Journal
SCIENCE
Volume 351, Issue 6274, Pages 733-737Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aac6054
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Funding
- Pennsylvania Department of Health Tobacco Settlement Funds
- Canadian Institutes of Health Research
- National Institutes of Health [NIH GM024129, 1R33EB019785-01]
- Howard Hughes Medical Institute
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Purine biosynthetic enzymes organize into dynamic cellular bodies called purinosomes. Little is known about the spatiotemporal control of these structures. Using super-resolution microscopy, we demonstrated that purinosomes colocalized with mitochondria, and these results were supported by isolation of purinosome enzymes with mitochondria. Moreover, the number of purinosome-containing cells responded to dysregulation of mitochondrial function and metabolism. To explore the role of intracellular signaling, we performed a kinome screen using a label-free assay and found that mechanistic target of rapamycin (mTOR) influenced purinosome assembly. mTOR inhibition reduced purinosome-mitochondria colocalization and suppressed purinosome formation stimulated by mitochondria dysregulation. Collectively, our data suggest an mTOR-mediated link between purinosomes and mitochondria, and a general means by which mTOR regulates nucleotide metabolism by spatiotemporal control over protein association.
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