Abstract
The interior of a eukaryotic cell is an extremely crowded environment containing thousands of different types of biomolecules. Within this dense morass, however, are differentiated micro‐environments, sometimes called mesoscale assemblies or biomolecular condensates, which are transiently assembled to respond to cellular stimuli. These protein systems provide a highly tunable and specific level of temporal and spatial control over processes such as metabolism and signaling. One such system has evolved to manage the needs of purine metabolism in eukaryotic cells. The purinosome is a newly discovered protein assembly that is involved in regulating de novo purine biosynthesis. This dynamic complex is composed of all six members of the pathway and several known accessory factors. Recent imaging and complementary biochemical analyses revealed that the purinosome structurally and functionally associates with mitochondria. This mutualistic interaction provides energy for purine biosynthesis while creating the necessary precursors for ATP production. The implications of this observation, additional observations about purinosome trafficking, and our lab's progress towards understanding the mechanisms of assembly will be presented.Support or Funding InformationThis work is funded by the National Institute of General Medical Sciences of the NIH under Award Number R35GM124898.This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.
Published Version
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