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Title: P-type ATPase diversity and evolution: the origins of ouabain sensitivity and subunit assembly. Author: Takeyasu K, Okamura H, Yasuhara JC, Ogita Y, Yoshimura SH. Journal: Cell Mol Biol (Noisy-le-grand); 2001 Mar; 47(2):325-33. PubMed ID: 11355008. 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.[Abstract] [Full Text] [Related] [New Search]