Regular ArticleFunctional Role of Oxygen-Containing Residues in the Fifth Transmembrane Segment of the Na,K-ATPase α Subunit☆,☆☆
References (37)
- et al.
J. Biol. Chem.
(1994) - et al.
J. Biol. Chem.
(1996) - et al.
FEBS Lett.
(1997) - et al.
J. Biol. Chem.
(1996) - et al.
J. Biol. Chem.
(1991) - et al.
J. Biol. Chem.
(1994) - et al.
J. Biol. Chem.
(1996) - et al.
J. Biol. Chem.
(1995) - et al.
J. Biol. Chem.
(1997) J. Biol. Chem.
(1995)
J. Biol. Chem.
J. Biol. Chem.
J. Biol. Chem.
Anal. Biochem.
Methods Enzymol.
J. Biol. Chem.
FEBS Lett.
J. Biol. Chem.
Cited by (17)
Neurological disease mutations of α3 Na<sup>+</sup>,K<sup>+</sup>-ATPase: Structural and functional perspectives and rescue of compromised function
2016, Biochimica et Biophysica Acta - BioenergeticsThe rapid-onset dystonia parkinsonism mutation D923N of the Na <sup>+</sup>,K<sup>+</sup>-ATPase α3 isoform disrupts Na<sup>+</sup> interaction at the third Na<sup>+</sup> site
2010, Journal of Biological ChemistryCitation Excerpt :In support of our hypothesis, mutation of Thr771, Ser772, and Tyr768 has led to quite significant (10- to 20-fold) reductions of the apparent Na+ affinity (38, 41, 47, 48). Importantly the effect was selective for Na+ in mutants T771A (38, 41, 48), Y768L (47), and Y768F (49), consistent with an involvement in the binding of the third Na+ ion. For mutant S772A, both Na+ and K+ affinities have been reported significantly reduced relative to wild type (48, 50, 51).
Thr-774 (transmembrane segment M5), Val-920 (M8), and Glu-954 (M9) are involved in Na<sup>+</sup> transport, and Gln-923 (M8) is essential for Na,K-ATPase activity
2005, Journal of Biological ChemistryCitation Excerpt :The data shown in Table I (compare both a and b with c and d of T774A) are consistent with the report that T774A reduced the apparent affinity for Na+, as estimated by Na+-dependent phosphorylation without affecting the affinity of Tl+ (K+) binding in a yeast expression system (37). The hydroxyl group of Tyr-771 has also been reported to be important for binding Na+ without participating in K+-enzyme interaction (42). The direct coordination of Gln-923 to the first Na+ and the first K+ without coordination from Thr-774 to any Na+ and K+ has been proposed based on homology modeling (46).
Identification of the transmembrane metal binding site in Cu <sup>+</sup>-transporting P<inf>IB</inf>-type ATPases
2004, Journal of Biological ChemistryCitation Excerpt :In the case of CopA, Asn675, Val718, and Asn721 substitutions lead to alterations compatible with the mutant enzymes being “locked” in an E1 conformation and thus largely inactive and undergoing little or none “backdoor” phosphorylation. Significant functional alterations have also been shown by previous work characterizing mutations of conserved polar amino acids located in the equivalent region of the Na,K-ATPase (58), Ca-ATPase (59, 60), and H,K-ATPase (61). Depending on the model protein and the introduced mutation, lack of activity, high activity in the absence of contra-ion (Na-ATPase), enzyme uncoupling, and reduced phosphoenzyme levels have been reported.
Electrophysiological Analysis of the Mutated Na,K-ATPase Cation Binding Pocket
2003, Journal of Biological ChemistryCitation Excerpt :The stationary current of N776Q (at -20 mV) was comparable with that of the wild-type enzyme. This is in contrast to the enzyme activity found by others, which was 7% (49) and 22% (53) of that of the wild-type activity. This discrepancy is probably due to differences in determining the enzyme activity and/or the expression system.
Site-directed mutagenesis of cation coordinating residues in the gastric H, K-ATPase
2001, Archives of Biochemistry and Biophysics
- ☆
This work was supported by National Institute of Health Grant HL28573 (J.B.L.).
- ☆☆
De Pont, J. J.
- 2
J.M.A. is a recipient of a Research Development Award for Minority Faculty, HL 03373, from the National Institute of Health.
- 3
To whom correspondence should be addressed. Fax: (508) 831-5933. E-mail:[email protected].