Current inhibition of human EAG1 potassium channels by the Ca2+ binding protein S100B

FEBS Lett. 2010 Sep 24;584(18):3896-900. doi: 10.1016/j.febslet.2010.07.063. Epub 2010 Aug 12.


Voltage-dependent human ether à go-go (hEAG1) potassium channels are implicated in neuronal signaling as well as in cancer cell proliferation. Unique sensitivity of the channel to intracellular Ca(2+) is mediated by calmodulin (CaM) binding to the intracellular N- and C-termini of the channel. Here we show that application of the acidic calcium-binding protein S100B to inside-out patches of Xenopus oocytes causes Ca(2+)-dependent inhibition of expressed hEAG1 channels. Protein pull-down assays and fluorescence correlation spectroscopy (FCS) revealed that S100B binds to hEAG1 and shares the same binding sites with CaM. Thus, S100B is a potential alternative calcium sensor for hEAG1 potassium channels.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Calcium / metabolism*
  • Cells, Cultured
  • Ether-A-Go-Go Potassium Channels / antagonists & inhibitors*
  • Ether-A-Go-Go Potassium Channels / metabolism
  • Humans
  • Microscopy, Fluorescence
  • Nerve Growth Factors / metabolism*
  • Oocytes
  • S100 Calcium Binding Protein beta Subunit
  • S100 Proteins / metabolism*
  • Xenopus


  • Ether-A-Go-Go Potassium Channels
  • KCNH1 protein, human
  • Nerve Growth Factors
  • S100 Calcium Binding Protein beta Subunit
  • S100 Proteins
  • S100B protein, human
  • Calcium