Aspects of gene structure and functional regulation of the isozymes of Na,K-ATPase.
Gaps in our understanding of the complex regulated expression of isozymes of Na,K-ATPase and the diverse systems for posttranslational modification and short term regulation of active Na,K-transport in animals and humans are the main problems in comprehensive Na,K-pump physiology. In mammalian genomes, the genes of four alpha-subunit and at least three beta-subunit isoforms of Na,K-ATPase are identified and two gamma-subunits are expressed in kidney. The isoforms combine in a number of Na,K-ATPase isozymes that are expressed in a tissue and cell specific manner. Models of the molecular mechanism of regulation of these isozymes have become more reliable due to progress in understanding the three-dimensional protein structure and conformational transitions mediating transfer of energy from the P-domain to intramembrane Na+ and K+ binding sites.
Jorgensen
P L
PL
Biomembrane Center, August Krogh Institute, Copenhagen University, Denmark. pljorgensen@aki.ku.dk
D000818:Animals; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D010766:Phosphorylation; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism
D007527:Isoenzymes; D021122:Protein Subunits; D000254:Sodium-Potassium-Exchanging ATPase