{"title":"沉默交配型信息调控因子2同源物1翻译后修饰在癌症和其他疾病中的作用。","authors":"Yeon-Hwa Lee, Su-Jung Kim, Young-Joon Surh","doi":"10.15430/JCP.2022.27.3.157","DOIUrl":null,"url":null,"abstract":"<p><p>Silent mating type information regulator 2 homolog 1 (SIRT1), an NAD<sup>+</sup>-dependent histone/protein deacetylase, has multifarious physiological roles in development, metabolic regulation, and stress response. Thus, its abnormal expression or malfunction is implicated in pathogenesis of various diseases. SIRT1 undergoes post-translational modifications, including phosphorylation, oxidation/reduction, carbonylation, nitrosylation, glycosylation, ubiquitination/deubiquitination, SUMOylation etc. which can modulate its catalytic activity, stability, subcellular localization, and also binding affinity for substrate proteins. This short review highlights the regulation of SIRT1 post-translational modifications and their pathophysiologic implications.</p>","PeriodicalId":15120,"journal":{"name":"Journal of Cancer Prevention","volume":"27 3","pages":"157-169"},"PeriodicalIF":2.5000,"publicationDate":"2022-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5a/4a/jcp-27-3-157.PMC9537581.pdf","citationCount":"0","resultStr":"{\"title\":\"Role of Post-translational Modification of Silent Mating Type Information Regulator 2 Homolog 1 in Cancer and Other Disorders.\",\"authors\":\"Yeon-Hwa Lee, Su-Jung Kim, Young-Joon Surh\",\"doi\":\"10.15430/JCP.2022.27.3.157\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Silent mating type information regulator 2 homolog 1 (SIRT1), an NAD<sup>+</sup>-dependent histone/protein deacetylase, has multifarious physiological roles in development, metabolic regulation, and stress response. Thus, its abnormal expression or malfunction is implicated in pathogenesis of various diseases. SIRT1 undergoes post-translational modifications, including phosphorylation, oxidation/reduction, carbonylation, nitrosylation, glycosylation, ubiquitination/deubiquitination, SUMOylation etc. which can modulate its catalytic activity, stability, subcellular localization, and also binding affinity for substrate proteins. This short review highlights the regulation of SIRT1 post-translational modifications and their pathophysiologic implications.</p>\",\"PeriodicalId\":15120,\"journal\":{\"name\":\"Journal of Cancer Prevention\",\"volume\":\"27 3\",\"pages\":\"157-169\"},\"PeriodicalIF\":2.5000,\"publicationDate\":\"2022-09-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5a/4a/jcp-27-3-157.PMC9537581.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Cancer Prevention\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15430/JCP.2022.27.3.157\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"ONCOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Cancer Prevention","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15430/JCP.2022.27.3.157","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"ONCOLOGY","Score":null,"Total":0}
Role of Post-translational Modification of Silent Mating Type Information Regulator 2 Homolog 1 in Cancer and Other Disorders.
Silent mating type information regulator 2 homolog 1 (SIRT1), an NAD+-dependent histone/protein deacetylase, has multifarious physiological roles in development, metabolic regulation, and stress response. Thus, its abnormal expression or malfunction is implicated in pathogenesis of various diseases. SIRT1 undergoes post-translational modifications, including phosphorylation, oxidation/reduction, carbonylation, nitrosylation, glycosylation, ubiquitination/deubiquitination, SUMOylation etc. which can modulate its catalytic activity, stability, subcellular localization, and also binding affinity for substrate proteins. This short review highlights the regulation of SIRT1 post-translational modifications and their pathophysiologic implications.