pH-dependent Cargo Sorting from the Golgi

The vacuolar proton-translocating ATPase (V-ATPase) plays a major role in organelle acidification and works together with other ion transporters to maintain pH homeostasis in eukaryotic cells. We analyzed a requirement for V-ATPase activity in protein trafficking in the yeast secretory pathway. Defi...

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Bibliographic Details
Published in:The Journal of biological chemistry 2011-03, Vol.286 (12), p.10058-10065
Main Authors: Huang, Chunjuan, Chang, Amy
Format: Article
Language:English
Subjects:
Amino Acid Transport Systems, Basic - genetics
Amino Acid Transport Systems, Basic - metabolism
Biological Transport - physiology
Cell Biology
Glucose - metabolism
Golgi Apparatus - genetics
Golgi Apparatus - metabolism
Hydrogen-Ion Concentration
Membrane Transport Proteins - genetics
Membrane Transport Proteins - metabolism
Plasma Membrane Proton Pumps
Proprotein Convertases - genetics
Proprotein Convertases - metabolism
Protein Sorting
Proton-Translocating ATPases - genetics
Proton-Translocating ATPases - metabolism
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Trafficking
Ubiquitination
Vacuolar ATPase
Vacuolar Proton-Translocating ATPases - genetics
Vacuolar Proton-Translocating ATPases - metabolism
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Summary:The vacuolar proton-translocating ATPase (V-ATPase) plays a major role in organelle acidification and works together with other ion transporters to maintain pH homeostasis in eukaryotic cells. We analyzed a requirement for V-ATPase activity in protein trafficking in the yeast secretory pathway. Deficiency of V-ATPase activity caused by subunit deletion or glucose deprivation results in missorting of newly synthesized plasma membrane proteins Pma1 and Can1 directly from the Golgi to the vacuole. Vacuolar mislocalization of Pma1 is dependent on Gga adaptors although no Pma1 ubiquitination was detected. Proper cell surface targeting of Pma1 was rescued in V-ATPase-deficient cells by increasing the pH of the medium, suggesting that missorting is the result of aberrant cytosolic pH. In addition to mislocalization of the plasma membrane proteins, Golgi membrane proteins Kex2 and Vrg4 are also missorted to the vacuole upon loss of V-ATPase activity. Because the missorted cargos have distinct trafficking routes, we suggest a pH dependence for multiple cargo sorting events at the Golgi.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M110.197889