifejXdT-tMce04MWTbEVKXuWMCvI0W2GMeU6IECfZixB6jJPI2fPshGCBeVWxVfawHWbttPMRtIMmIKUjuoPYgUUj2DmagKJDYDuoISJvtJ8hjsZG5FoUYGfVMIDdoTY1Ov8HTj-4VdE06HJ7tW8x0yJ13s27Dqlj7dePn42ZjG2S3xmKXtmgPUwRnE0S2KOIRqM7ZSGML7NnrRqCeXV4T7NvV5dfL67zm8_bTxfnN7kuGRe54YyxtuSsroqSsVI3NdYVw4wa3gpciUaxVKOGtRUnSohSbIqmohUxRbtRgp5mHxbfaa5H0-gUwqtBTh5G5e-lUyD_Vix0cuduJWG8wIwlg3cHA---zyZEOULQZhiUNW4OkhOCCeYkgW__AXs3-zTXIAvCSdoY3UPrBdLeheBNe0xCsNxfggy9TJcgD5eQGt48zv8IX1afALoAdzCY-__YyY9frgndCPobSfLH_g</recordid><startdate>200005</startdate><enddate>200005</enddate><creator>Croxtall, Jamie D</creator><creator>Choudhury, Qam</creator><creator>Flower, Rod J</creator><general>Blackwell Publishing Ltd</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>3V.</scope><scope>7QP</scope><scope>7RV</scope><scope>7TK</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200005</creationdate><title>Glucocorticoids act within minutes to inhibit recruitment of signalling factors to activated EGF receptors through a receptor‐dependent, transcription‐independent mechanism</title><author>Croxtall, Jamie D ; 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Activated Erk phosphorylates specific serine residues within cytosolic phospholipase A2 (PLA2), promoting enzyme translocation to membranes and facilitating liberation of arachidonic acid (AA).
In the A549 human adenocarcinoma cell line dexamethasone inhibited epidermal growth factor (EGF)‐stimulated cytosolic PLA2 (cPLA2) activation and AA release by blocking the recruitment of Grb2 to the activated EGF receptor (EGF‐R) through a glucocorticoid receptor (GR)‐dependent (RU486‐sensitive), transcription‐independent (actinomycin‐insensitive), mechanism.
The dexamethasone‐induced block of Grb2 recruitment was parallelled by changes in phosphorylation status and subcellular localization of lipocortin 1 (LC1) and an increase in the amount of the tyrosine phosphoprotein co‐localized with EGF‐R.
Like dexamethasone, peptides containing E‐Q‐E‐Y‐V from the N‐terminal domain of LC1 also blocked ligand‐induced association of Grb2, p21ras and Raf.
Our results point to an unsuspected rapid effect of glucocorticoids, mediated by occupation of GR but not by changes in gene transcription, which is brought about by competition between LC1 and Grb2 leading to a failure of recruitment off signalling factors to EGF‐R
British Journal of Pharmacology (2000) 130, 289–298; doi:10.1038/sj.bjp.0703272</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>10807665</pmid><doi>10.1038/sj.bjp.0703272</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | A549 cells Adaptor Proteins, Signal Transducing annexin 1 Annexin A1 - biosynthesis Annexin A1 - metabolism Binding, Competitive Dexamethasone - pharmacology Enzyme Activation epidermal growth factor epidermal growth factor receptors glucocorticoids Glucocorticoids - pharmacology Grb2 GRB2 Adaptor Protein Humans Lipocortin 1 MAP Kinase Signaling System - physiology mitogen‐activated protein kinase phospholipase A2 Phospholipases A - metabolism Phosphorylation - drug effects Protein Conformation Proteins - chemistry Proteins - metabolism Receptor, Epidermal Growth Factor - metabolism Receptors, Glucocorticoid - metabolism Signal Transduction - drug effects Signal Transduction - physiology Transcription, Genetic Tumor Cells, Cultured |
| title | Glucocorticoids act within minutes to inhibit recruitment of signalling factors to activated EGF receptors through a receptor‐dependent, transcription‐independent mechanism |
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