The sodium pump

The sodium pump (Na+/K+-ATPase; sodium- and potassium-activated adenosine 5′-triphosphatase; EC 3.6.1.37) has been under investigation for more than four decades. During this time, the knowledge about the structure and properties of the enzyme has increased to such an extent that specialized groups have formed within this field that focus on specific aspects of the active ion transport catalyzed by this enzyme. Taking this into account, this review, while somewhat speculative, is an attempt to summarize the information regarding the enzymology of the sodium pump with the hope of providing to interested readers from outside the field a concentrated overview and to readers from related fields a guide in their search for gathering specific information concerning the structure, function, and enzymology of this enzyme.

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[2]  Zijian Xie,et al.  Na(+)/K(+)-ATPase as a signal transducer. , 2002, European journal of biochemistry.

[3]  K. Geering,et al.  Structural and Functional Features of the Transmembrane Domain of the Na,K-ATPase β Subunit Revealed by Tryptophan Scanning* , 2001, The Journal of Biological Chemistry.

[4]  P. A. Pedersen,et al.  Structure–function relationships of Na+, K+, ATP, or Mg2+ binding and energy transduction in Na,K-ATPase , 2001 .

[5]  K. Sweadner,et al.  Thermal Denaturation of the Na,K-ATPase Provides Evidence for α-α Oligomeric Interaction and γ Subunit Association with the C-terminal Domain* , 2001, The Journal of Biological Chemistry.

[6]  K. Abe,et al.  The oligomeric nature of Na/K-transport ATPase. , 2001, Journal of biochemistry.

[7]  G. Scheiner-Bobis,et al.  A Hybrid between Na+,K+-ATPase and H+,K+-ATPase Is Sensitive to Palytoxin, Ouabain, and SCH 28080* , 2001, The Journal of Biological Chemistry.

[8]  G. Scheiner-Bobis Sanguinarine induces K+ outflow from yeast cells expressing mammalian sodium pumps , 2001, Naunyn-Schmiedeberg's Archives of Pharmacology.

[9]  H. Vorum,et al.  Identification of a Phospholemman-like Protein from Shark Rectal Glands , 2000, The Journal of Biological Chemistry.

[10]  S. Karlish,et al.  The complex ATP–Fe2+ serves as a specific affinity cleavage reagent in ATP-Mg2+ sites of Na,K-ATPase: Altered ligation of Fe2+ (Mg2+) ions accompanies the E1P→E2P conformational change , 2000 .

[11]  A. Askari,et al.  Involvement of Src and epidermal growth factor receptor in the signal-transducing function of Na+/K+-ATPase. , 2000, The Journal of biological chemistry.

[12]  M. Nakasako,et al.  Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution , 2000, Nature.

[13]  D. Martin,et al.  Alphabeta protomers of Na+,K+-ATPase from microsomes of duck salt gland are mostly monomeric: formation of higher oligomers does not modify molecular activity. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[14]  H. Guy,et al.  Does the KdpA subunit from the high affinity K(+)-translocating P-type KDP-ATPase have a structure similar to that of K(+) channels? , 2000, Biophysical journal.

[15]  K. Sweadner,et al.  The γ Subunit Modulates Na+ and K+Affinity of the Renal Na,K-ATPase* , 1999, The Journal of Biological Chemistry.

[16]  G. Scheiner-Bobis,et al.  Glutamic acid 472 and lysine 480 of the sodium pump alpha 1 subunit are essential for activity. Their conservation in pyrophosphatases suggests their involvement in recognition of ATP phosphates. , 1999, Biochemistry.

[17]  A. Therien,et al.  Expression and Functional Role of the γ Subunit of the Na,K-ATPase in Mammalian Cells* , 1999, The Journal of Biological Chemistry.

[18]  M. Shimon,et al.  Specific Cu2+-catalyzed Oxidative Cleavage of Na,K-ATPase at the Extracellular Surface* , 1998, The Journal of Biological Chemistry.

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[20]  K. Geering,et al.  The γ subunit is a specific component of the Na,K‐ATPase and modulates its transport function , 1997, The EMBO journal.

