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Function and Regulation of Mammalian V-ATPase Isoforms

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Book cover Regulation of Ca2+-ATPases,V-ATPases and F-ATPases

Part of the book series: Advances in Biochemistry in Health and Disease ((ABHD,volume 14))

Abstract

The vacuolar (H+)-ATPases (V-ATPase) are a family of highly conserved multisubunit ATP-driven nanomotors, responsible for the acidification of a variety of intracellular compartments in eukaryotic cells. Vacuolar (H+)-ATPases are important in both normal physiology and in pathophysiology. These complicated and huge enzymes consist of at least 14 subunits divided into two domains (membrane-bound Vo and cytosolic V1). The peripheral stalk subunits of eukaryotic or mammalian vacuolar ATPases (V-ATPases) play key roles in regulating the assembly and disassembly of the enzyme. Interestingly, many of the peripheral stalk subunits also possess several homologues, which are known to be tissue-specific and are responsible for the formation of proton pumps with specialized functions within different tissues. Such tissue-specific isoforms/homologues and splice variants cannot complement each other, meaning that tissue/cell-specific regulation of V-ATPases is difficult to understand. In order to understand the structure/function and isoform-specific regulation mechanism of the human V-ATPase, several of the peripheral stalk subunits and their isoforms were expressed and characterized. In this review, we will discuss the binding interaction phenomena specifically at the stalk region, which mediates the reversible assembly and disassembly of V-ATPase in eukaryotic/mammalian cell systems.

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Authors and Affiliations

  1. Department of Biological Science and Technology, Tokyo University of Science, 6-3-1 Niijuku, Katsushika-ku, Tokyo, 125-8585, Japan

    Suhaila Rahman & Ichiro Yamato

  2. Department of Chemistry, Graduate School of Science, Chiba University, 1-33 Yayoi-cho, Inage, Chiba, 263-8522, Japan

    Takeshi Murata

  3. RIKEN Systems and Structural Biology Center, 1-7-22 Suehiro-cho, Tsurumi, Yokohama, 230-0045, Japan

    Takeshi Murata

  4. JST, PRESTO, 1-33 Yayoi-cho, Inage, Chiba, 263-8522, Japan

    Takeshi Murata

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  1. Suhaila Rahman
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  2. Ichiro Yamato
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Correspondence to Ichiro Yamato .

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Editors and Affiliations

  1. Biochemistry and Biophysics, University of Kalyani, Kalyani, West Bengal, India

    Sajal Chakraborti

  2. University of Manitoba, Institute of Cardiovascular Science St. Boniface Hospital Research, Winnipeg, Manitoba, Canada

    Naranjan S Dhalla

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Rahman, S., Yamato, I., Murata, T. (2016). Function and Regulation of Mammalian V-ATPase Isoforms. In: Chakraborti, S., Dhalla, N. (eds) Regulation of Ca2+-ATPases,V-ATPases and F-ATPases. Advances in Biochemistry in Health and Disease, vol 14. Springer, Cham. https://doi.org/10.1007/978-3-319-24780-9_15

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