Vacuolar H+-ATPase subunits Voa1 and Voa2 cooperatively regulate secretory vesicle acidification, transmitter uptake, and storage

@inproceedings{Saw2011VacuolarHS,
  title={Vacuolar H+-ATPase subunits Voa1 and Voa2 cooperatively regulate secretory vesicle acidification, transmitter uptake, and storage},
  author={Ner Mu Nar Saw and Soo-Young Ann Kang and Leon Parsaud and Gayoung Anna Han and Tiandan Jiang and Krzysztof Grzegorczyk and Michael Surkont and Ge-hong Sun-Wada and Yoh Wada and Lijun Li and Shuzo Sugita},
  booktitle={Molecular biology of the cell},
  year={2011}
}
The Vo sector of the vacuolar H(+)-ATPase is a multisubunit complex that forms a proteolipid pore. Among the four isoforms (a1-a4) of subunit Voa, the isoform(s) critical for secretory vesicle acidification have yet to be identified. An independent function of Voa1 in exocytosis has been suggested. Here we investigate the function of Voa isoforms in secretory vesicle acidification and exocytosis by using neurosecretory PC12 cells. Fluorescence-tagged and endogenous Voa1 are primarily localized… CONTINUE READING
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