Biochemistry of Na,K-ATPase

被引:895
作者
Kaplan, JH [1 ]
机构
[1] Oregon Hlth & Sci Univ, Dept Biochem & Mol Biol, Portland, OR 97201 USA
关键词
sodium pump; structure-function; active transport; P-type ATPases;
D O I
10.1146/annurev.biochem.71.102201.141218
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Na,K-ATPase or sodium pump carries out the coupled extrusion and uptake of Na and K ions across the plasma membranes of cells of most higher eukaryotes. It is a member of the P-type ATPase superfamily. This heterodimeric integral membrane protein is composed of a 100-kDa alpha-subunit with ten transmembrane segments and a heavily glycosylated beta subunit of about 55 kDa, which is a type II membrane protein. Current ideas on how the protein achieves active transport are based on a fusion of results of transport physiology, protein chemistry, and heterologous expression of mutant proteins. Recently acquired high resolution structural information provides an important new avenue for a more complete understanding of this protein. In this review, the current status of knowledge of Na,K-ATPase is discussed, and areas where there is still considerable uncertainty are highlighted.
引用
收藏
页码:511 / 535
页数:25
相关论文
共 121 条
[1]   MUTUAL DEPENDENCE OF NA,K-ATPASE ALPHA-SUBUNITS AND BETA-SUBUNITS FOR CORRECT POSTTRANSLATIONAL PROCESSING AND INTRACELLULAR-TRANSPORT [J].
ACKERMANN, U ;
GEERING, K .
FEBS LETTERS, 1990, 269 (01) :105-108
[2]   Dissection of the functional domains of the sarcoplasmic reticulum Ca2+-ATPase by site-directed mutagenesis [J].
Andersen, JP .
BIOSCIENCE REPORTS, 1995, 15 (05) :243-261
[3]   Affinity labelling with MgATP analogues reveals coexisting Na+ and K+ forms of the α-subunits of Na+/K+-ATPase [J].
Antolovic, R ;
Hamer, E ;
Serpersu, EH ;
Kost, H ;
Linnertz, H ;
Kovarik, Z ;
Schoner, W .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1999, 261 (01) :181-189
[4]  
ARGUELLO JM, 1991, J BIOL CHEM, V266, P14627
[5]   Alanine scanning mutagenesis of oxygen-containing amino acids in the transmembrane region of the Na,K-ATPase [J].
Argüello, JM ;
Whitis, J ;
Lingrel, JB .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 367 (02) :341-347
[6]  
ARGUELLO JM, 1994, J BIOL CHEM, V269, P6892
[7]   Evolution of substrate specificities in the P-type ATPase superfamily [J].
Axelsen, KB ;
Palmgren, MG .
JOURNAL OF MOLECULAR EVOLUTION, 1998, 46 (01) :84-101
[8]  
AXELSEN KB, 2001, P TYPE ATPASE DATAB
[9]   Electrogenic properties of the Na+,K+-ATPase probed by presteady state and relaxation studies [J].
Bamberg, E ;
Clarke, RJ ;
Fendler, K .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 2001, 33 (05) :401-405
[10]  
Beggah AT, 1997, J BIOL CHEM, V272, P10318