Oligomerization and maturation of Na,K-ATPase: functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit

@article{Geering1996OligomerizationAM,
  title={Oligomerization and maturation of Na,K-ATPase: functional interaction of the cytoplasmic NH2 terminus of the beta subunit with the alpha subunit},
  author={Kaethi Geering and Ahmed T. Beggah and P W Good and S Girardet and Siddhartha Roy and Dani{\`e}le Schaer and Philippe Jaunin},
  journal={The Journal of Cell Biology},
  year={1996},
  volume={133},
  pages={1193 - 1204}
}
Subunit assembly plays an essential role in the maturation of oligomeric proteins. In this study, we have characterized the main structural and functional consequences of the assembly of alpha and beta subunits of Na,K-ATPase. Xenopus oocytes injected with alpha and/or beta cRNA were treated with brefeldin A, which permitted the accumulation of individual subunits or alpha-beta complexes in the ER. Only alpha subunits that are associated with beta subunits become resistant to trypsin digestion… CONTINUE READING

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Modulation of cation occlusion on Na/K-ATPase by the cytoplasmic domain of the 13 subunit

  • A. Shainskaya, S.J.D. Karlish
  • J. Biol
  • 1996

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