[21]  H. Schneider,et al.  Involvement of the M7/M8 extracellular loop of the sodium pump alpha subunit in ion transport. Structural and functional homology to P-loops of ion channels. , 1997, The Journal of biological chemistry.

[22]  D. Fambrough,et al.  Subunit Interactions in the Na,K-ATPase Explored with the Yeast Two-hybrid System* , 1997, The Journal of Biological Chemistry.

[23]  J. Kaplan,et al.  Chemical modification with dihydro-4,4'-diisothiocyanostilbene-2,2'-disulfonate reveals the distance between K480 and K501 in the ATP-binding domain of the Na,K-ATPase. , 1997, Archives of biochemistry and biophysics.

[24]  C. Wu,et al.  Palytoxin-induced single-channel currents from the sodium pump synthesized by in vitro expression. , 1997, Toxicon : official journal of the International Society on Toxinology.

[25]  N. Davidson,et al.  A regenerative link in the ionic fluxes through the weaver potassium channel underlies the pathophysiology of the mutation. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[26]  D. Maclennan,et al.  Scanning Mutagenesis Reveals a Similar Pattern of Mutation Sensitivity in Transmembrane Sequences M4, M5, and M6, but Not in M8, of the Ca2+-ATPase of Sarcoplasmic Reticulum (SERCA1a)* , 1996, The Journal of Biological Chemistry.

[27]  J. Lingrel,et al.  Asp804 and Asp808 in the Transmembrane Domain of the Na,K-ATPase α Subunit Are Cation Coordinating Residues* , 1996, The Journal of Biological Chemistry.

[28]  J. Lingrel,et al.  Ouabain Interactions with the H5-H6 Hairpin of the Na,K-ATPase Reveal a Possible Inhibition Mechanism via the Cation Binding Domain* , 1996, The Journal of Biological Chemistry.

[29]  J. Kaplan,et al.  Organization of P-type ATPases: significance of structural diversity. , 1995, Biochemistry.

[30]  R. Farley,et al.  The influence of beta subunit structure on the interaction of Na+/K(+)-ATPase complexes with Na+. A chimeric beta subunit reduces the Na+ dependence of phosphoenzyme formation from ATP. , 1995, The Journal of biological chemistry.

[31]  B. Vilsen Mutant Glu781-->Ala of the rat kidney Na+,K(+)-ATPase displays low cation affinity and catalyzes ATP hydrolysis at a high rate in the absence of potassium ions. , 1995, Biochemistry.

[32]  G. Scheiner-Bobis,et al.  Subunit requirements for expression of functional sodium pumps in yeast cells. , 1994, Biochimica et biophysica acta.

[33]  M. Christ,et al.  Palytoxin induces K+ efflux from yeast cells expressing the mammalian sodium pump. , 1994, Molecular pharmacology.

[34]  G. Scheiner-Bobis,et al.  Identification of an amino acid in the ATP binding site of Na+/K(+)-ATPase after photochemical labeling with 8-azido-ATP. , 1994, Biochemistry.

[35]  A. Shainskaya,et al.  Evidence that the cation occlusion domain of Na/K-ATPase consists of a complex of membrane-spanning segments. Analysis of limit membrane-embedded tryptic fragments. , 1994, The Journal of biological chemistry.

[36]  K. Takeyasu,et al.  26 amino acids of an extracellular domain of the Na,K-ATPase alpha-subunit are sufficient for assembly with the Na,K-ATPase beta-subunit. , 1994, The Journal of biological chemistry.

[37]  R. Farley,et al.  Photochemical labeling and inhibition of Na,K-ATPase by 2-Azido-ATP. Identification of an amino acid located within the ATP binding site. , 1994, The Journal of biological chemistry.

[38]  J. Lingrel,et al.  Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains. , 1993, Biochemistry.

[39]  B. Vilsen Glutamate 329 located in the fourth transmembrane segment of the alpha-subunit of the rat kidney Na+,K+-ATPase is not an essential residue for active transport of sodium and potassium ions. , 1993, Biochemistry.

