A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation.

@article{Bhattacharya2010ACS,
  title={A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation.},
  author={Shibani Bhattacharya and Zhongping Dai and Jianquan Li and Sabine C Baxter and David J. E. Callaway and David Cowburn and Zimei Bu},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 13},
  pages={9981-94}
}
The mammalian Na(+)/H(+) exchange regulatory factor 1 (NHERF1) is a multidomain scaffolding protein essential for regulating the intracellular trafficking and macromolecular assembly of transmembrane ion channels and receptors. NHERF1 consists of tandem PDZ-1, PDZ-2 domains that interact with the cytoplasmic domains of membrane proteins and a C-terminal (CT) domain that binds the membrane-cytoskeleton linker protein ezrin. NHERF1 is held in an autoinhibited state through intramolecular… CONTINUE READING