Ligand‐Induced Conformational Changes in the Na,K‐ATPase α Subunit<sup>a</sup>

Kaplan, Jack H.; Lutsenko, Svetlana; Gatto, Craig; Daoud, Sylvia; Kenney, Linda J.

doi:10.1111/j.1749-6632.1997.tb52224.x

Cited by 6 publications

(3 citation statements)

References 24 publications

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“…The most important difference with earlier results [13]lies in the fact that our construct gives rise to a soluble protein which does not have to undergo any denaturation‐refolding procedures. As far as the Na,K‐ATPase is concerned, Kaplan and co‐workers [16]have also reported recently the expression of a similar construct.…”

Section: Discussionmentioning

confidence: 98%

The isolated H₄‐H₅ cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP

et al. 1998

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The H R -H S loop of the K K-subunit of mouse brain Na,K-ATPase was expressed and isolated from Escherichia coli cells. Using fluorescence analogues of ATP, this loop was shown to retain its capability to bind ATP. Isolation of a soluble H R -H S loop with the native ATP binding site is a crucial step for detailed studies of the molecular mechanism of ATP binding and utilisation.z 1998 Federation of European Biochemical Societies.

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Section: Discussionmentioning

confidence: 98%

The isolated H₄‐H₅ cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP

et al. 1998

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“…We reported previously that this GST-M4M5 loop was able to bind ATP as determined via protection against FITC labeling (37). More recently, the corresponding domain in the full-length rabbit fast twitch SERCA has been shown to coordinate TNP-AMP binding by x-ray crystallographic analysis (8).…”

Section: Resultsmentioning

confidence: 99%

Interactions between Na,K-ATPase α-Subunit ATP-binding Domains

Costa¹,

Gatto²,

Kaplan³

2003

Journal of Biological Chemistry

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The reaction mechanism of the Na,K-ATPase is thought to involve a number of ligand-induced conformational changes. The specific amino acid residues responsible for binding many of the important ligands have been identified; however, details of the specific conformational changes produced by ligand binding are largely undescribed. The experiments described in this paper begin to identify interactions between domains of the Na,K-ATPase ␣-subunit that depend on the presence of particular ligands. The major cytoplasmic loop (between TM4 and TM5), which we have previously shown contains the ATP-binding domain, was overexpressed in bacteria either with a His 6 tag or as a fusion protein with glutathione S-transferase. We have observed that these polypeptides associate in the presence of MgATP. Incubation with [␥-32 P]ATP under conditions that result in phosphorylation of the full-length Na,K-ATPase did not result in 32 P incorporation into either the His 6 tag or glutathione S-transferase fusion proteins. The MgATPinduced association was strongly inhibited by prior modification of the fusion proteins with fluorescein isothiocyanate or by simultaneous incubation with 10 M eosin, indicating that the effect of MgATP is due to interactions within the nucleotide-binding domain. These data are consistent with Na,K-ATPase associating within cells via interactions in the nucleotide-binding domains. Although any functional significance of these associations for ion transport remains unresolved, they may play a role in cell function and in modulating interactions between the Na,K-ATPase and other proteins.

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“…Recent functional studies of P-type ATPases have focused on two major activities, the transmembrane transport of cations and the hydrolysis of ATP via a phosphoenzyme intermediate, which appear to be carried out by the actions of two separate protein domains, the intramembrane domain that binds cations and the major cytoplasmic loop responsible for ATP binding and hydrolysis (1,2). P-type ATPases can be classified into two subgroups based upon their function and structure (3).…”

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Stabilization of the H,K-ATPase M5M6 Membrane Hairpin by K+ Ions

Gatto¹,

Lutsenko²,

Shin³

et al. 1999

Journal of Biological Chemistry

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The integral membrane protein, the gastric H,KATPase, is an ␣-␤ heterodimer, with 10 putative transmembrane segments in the ␣-subunit and one such segment in the ␤-subunit. Recent functional studies of P-type ATPases have focused on two major activities, the transmembrane transport of cations and the hydrolysis of ATP via a phosphoenzyme intermediate, which appear to be carried out by the actions of two separate protein domains, the intramembrane domain that binds cations and the major cytoplasmic loop responsible for ATP binding and hydrolysis (1, 2).

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Ligand‐Induced Conformational Changes in the Na,K‐ATPase α Subunit^a

Cited by 6 publications

References 24 publications

The isolated H₄‐H₅ cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP

The isolated H₄‐H₅ cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP

Interactions between Na,K-ATPase α-Subunit ATP-binding Domains

Stabilization of the H,K-ATPase M5M6 Membrane Hairpin by K+ Ions

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Ligand‐Induced Conformational Changes in the Na,K‐ATPase α Subunita

Cited by 6 publications

References 24 publications

The isolated H4‐H5 cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP

The isolated H4‐H5 cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP

Interactions between Na,K-ATPase α-Subunit ATP-binding Domains

Stabilization of the H,K-ATPase M5M6 Membrane Hairpin by K+ Ions

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Ligand‐Induced Conformational Changes in the Na,K‐ATPase α Subunit^a

The isolated H₄‐H₅ cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP

The isolated H₄‐H₅ cytoplasmic loop of Na,K‐ATPase overexpressed in Escherichia coli retains its ability to bind ATP