Work

Displacement of the Na + /K + pump’s transmembrane domains demonstrates conserved conformational changes in P-type 2 ATPases

Year: 2021

Type: article

Abstract: Significance The P-type 2 ATPase subfamily includes several essential primary active ion transporters like the Na + /K + , H + /K + , and SERCA pumps. These transporters are thought to act by a conserved mechanism. However, major conformational changes seen in the transmembrane domains in crystal structures of SERCA and also proposed to occur in H + /K + pumps are absent in available Na + /K + -pump structures. Here we use cross-linking of engineered cysteines and voltage clamp fluorometry (VCF) to show that the movements of transmembrane segments conserved in other pumps, which are absent in Na + /K + pump crystal structures, occur in functional Na + /K + pumps. In addition, we illustrate a twist to the usual VCF approach that may help in future studies using this technique with other membrane proteins.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.2019317118

Authors: Victoria C. Young, Pablo Artigas

Institutions: Texas Tech University, Texas Tech University Health Sciences Center

Language: English

Topic: ATP Synthase and ATPases Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Science Foundation, American Heart Association, CH Foundation, National Institute of Neurological Disorders and Stroke

Awards: Ion-selectivity and mechanisms of the Na/K pump, Physiologically relevant energetic interactions within the Na/K Pump, G7638173934