[40]  J. Kaplan,et al.  An essential role for the extracellular domain of the Na,K-ATPase beta-subunit in cation occlusion. , 1993, Biochemistry.

[41]  D. Ward,et al.  Solubilized alpha beta Na,K-ATPase remains protomeric during turnover yet shows apparent negative cooperativity toward ATP. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[42]  I. Glynn,et al.  Annual review prize lecture. ‘All hands to the sodium pump’. , 1993, The Journal of physiology.

[43]  J. Lingrel,et al.  Site-directed mutagenesis of a predicted cation binding site of Na, K-ATPase. , 1993, Biochemistry.

[44]  K. Altendorf,et al.  The KDP ATPase of Escherichia coli a , 1992 .

[45]  M. Schachner,et al.  The adhesion molecule on glia (AMOG/beta 2) and alpha 1 subunits assemble to functional sodium pumps in Xenopus oocytes. , 1992, The Journal of biological chemistry.

[46]  D. Linder,et al.  Epitope mapping by amino-acid-sequence-specific antibodies reveals that both ends of the alpha subunit of Na+/K(+)-ATPase are located on the cytoplasmic side of the membrane. , 1991, European journal of biochemistry.

[47]  K. Geering Posttranslational modifications and intracellular transport of sodium pumps: importance of subunit assembly. , 1991, Society of General Physiologists series.

[48]  T. Kirley,et al.  Lysine 480 is an essential residue in the putative ATP site of lamb kidney (Na,K)-ATPase. Identification of the pyridoxal 5'-diphospho-5'-adenosine and pyridoxal phosphate reactive residue. , 1990, The Journal of biological chemistry.

[49]  Two-dimensional crystalline arrays of Na,K-ATPase with new subunit interactions induced by cobalt-tetrammine-ATP. , 1989, Journal of ultrastructure and molecular structure research.

[50]  E. Habermann Palytoxin acts through Na+,K+-ATPase. , 1989, Toxicon : official journal of the International Society on Toxinology.

[51]  P. L. Jørgensen,et al.  Occlusion of 22Na+ and 86Rb+ in membrane-bound and soluble protomeric alpha beta-units of Na,K-ATPase. , 1987, Progress in clinical and biological research.

[52]  J. Skou,et al.  [1] Overview: The Na,K-pump , 1988 .

[53]  Y. Ovchinnikov,et al.  Affinity modification of E1‐form of Na+, K+ ‐ATPase revealed Asp‐710 in the catalytic site , 1987, FEBS letters.

[54]  J. A. Dani,et al.  An introduction to molecular architecture and permeability of ion channels. , 1987, Annual Review of Biophysics and Biophysical Chemistry.

[55]  M. Yoshida,et al.  The active site structure of Na+/K+-transporting ATPase: location of the 5'-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides released by trypsin. , 1986, Proceedings of the National Academy of Sciences of the United States of America.

[56]  K. Geering,et al.  Membrane insertion of alpha- and beta-subunits of Na+,K+-ATPase. , 1985, The Journal of biological chemistry.

[57]  D. Hawke,et al.  The amino acid sequence of a fluorescein-labeled peptide from the active site of (Na,K)-ATPase. , 1984, The Journal of biological chemistry.

[58]  W. Huang,et al.  Na+, K+-ATPase: evidence for the binding of ATP to the phosphoenzyme. , 1982, Biochemical and biophysical research communications.

[59]  I. Plesner,et al.  The steady-state kinetic mechanism of ATP hydrolysis catalyzed by membrane-bound (Na+ + K+)-ATPase from ox brain. III. A minimal model. , 1981, Biochimica et biophysica acta.

[60]  K. Repke,et al.  Flip-flop model of (NaK)-ATPase function. , 1973, Acta biologica et medica Germanica.

[61]  A. K. Sen,et al.  (K+)-dependent acyl phosphatase as part of the (na+ + K+)-dependent ATPase of cell membranes. , 1966, Biochimica et biophysica acta.

[62]  J C SKOU,et al.  The influence of some cations on an adenosine triphosphatase from peripheral nerves. , 1957, Biochimica et biophysica acta.