Identification of a vesicular nucleotide transporter

ATP is a major chemical transmitter in purinergic signal transmission. Before secretion, ATP is stored in secretory vesicles found in purinergic cells. Although the presence of active transport mechanisms for ATP has been postulated for a long time, the proteins responsible for its vesicular accumul...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2008-04, Vol.105 (15), p.5683-5686
Main Authors: Sawada, Keisuke, Echigo, Noriko, Juge, Narinobu, Miyaji, Takaaki, Otsuka, Masato, Omote, Hiroshi, Yamamoto, Akitsugu, Moriyama, Yoshinori
Format: Article
Language:English
Subjects:
Acetates
Adenosine Diphosphate
Adenosine triphosphatase
Adenosine Triphosphate - metabolism
Adrenal glands
Animals
Anions
ATP
Biochemistry
Biological Sciences
Cells
Chromaffin cells
Exocytosis
Genes
Guanosine Triphosphate
Humans
Liposomes
Mice
Nucleotide Transport Proteins - isolation & purification
Nucleotide Transport Proteins - metabolism
Nucleotides
Nucleotides - metabolism
PC12 Cells
Proteins
Rats
Secretory vesicles
Transfection
Ungulates
Vesicular Transport Proteins - isolation & purification
Vesicular Transport Proteins - metabolism
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Summary:ATP is a major chemical transmitter in purinergic signal transmission. Before secretion, ATP is stored in secretory vesicles found in purinergic cells. Although the presence of active transport mechanisms for ATP has been postulated for a long time, the proteins responsible for its vesicular accumulation remains unknown. The transporter encoded by the human and mouse SLC17A9 gene, a novel member of an anion transporter family, was predominantly expressed in the brain and adrenal gland. The mouse and bovine counterparts were associated with adrenal chromaffin granules. Proteoliposomes containing purified transporter actively took up ATP, ADP, and GTP by using membrane potential as the driving force. The uptake properties of the reconstituted transporter were similar to that of the ATP uptake by synaptic vesicles and chromaffin granules. Suppression of endogenous SLC17A9 expression in PC12 cells decreased exocytosis of ATP. These findings strongly suggest that SLC17A9 protein is a vesicular nucleotide transporter and should lead to the elucidation of the molecular mechanism of ATP secretion in purinergic signal transmission.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0800141105