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Literature DB >> 10600679

Luminal acidification of diverse organelles by V-ATPase in animal cells.

M Futai¹, T Oka, G Sun-Wada, Y Moriyama, H Kanazawa, Y Wada.

Abstract

Eukaryotic cells contain organelles bounded by a single membrane in the cytoplasm. These organelles have differentiated to carry out various functions in the pathways of endocytosis and exocytosis. Their lumina are acidic, with pH ranging from 4.5 to 6.5. This article describes recent studies on these animal cell organelles focusing on (1) the primary proton pump (vacuolar-type H(+)-ATPase) and (2) the functions of the organelle luminal acidity. We also discuss similarities and differences between vacuolar-type H(+)-ATPase and F-type ATPase. Our own studies and interests are emphasized.

Entities: Chemical

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Year: 2000 PMID： 10600679 DOI： 10.1242/jeb.203.1.107

Source DB: PubMed Journal: J Exp Biol ISSN： 0022-0949 Impact factor: 3.312

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Cited

24 in total

1. Regulation of organelle acidity.

Authors: M Grabe; G Oster
Journal: J Gen Physiol Date: 2001-04 Impact factor: 4.086

2. V-ATPase V1 sector is required for corpse clearance and neurotransmission in Caenorhabditis elegans.

Authors: Glen G Ernstrom; Robby Weimer; Divya R L Pawar; Shigeki Watanabe; Robert J Hobson; David Greenstein; Erik M Jorgensen
Journal: Genetics Date: 2012-03-16 Impact factor: 4.562

3. An extended nomenclature for mammalian V-ATPase subunit genes and splice variants.

Authors: Kevin C Miranda; Fiona E Karet; Dennis Brown
Journal: PLoS One Date: 2010-03-10 Impact factor: 3.240

4. Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.

Authors: S Kawasaki-Nishi; T Nishi; M Forgac
Journal: Proc Natl Acad Sci U S A Date: 2001-10-09 Impact factor: 11.205

5. The proton translocation domain of cellular vacuolar ATPase provides a target for the treatment of influenza A virus infections.

Authors: Konstantin H Müller; Denis E Kainov; Karim El Bakkouri; Xavier Saelens; Jef K De Brabander; Christian Kittel; Elisabeth Samm; Claude P Muller
Journal: Br J Pharmacol Date: 2011-09 Impact factor: 8.739

Review 10. Vacuolar H+ pumping ATPases in luminal acidic organelles and extracellular compartments: common rotational mechanism and diverse physiological roles.

Authors: Ge-Hong Sun-Wada; Yoh Wada; Masamitsu Futai
Journal: J Bioenerg Biomembr Date: 2003-08 Impact factor: 2.945

Luminal acidification of diverse organelles by V-ATPase in animal cells.

1. Regulation of organelle acidity.

2. V-ATPase V1 sector is required for corpse clearance and neurotransmission in Caenorhabditis elegans.

3. An extended nomenclature for mammalian V-ATPase subunit genes and splice variants.

4. Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.

5. The proton translocation domain of cellular vacuolar ATPase provides a target for the treatment of influenza A virus infections.

6. Ligand-dependent structural changes in the V(1) ATPase from Manduca sexta.

7. Coxsackievirus A9 infects cells via nonacidic multivesicular bodies.

8. Coordinate regulation of gene expression in the C. elegans excretory cell by the POU domain protein CEH-6.

Review 9. Regulation of vacuolar pH and its modulation by some microbial species.

Review 10. Vacuolar H+ pumping ATPases in luminal acidic organelles and extracellular compartments: common rotational mechanism and diverse physiological roles.