Functional significance of E2 state stabilization by specific alpha/beta-subunit interactions of Na,K- and H,K-ATPase.

@article{Drr2009FunctionalSO,
  title={Functional significance of E2 state stabilization by specific alpha/beta-subunit interactions of Na,K- and H,K-ATPase.},
  author={Katharina L. D{\"u}rr and Neslihan N. Tavraz and Robert E. Dempski and Ernst Bamberg and Thomas Friedrich},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 6},
  pages={3842-54}
}
The beta-subunits of Na,K-ATPase and H,K-ATPase have important functions in maturation and plasma membrane targeting of the catalytic alpha-subunit but also modulate the transport activity of the holoenzymes. In this study, we show that tryptophan replacement of two highly conserved tyrosines in the transmembrane domain of both Na,K- and gastric H,K-ATPase beta-subunits resulted in considerable shifts of the voltage-dependent E1P/E2P distributions toward the E1P state as inferred from presteady… CONTINUE READING