Yunyan Li , Yong Liu , Huiqin Zhang , Zhen Wang , Maosen Ruan , Jiarong Wang , Jing Yang , Bo Wu , Junfeng Wang
{"title":"FGFR1近膜结构域与磷脂相互作用的核磁共振和生化表征","authors":"Yunyan Li , Yong Liu , Huiqin Zhang , Zhen Wang , Maosen Ruan , Jiarong Wang , Jing Yang , Bo Wu , Junfeng Wang","doi":"10.1016/j.mrl.2022.07.002","DOIUrl":null,"url":null,"abstract":"<div><p>Fibroblast growth factor receptors (FGFRs) play an important role in the regulation of cell proliferation, migration and differentiation, while the juxtamembrane domain (JMD) of FGFRs is the key in mediating these transmembrane signal transduction processes. Here, we expressed and purified the JMD (398K-470R) of FGFR1 with the presence of transmembrane domain (377I-397Y). The results from nuclear magnetic resonance (NMR) chemical shift analysis demonstrate that the main structure of JMD is disordered. Yet, the N-terminus of JMD was observed to form a short α-helix upon introducing negatively charged lipid 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS) into its membrane mimic bicelles. Moreover, the N-terminus of JMD interacts with FRS2α, which is a substrate 2α of FGFR. Hence, we propose a model that FGFR1-JMD may interact with FRS2α and negatively charged lipids competitively. Our study provides a new understanding on the role of the JMD of FGFRs.</p></div>","PeriodicalId":93594,"journal":{"name":"Magnetic Resonance Letters","volume":"2 4","pages":"Pages 205-213"},"PeriodicalIF":1.7000,"publicationDate":"2022-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2772516222000274/pdfft?md5=fe6259e165cab66398dc1a2c06a56580&pid=1-s2.0-S2772516222000274-main.pdf","citationCount":"0","resultStr":"{\"title\":\"NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids\",\"authors\":\"Yunyan Li , Yong Liu , Huiqin Zhang , Zhen Wang , Maosen Ruan , Jiarong Wang , Jing Yang , Bo Wu , Junfeng Wang\",\"doi\":\"10.1016/j.mrl.2022.07.002\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Fibroblast growth factor receptors (FGFRs) play an important role in the regulation of cell proliferation, migration and differentiation, while the juxtamembrane domain (JMD) of FGFRs is the key in mediating these transmembrane signal transduction processes. Here, we expressed and purified the JMD (398K-470R) of FGFR1 with the presence of transmembrane domain (377I-397Y). The results from nuclear magnetic resonance (NMR) chemical shift analysis demonstrate that the main structure of JMD is disordered. Yet, the N-terminus of JMD was observed to form a short α-helix upon introducing negatively charged lipid 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS) into its membrane mimic bicelles. Moreover, the N-terminus of JMD interacts with FRS2α, which is a substrate 2α of FGFR. Hence, we propose a model that FGFR1-JMD may interact with FRS2α and negatively charged lipids competitively. Our study provides a new understanding on the role of the JMD of FGFRs.</p></div>\",\"PeriodicalId\":93594,\"journal\":{\"name\":\"Magnetic Resonance Letters\",\"volume\":\"2 4\",\"pages\":\"Pages 205-213\"},\"PeriodicalIF\":1.7000,\"publicationDate\":\"2022-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S2772516222000274/pdfft?md5=fe6259e165cab66398dc1a2c06a56580&pid=1-s2.0-S2772516222000274-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Magnetic Resonance Letters\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2772516222000274\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Magnetic Resonance Letters","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2772516222000274","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids
Fibroblast growth factor receptors (FGFRs) play an important role in the regulation of cell proliferation, migration and differentiation, while the juxtamembrane domain (JMD) of FGFRs is the key in mediating these transmembrane signal transduction processes. Here, we expressed and purified the JMD (398K-470R) of FGFR1 with the presence of transmembrane domain (377I-397Y). The results from nuclear magnetic resonance (NMR) chemical shift analysis demonstrate that the main structure of JMD is disordered. Yet, the N-terminus of JMD was observed to form a short α-helix upon introducing negatively charged lipid 1,2-dioleoyl-sn-glycero-3-phospho-L-serine (DOPS) into its membrane mimic bicelles. Moreover, the N-terminus of JMD interacts with FRS2α, which is a substrate 2α of FGFR. Hence, we propose a model that FGFR1-JMD may interact with FRS2α and negatively charged lipids competitively. Our study provides a new understanding on the role of the JMD of FGFRs.
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