Functional assembly and purinergic activation of bestrophins

@article{Milenkovic2008FunctionalAA,
  title={Functional assembly and purinergic activation of bestrophins},
  author={Vladimir M Milenkovic and Ren{\'e} Barro Soria and Fadi Aldehni and Rainer Schreiber and Karl Kunzelmann},
  journal={Pfl{\"u}gers Archiv - European Journal of Physiology},
  year={2008},
  volume={458},
  pages={431-441}
}
Proteins of the bestrophin family produce Ca2+-activated Cl− currents and regulate voltage-gated Ca2+ channels. Bestrophin 1 was first identified in the retinal pigment epithelium. Four human paralogs (hBest1–hBest4) exist, and for some bestrophins, dimeric and heterotetrameric structures have been proposed. Here, we demonstrate that hBest1–hBest4 induce Cl− conductances of different amplitudes when expressed in HEK293 cells and when activated through purinergic stimulation. hBest1 mutants that… CONTINUE READING