Spatial Colocalization and Functional Link of Purinosomes with Mitochondria
- Authors
- French, Jarrod B.; Jones, Sara A.; Deng, Huayun; Pedley, Anthony M.; Kim, Doory; Chan, Chung Yu; Hu, Haibei; Pugh, Raymond J.; Zhao, Hong; Zhang, Youxin; Huang, Tony Jun; Fang, Ye; Zhuang, Xiaowei; Benkovic,Stephen J.
- Issue Date
- Feb-2016
- Publisher
- AMER ASSOC ADVANCEMENT SCIENCE
- Citation
- SCIENCE, v.351, no.6274, pp.733 - 737
- Indexed
- SCIE
SCOPUS
- Journal Title
- SCIENCE
- Volume
- 351
- Number
- 6274
- Start Page
- 733
- End Page
- 737
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/142853
- DOI
- 10.1126/science.aac6054
- ISSN
- 0036-8075
- Abstract
- 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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