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Updated: Apr 11, 2026

Study of Protein-protein Interactions in Autophagy Research
Published on: September 9, 2017
Protein-protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular
Asha Manikkoth Balakrishna1, Malathy Sony Subramanian Manimekalai1, Gerhard Grüber1
1Nanyang Technological University, Division of Structural Biology and Biochemistry, School of Biological Sciences, 60 Nanyang Drive, Singapore 637551, Republic of Singapore.
Abstract:
The V1VO-ATPase (V-ATPase) is the important proton-pump in eukaryotic cells, responsible for pH-homeostasis, pH-sensing and amino acid sensing, and therefore essential for cell growths and metabolism. ATP-cleavage in the catalytic A3B3-hexamer of V1 has to be communicated via several so-called central and peripheral stalk units to the proton-pumping VO-part, which is membrane-embedded. A unique feature of V1VO-ATPase regulation is its reversible disassembly of the V1 and VO domain. Actin provides a network to hold the V1 in proximity to the VO, enabling effective V1VO-assembly to occur. Besides binding to actin, the 14-subunit V-ATPase interacts with multi-subunit machineries to form cellular sensors, which regulate the pH in cellular compartments or amino acid signaling in lysosomes. Here we describe a variety of subunit-subunit interactions within the V-ATPase enzyme during catalysis and its protein-protein assembling with key cellular machineries, essential for cellular function.
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