The C-Terminus of Na+,K+-ATPase β-Subunit Contains a Hydrophobic Assembly Domain

  • A. T. Beggah
  • P. Beguin
  • P. Jaunin
  • M. C. Peitsch
  • K. Geering

Abstract

Assembly of catalytic α-subunits of Na+,K+-ATPase with β-subunits is a prerequisite for the structural and functional maturation of newly synthesized α-subunit and its intracellular transport from the ER to the plasma membrane (2). Little is known on the structural domains in α- and β-subunits that are involved in subunit assembly. Recently, Renaud et al (7) have reported that cytoplasmic and transmembrane deletion mutants of β-subunits are all able to assemble with α-subunits, provided that they are capable to insert into ER membranes. Together with the observation that deletions of 11 amino acids from the C-terminal ectodomain abolishes assembly (6), these results suggest that the C-terminal domain of β-subunits contain important structural information for subunit assembly.

Keywords

Polypeptide Alanine Asparagine Ouabain 

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Copyright information

© Dietrich Steinkopff Verlag GmbH & Co. KG, Darmstadt 1994

Authors and Affiliations

  • A. T. Beggah
    • 1
  • P. Beguin
    • 1
  • P. Jaunin
    • 1
  • M. C. Peitsch
    • 2
  • K. Geering
    • 1
  1. 1.Institut de Pharmacologie et de Toxicologie de l’UniversitéLausanneSwitzerland
  2. 2.Institut de Biochimie de l’UniversitéEpalingesSwitzerland

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