» Articles » PMID: 20511227

Regulation of Vacuolar Proton-translocating ATPase Activity and Assembly by Extracellular PH

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2010 Jun 1
PMID 20511227
Citations 40
Authors
Affiliations
Soon will be listed here.
Abstract

Vacuolar proton-translocating ATPases (V-ATPases) are responsible for organelle acidification in all eukaryotic cells. The yeast V-ATPase, known to be regulated by reversible disassembly in response to glucose deprivation, was recently reported to be regulated by extracellular pH as well (Padilla-López, S., and Pearce, D. A. (2006) J. Biol. Chem. 281, 10273-10280). Consistent with those results, we find 57% higher V-ATPase activity in vacuoles isolated after cell growth at extracellular pH of 7 than after growth at pH 5 in minimal medium. Remarkably, under these conditions, the V-ATPase also becomes largely insensitive to reversible disassembly, maintaining a low vacuolar pH and high levels of V(1) subunit assembly, ATPase activity, and proton pumping during glucose deprivation. Cytosolic pH is constant under these conditions, indicating that the lack of reversible disassembly is not a response to altered cytosolic pH. We propose that when alternative mechanisms of vacuolar acidification are not available, maintaining V-ATPase activity becomes a priority, and the pump is not down-regulated in response to energy limitation. These results also suggest that integrated pH and metabolic inputs determine the final assembly state and activity of the V-ATPase.

Citing Articles

Human V-ATPase function is positively and negatively regulated by TLDc proteins.

Oot R, Wilkens S Structure. 2024; 32(7):989-1000.e6.

PMID: 38593795 PMC: 11246223. DOI: 10.1016/j.str.2024.03.009.


Molecular mechanism of Oxr1p mediated disassembly of yeast V-ATPase.

Khan M, Wilkens S EMBO Rep. 2024; 25(5):2323-2347.

PMID: 38565737 PMC: 11094088. DOI: 10.1038/s44319-024-00126-5.


Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.

Wilkens S, Khan M, Knight K, Oot R Bioessays. 2023; 45(7):e2200251.

PMID: 37183929 PMC: 10392918. DOI: 10.1002/bies.202200251.


Chimeric a-subunit isoforms generate functional yeast V-ATPases with altered regulatory properties in vitro and in vivo.

Tuli F, Kane P Mol Biol Cell. 2023; 34(3):ar14.

PMID: 36598799 PMC: 10011726. DOI: 10.1091/mbc.E22-07-0265.


Coordinated conformational changes in the V complex during V-ATPase reversible dissociation.

Vasanthakumar T, Keon K, Bueler S, Jaskolka M, Rubinstein J Nat Struct Mol Biol. 2022; 29(5):430-439.

PMID: 35469063 DOI: 10.1038/s41594-022-00757-z.


References
1.
Perzov N, Nelson H, Nelson N . Altered distribution of the yeast plasma membrane H+-ATPase as a feature of vacuolar H+-ATPase null mutants. J Biol Chem. 2000; 275(51):40088-95. DOI: 10.1074/jbc.M007011200. View

2.
Ali R, Brett C, Mukherjee S, Rao R . Inhibition of sodium/proton exchange by a Rab-GTPase-activating protein regulates endosomal traffic in yeast. J Biol Chem. 2003; 279(6):4498-506. DOI: 10.1074/jbc.M307446200. View

3.
Smardon A, Tarsio M, Kane P . The RAVE complex is essential for stable assembly of the yeast V-ATPase. J Biol Chem. 2002; 277(16):13831-9. DOI: 10.1074/jbc.M200682200. View

4.
Serrano R, Bernal D, Simon E, Arino J . Copper and iron are the limiting factors for growth of the yeast Saccharomyces cerevisiae in an alkaline environment. J Biol Chem. 2004; 279(19):19698-704. DOI: 10.1074/jbc.M313746200. View

5.
Uchida E, Ohsumi Y, Anraku Y . Purification and properties of H+-translocating, Mg2+-adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J Biol Chem. 1985; 260(2):1090-5. View