P-type ATPase diversity and evolution: the origins of ouabain sensitivity and subunit assembly

Cell Mol Biol (Noisy-le-grand). 2001 Mar;47(2):325-33.

Abstract

Molecular aspects of the diversity of P-type ATPases are explored in this review. From the substrate specificities among different ATPase molecules, the existence of isoforms within a single class of pump becomes evident and it is now recognized as a universal phenomenon. From the phylogenetic analyses using a vast collection of the deduced amino acid sequences for the P-type ATPase subunits, it also becomes evident that the divergence of substrate-specificity occurred early in the evolution and has been conserved ever since. Further extensive analyses identify a set of novel isoforms that retain an ancestral characteristic of the Na+/K+-(H+/K+-)ATPases in invertebrates.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Calcium-Transporting ATPases / chemistry
  • Calcium-Transporting ATPases / classification
  • Calcium-Transporting ATPases / genetics*
  • Calcium-Transporting ATPases / metabolism
  • Catalytic Domain
  • Evolution, Molecular*
  • H(+)-K(+)-Exchanging ATPase / chemistry
  • H(+)-K(+)-Exchanging ATPase / classification
  • H(+)-K(+)-Exchanging ATPase / genetics*
  • H(+)-K(+)-Exchanging ATPase / metabolism
  • Humans
  • Isoenzymes / genetics
  • Models, Molecular
  • Molecular Sequence Data
  • Phylogeny
  • Protein Subunits
  • Sequence Alignment
  • Sodium-Potassium-Exchanging ATPase / chemistry
  • Sodium-Potassium-Exchanging ATPase / classification
  • Sodium-Potassium-Exchanging ATPase / genetics*
  • Sodium-Potassium-Exchanging ATPase / metabolism

Substances

  • Isoenzymes
  • Protein Subunits
  • H(+)-K(+)-Exchanging ATPase
  • Calcium-Transporting ATPases
  • Sodium-Potassium-Exchanging ATPase