SLC17A9 Protein Functions as a Lysosomal ATP Transporter and Regulates Cell Viability

Lysosomes contain abundant ATP, which is released through lysosomal exocytosis following exposure to various stimuli. However, the molecular mechanisms underlying lysosomal ATP accumulation remain unknown. The vesicular nucleotide transporter, also known as solute carrier family 17 member 9 (SLC17A9...

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Bibliographic Details
Published in:The Journal of biological chemistry 2014-08, Vol.289 (33), p.23189-23199
Main Authors: Cao, Qi, Zhao, Kexin, Zhong, Xi Zoë, Zou, Yuanjie, Yu, Haichuan, Huang, Peng, Xu, Tian-Le, Dong, Xian-Ping
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - genetics
Adenosine Triphosphate - metabolism
Animals
Biological Transport, Active - physiology
Cell Biology
Cell Death
Cell Survival - physiology
Chlorocebus aethiops
Chromaffin Cells - cytology
Chromaffin Cells - metabolism
COS Cells
HEK293 Cells
Humans
Lysosomes - genetics
Lysosomes - metabolism
Nucleotide Transport Proteins - genetics
Nucleotide Transport Proteins - metabolism
Pancreas - cytology
Pancreas - metabolism
T-Lymphocytes - cytology
T-Lymphocytes - metabolism
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Summary:Lysosomes contain abundant ATP, which is released through lysosomal exocytosis following exposure to various stimuli. However, the molecular mechanisms underlying lysosomal ATP accumulation remain unknown. The vesicular nucleotide transporter, also known as solute carrier family 17 member 9 (SLC17A9), has been shown to function in ATP transport across secretory vesicles/granules membrane in adrenal chromaffin cells, T cells, and pancreatic cells. Here, using mammalian cell lines, we report that SLC17A9 is highly enriched in lysosomes and functions as an ATP transporter in those organelles. SLC17A9 deficiency reduced lysosome ATP accumulation and compromised lysosome function, resulting in cell death. Our data suggest that SLC17A9 activity mediates lysosomal ATP accumulation and plays an important role in lysosomal physiology and cell viability.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M114.567107