Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit.

@article{Devarajan1994AnkyrinBT,
  title={Ankyrin binds to two distinct cytoplasmic domains of Na,K-ATPase alpha subunit.},
  author={Prasad Devarajan and Dominick Scaramuzzino and Jon S. Morrow},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1994},
  volume={91 8},
  pages={2965-9}
}
Ankyrin has emerged as a ubiquitous protein linking integral membrane transport proteins such as Na,K-ATPase to an underlying spectrin cytoskeleton. This interaction is mediated by the alpha subunit of Na,K-ATPase; however, the nature of the ankyrin binding site in Na,K-ATPase is unknown. As a step to determine the mechanism of this interaction, the ankyrin binding region of human erythrocyte spectrin and each of five putative cytoplasmic domains of the Na,K-ATPase alpha subunit have been… CONTINUE READING

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