Spatial colocalization and functional link of purinosomes with mitochondria

Jarrod B. French, Sara A. Jones, Huayun Deng, Anthony M. Pedley, Doory Kim, Chung Yu Chan, Haibei Hu, Raymond J. Pugh, Hong Zhao, Youxin Zhang, Tony Jun Huang, Ye Fang, Xiaowei Zhuang, Stephen J. Benkovic

Research output: Contribution to journalArticlepeer-review

151 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)733-737
Number of pages5
Issue number6274
StatePublished - Feb 12 2016

All Science Journal Classification (ASJC) codes

  • General


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