Our Research on Proton Pumping ATPases over Three Decades: Their Biochemistry, Molecular Biology and Cell Biology

Overview

Journal Proc Jpn Acad Ser B Phys Biol Sci

Specialties Biology
Science

Date 2015 Mar 21

PMID 25792771

Citations 5

Authors

Masamitsu Futai

Affiliations

Soon will be listed here.

Abstract

ATP is synthesized by F-type proton-translocating ATPases (F-ATPases) coupled with an electrochemical proton gradient established by an electron transfer chain. This mechanism is ubiquitously found in mitochondria, chloroplasts and bacteria. Vacuolar-type ATPases (V-ATPases) are found in endomembrane organelles, including lysosomes, endosomes, synaptic vesicles, etc., of animal and plant cells. These two physiologically different proton pumps exhibit similarities in subunit assembly, catalysis and the coupling mechanism from chemistry to proton transport through subunit rotation. We mostly discuss our own studies on the two proton pumps over the last three decades, including ones on purification, kinetic analysis, rotational catalysis and the diverse roles of acidic luminal organelles. The diversity of organellar proton pumps and their stochastic fluctuation are the important concepts derived recently from our studies.

Citing Articles

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Song Q, Meng B, Xu H, Mao Z Transl Neurodegener. 2020; 9(1):17.

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Vacuolar-type ATPase: A proton pump to lysosomal trafficking.

Futai M, Sun-Wada G, Wada Y, Matsumoto N, Nakanishi-Matsui M Proc Jpn Acad Ser B Phys Biol Sci. 2019; 95(6):261-277.

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Defective Expression of Mitochondrial, Vacuolar H-ATPase and Histone Genes in a Model of SMA.

Gao X, Xu J, Chen H, Xue D, Pan W, Zhou C Front Genet. 2019; 10:410.

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Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of F-ATPase.

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