典型文献
NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids
文献摘要：
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 trans-membrane 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.
文献关键词：
中图分类号：
作者姓名：
Yunyan Li;Yong Liu;Huiqin Zhang;Zhen Wang;Maosen Ruan;Jiarong Wang;Jing Yang;Bo Wu;Junfeng Wang
作者机构：
High Magnetic Field Laboratory,CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology,Hefei Institutes of Physical Science,Chinese Academy of Sciences,Hefei,230031,China;University of Science and Technology of China,Hefei,230026,China;Institutes of Physical Science and Information Technology,Anhui University,Hefei,230601,China;Anhui University,Hefei,230039,China
文献出处：
引用格式：
[1]Yunyan Li;Yong Liu;Huiqin Zhang;Zhen Wang;Maosen Ruan;Jiarong Wang;Jing Yang;Bo Wu;Junfeng Wang-.NMR and biochemical characterization of the interaction between FGFR1 juxtamembrane domain and phospholipids)[J].磁共振快报（英文）,2022(04):205-213
A类：
juxtamembrane,FGFRs,JMD,398K,470R,377I,397Y,bicelles
B类：
NMR,biochemical,characterization,interaction,between,FGFR1,domain,phospholipids,Fibroblast,growth,receptors,play,important,role,regulation,proliferation,migration,differentiation,while,key,mediating,these,transmembrane,signal,transduction,processes,Here,expressed,purified,presence,results,from,nuclear,magnetic,resonance,shift,analysis,demonstrate,that,structure,disordered,Yet,terminus,was,observed,form,short,helix,upon,introducing,negatively,charged,dioleoyl,sn,glycero,serine,DOPS,into,its,mimic,Moreover,interacts,FRS2,which,substrate,Hence,propose,model,may,competitively,Our,study,provides,new,understanding
AB值：
0.491289
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