Transmembrane Nox4 topology revealed by topological determination by Ubiquitin Fusion Assay, a novel method to uncover membrane protein topology
作者: Francis RoussetLeilei ZhangBernard LardyFrançoise MorelMinh Vu Chuong Nguyen
作者单位: 1Univ.Grenoble Alpes, CNRS, CHU Grenoble Alpes, Grenoble INP 1 , TIMC-IMAG, GREPI, 38000, Grenoble Cedex, France
2Laboratoire de Biochimie des Enzymes et des Protéines, Pôle de Biologie, Centre Hospitalier Universitaire Grenoble Alpes, 38700, La Tronche, France
刊名: Biochemical and Biophysical Research Communications, 2020, Vol.521 (2), pp.383-388
来源数据库: Elsevier Journal
DOI: 10.1016/j.bbrc.2019.10.098
关键词: NADH oxidase 4Membrane topologyUbiquitin
英文摘要: Abstract(#br)The NADPH oxidase Nox4 is a multi-pass membrane protein responsible for the generation of reactive oxygen species that are implicated in cellular signaling but may also cause pathological situations when dysregulated. Although topological organization of integral membrane protein dictates its function, only limited experimental data describing Nox4's topology are available.(#br)To provide deeper insight on Nox4 structural organization, we developed a novel method to determinate membrane protein topology in their cellular environment, named Topological Determination by Ubiquitin Fusion Assay (ToDUFA). It is based on the proteolytic capacity of the deubiquitinase enzymes to process ubiquitin fusion proteins. This straightforward method, validated on two well-known protein's...
全文获取路径: Elsevier  (合作)

  • topological 拓扑的
  • topology 局部解剖学
  • membrane 
  • determination 测定
  • protein 蛋白质
  • method 方法
  • uncover 打开
  • novel 长篇小说