{"title":"应用磷酸化位点特异性抗体测量核受体信号:雌激素受体α的新型磷酸化抗体的表征。","authors":"Mariam H Al-Dhaheri, Brian G Rowan","doi":"10.1621/nrs.04007","DOIUrl":null,"url":null,"abstract":"<p><p>An understanding of posttranslational events in nuclear receptor signaling is crucial for drug design and clinical therapeutic strategies. Phosphorylation is a well-characterized posttranslational modification that regulates subcellular localization and function of nuclear receptors and coregulators. Although the role of single phosphorylation sites in nuclear receptor function has been described, the contribution of combinations of multiple phosphorylation sites to receptor function remains unclear. The development of phosphoantibodies to each phosphorylation site in a nuclear receptor is a powerful tool to address the role of phosphorylation in multiply phosphorylated receptors. However, phosphoantibodies must be rigorously validated prior to use. This review describes the general methodology for design, characterization and validation of phosphoantibodies using the example of eight phosphoantibodies raised against phosphorylation sites in estrogen receptor alpha (ERalpha).</p>","PeriodicalId":87415,"journal":{"name":"Nuclear receptor signaling","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1621/nrs.04007","citationCount":"32","resultStr":"{\"title\":\"Application of phosphorylation site-specific antibodies to measure nuclear receptor signaling: characterization of novel phosphoantibodies for estrogen receptor alpha.\",\"authors\":\"Mariam H Al-Dhaheri, Brian G Rowan\",\"doi\":\"10.1621/nrs.04007\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>An understanding of posttranslational events in nuclear receptor signaling is crucial for drug design and clinical therapeutic strategies. Phosphorylation is a well-characterized posttranslational modification that regulates subcellular localization and function of nuclear receptors and coregulators. Although the role of single phosphorylation sites in nuclear receptor function has been described, the contribution of combinations of multiple phosphorylation sites to receptor function remains unclear. The development of phosphoantibodies to each phosphorylation site in a nuclear receptor is a powerful tool to address the role of phosphorylation in multiply phosphorylated receptors. However, phosphoantibodies must be rigorously validated prior to use. This review describes the general methodology for design, characterization and validation of phosphoantibodies using the example of eight phosphoantibodies raised against phosphorylation sites in estrogen receptor alpha (ERalpha).</p>\",\"PeriodicalId\":87415,\"journal\":{\"name\":\"Nuclear receptor signaling\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2006-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1621/nrs.04007\",\"citationCount\":\"32\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nuclear receptor signaling\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1621/nrs.04007\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2006/4/28 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nuclear receptor signaling","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1621/nrs.04007","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2006/4/28 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
Application of phosphorylation site-specific antibodies to measure nuclear receptor signaling: characterization of novel phosphoantibodies for estrogen receptor alpha.
An understanding of posttranslational events in nuclear receptor signaling is crucial for drug design and clinical therapeutic strategies. Phosphorylation is a well-characterized posttranslational modification that regulates subcellular localization and function of nuclear receptors and coregulators. Although the role of single phosphorylation sites in nuclear receptor function has been described, the contribution of combinations of multiple phosphorylation sites to receptor function remains unclear. The development of phosphoantibodies to each phosphorylation site in a nuclear receptor is a powerful tool to address the role of phosphorylation in multiply phosphorylated receptors. However, phosphoantibodies must be rigorously validated prior to use. This review describes the general methodology for design, characterization and validation of phosphoantibodies using the example of eight phosphoantibodies raised against phosphorylation sites in estrogen receptor alpha (ERalpha).