For several decades sequential metabolic enzymes had long been hypothesized to form multi-enzyme complexes in cells to regulate metabolic flux.  Single molecule fluorescence imaging in live cells of the enzymes involved in human de novo purine biosynthesis uncovered the reversible formation of a metabolic multi-enzyme complex, the �purinosome�.  Purinosome formation was found to be significantly promoted in cells by the addition of small-molecule CK-2 specific inhibitors as well as by silencing the endogenous hCK2 alpha catalytic subunit with siRNA.  In addition, signaling for purinosome assembly is through a Gai   couple receptor.  Our present focus is on identifying factors that control the spatial distribution of the purinosome in the cytoplasm; transient protein-protein interactions within the purinosome; and the composition of the purinosome.

On de novo purine biosynthesis: The Purinosome

244th National Meeting (2012)

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