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Na,K-ATPase α-subunit conformation determines glutathionylation efficiency
Yuri M Poluektov1, Elena A Dergousova2, Olga D Lopina2
1Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov St. 32, 119991, Moscow, Russia; I.M. Sechenov First Moscow State Medical University, Ministry of Healthcare of the Russian Federation, Trubetskaya St. 8/2, 119991, Moscow, Russia.
Biochemical and Biophysical Research Communications
|January 22, 2019
Summary
The Na,K-ATPase enzyme
Area of Science:
- Biochemistry
- Cellular Physiology
- Molecular Biology
Background:
- The Na,K-ATPase is crucial for cellular function and its activity is redox-sensitive.
- Oxidative stress and hypoxia inhibit Na,K-ATPase activity via glutathionylation of its α-subunit.
- The impact of Na,K-ATPase conformation on glutathionylation remains unclear.
Purpose of the Study:
- To investigate how Na,K-ATPase conformation influences α-subunit glutathionylation.
- To determine which enzyme conformations are most susceptible to glutathionylation.
Main Methods:
- Utilized molecular modeling to analyze cysteine residue accessibility in different Na,K-ATPase conformations.
- Examined the relationship between enzyme conformation (E1 vs. E2 states) and glutathionylation efficiency.
Main Results:
- Glutathionylation of the Na,K-ATPase α-subunit is highest in the E1 (Na+-induced) conformation.
- Transition to E2 (K+-induced) conformations, particularly E2P and E2P ouabain states, decreases glutathionylation efficiency.
- Molecular modeling indicates cysteine residues are more accessible in the E1P conformation than in E2P.
Conclusions:
- Enzyme conformation, dictated by ligand binding, significantly affects Na,K-ATPase α-subunit glutathionylation.
- A conformational shift favoring the E1 state enhances accessibility for glutathionylation.
- Understanding this conformational dependence is key to Na,K-ATPase regulation under cellular stress.
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