July 28, 2025Open Access

Active Conformations of Neuronal Na+,K+-ATPase isoforms and a Disease-Causing Mutant

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Cryo-EM reveals distinct conformational states in Na+,K+-ATPase isoforms, suggesting new insights into ion transport and a disease-causing mutant.

Na+,K+-ATPases maintain essential Na+ and K+ gradients across cell membranes, crucial for neuronal function.
Cryo-EM structures expose four active conformational states, including a significant sodium-bound phosphoenzyme intermediate.
The α3 isoform shows higher Na+ affinity than α1, influencing the transport mechanism of sodium ions.
A disease causing mutant α3 (Q140L), linked to alternating hemiplegia, alters lipid binding, affecting enzyme activity.

Christensen et al. (2025) studied this question.

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Cryo-EM reveals distinct conformational states in Na+,K+-ATPase isoforms, suggesting new insights into ion transport and a disease-causing mutant.