Protein-protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular machineries

Asha Manikkoth Balakrishna; Malathy Sony Subramanian Manimekalai; Gerhard Grüber

doi:10.1016/j.pbiomolbio.2015.05.003

Protein-protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular machineries

Asha Manikkoth Balakrishna, Malathy Sony Subramanian Manimekalai, Gerhard Grüber^*

^*Corresponding author for this work

Nanyang Technological University

Research output: Contribution to journal › Review article › peer-review

2 Citations (Scopus)

Abstract

The V₁V_O-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 V_O-part, which is membrane-embedded.A unique feature of V₁V_O-ATPase regulation is its reversible disassembly of the V₁ and V_O domain. Actin provides a network to hold the V₁ in proximity to the V_O, enabling effective V₁V_O-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.

Original language	English
Pages (from-to)	84-93
Number of pages	10
Journal	Progress in Biophysics and Molecular Biology
Volume	119
Issue number	1
DOIs	https://doi.org/10.1016/j.pbiomolbio.2015.05.003
Publication status	Published - Oct 1 2015
Externally published	Yes

Bibliographical note

Publisher Copyright:
© 2015 Elsevier Ltd.

ASJC Scopus Subject Areas

Biophysics
Molecular Biology

Keywords

Bioenergetics
Coupling
Molecular engine
Saccharomyces cerevisiae
Structural biology
V-ATPase
Vacuolar ATPase

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10.1016/j.pbiomolbio.2015.05.003

Cite this

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title = "Protein-protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular machineries",

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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doi = "10.1016/j.pbiomolbio.2015.05.003",

language = "English",

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Protein-protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular machineries. / Balakrishna, Asha Manikkoth; Manimekalai, Malathy Sony Subramanian; Grüber, Gerhard.
In: Progress in Biophysics and Molecular Biology, Vol. 119, No. 1, 01.10.2015, p. 84-93.

Research output: Contribution to journal › Review article › peer-review

TY - JOUR

T1 - Protein-protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular machineries

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AU - Manimekalai, Malathy Sony Subramanian

AU - Grüber, Gerhard

PY - 2015/10/1

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N2 - 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.

AB - 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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KW - Saccharomyces cerevisiae

KW - Structural biology

KW - V-ATPase

KW - Vacuolar ATPase

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Protein-protein interactions within the ensemble, eukaryotic V-ATPase, and its concerted interactions with cellular machineries

Abstract

Bibliographical note

ASJC Scopus Subject Areas

Keywords

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