P-type ATPase diversity and evolution: the origins of ouabain sensitivity and subunit assembly.
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.
Takeyasu
K
K
Laboratory of Plasma Membrane and Nuclear Signaling, Kyoto University Graduate School of Biostudies, Japan. takeyasu@lif.kyoto-u.ac.jp
Okamura
H
H
Yasuhara
J C
JC
Ogita
Y
Y
Yoshimura
S H
SH
D000595:Amino Acid Sequence; D000818:Animals; D000252:Calcium-Transporting ATPases / Q000737:chemistry / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D020134:Catalytic Domain; D019143:Evolution, Molecular; D017506:H(+)-K(+)-Exchanging ATPase / Q000737:chemistry / Q000145:classification / Q000235:genetics* / Q000378:metabolism; D006801:Humans; D007527:Isoenzymes / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D021122:Protein Subunits; D016415:Sequence Alignment; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000145:classification / Q000235:genetics* / Q000378:metabolism
D007527:Isoenzymes; D021122:Protein Subunits; D017506:H(+)-K(+)-Exchanging ATPase; D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase