Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.

@article{Bossuyt2009IsoformSO,
  title={Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.},
  author={Julie Bossuyt and Sanda Despa and Fei Han and Zhanjia Hou and Seth L Robia and Jerry B. Lingrel and Donald M. Bers},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 39},
  pages={26749-57}
}
Phospholemman (PLM) phosphorylation mediates enhanced Na/K-ATPase (NKA) function during adrenergic stimulation of the heart. Multiple NKA isoforms exist, and their function/regulation may differ. We combined fluorescence resonance energy transfer (FRET) and functional measurements to investigate isoform specificity of the NKA-PLM interaction. FRET was measured as the increase in the donor fluorescence (CFP-NKA-alpha1 or CFP-NKA-alpha2) during progressive acceptor (PLM-YFP) photobleach in HEK… CONTINUE READING

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