Na+/K+-ATPase - Sodium/Potassium-Exchanging ATPase

Family:
P-type ATPase (P-ATPase) Superfamily

Subgroups and Members:
P-type ATPases can be divided into five subfamilies (types)
Type I consists of the transition/heavy metal ATPases.
Type II ATPases (specific for Na⁺,K⁺, H⁺ Ca²⁺, Mg²⁺ and phospholipids) predominate in eukaryotes. SERCA and  Na⁺/K⁺ ATPases are member of this group.
There are 3 major paralogs, SERCA1-3, which are expressed at various levels in different cell types: SERCA1 - SERCA3, encoded by the genes  ATP2A1 - ATP2A3.
Type III ATPases contains the plasma membrane H⁺-ATPases from plants and fungi.
Type IV ATPases have been shown to be involved in the transport of phospholipids
Type V ATPases have unknown specificity.

Topology:
Many of these protein complexes are multisubunit with a large subunit serving the primary ATPase and ion translocation functions. Many eukaryotic P-type ATPases are monomeric or homodimeric enzymes of the catalytic subunit that hydrolyzes ATP. They contain the aspartyl phosphorylation site and catalyzes ion transport. The Na+/K+-ATPases, the Ca²⁺-ATPases and the (fungal) H⁺-ATPases of higher organisms exhibit 10 transmembrane α helical spanners (TMSs).

Function:
P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation of a key conserved aspartate residue within the pump and their energy source, adenosine triphosphate (ATP). Most members of this transporter superfamily catalyze cation uptake and/or efflux, however one subfamily is involved in flipping phospholipids to maintain the asymmetric nature of the biomembrane.

Data and Applications

Sodium-Potassium ATPase - Analysis

  SURFE²R N1 data and applications:

The Sodium-Potassium ATPase, also known as Na⁺/K⁺ pump is responsible for the active transport of Na⁺ and K⁺ in the cells containing relatively high concentrations of K⁺ ions but low concentrations of Na⁺ ions. The Na⁺/K⁺-ATPase helps maintain resting potential, avail transport, and regulate cellular volume. Here, we demonstrate the conductance of the pump, in the presence of ATP, Na⁺ and K⁺, or in the presence of ATP and Na⁺.

Posters

2018 - A Sensor Based Technique for Pharmacological Safety Testing of Cardiac Transport Proteins NCX, NaKATPase and Respiratory Chain Complexes

   CardioExcyte 96 and      SUFE²R 96SE poster, SPS 2018     (1.7 MB)

preview the file here for download

2017 - An emerging technique for the characterization of transport proteins: SSM-based electrophysiology

  SURFE²R N1 and      SURFE²R SE96 poster, 19th IUPAB / 11th EBSA congress 2017     (3.3 MB)

preview the file here for download