P-type ATPase diversity and evolution: the origins of ouabain sensitivity and subunit assembly
K Takeyasu1, H Okamura, J C Yasuhara
1Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies, Japan. takeyasu@lif.kyoto-u.ac.jp
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.
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