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Observations on the Cellular Dynamics of a Metabolic Complex, the Purinosome
Abstract   Open access   Peer reviewed

Observations on the Cellular Dynamics of a Metabolic Complex, the Purinosome

Stephen Benkovic, Chung Yu (Keith) Chan, Doory Kim, Anthony Pedley and Xiaowei Zhuang
The FASEB journal, Vol.30(S1)
04/2016
DOI: 10.1096/fasebj.30.1_supplement.240.1
url
https://doi.org/10.1096/fasebj.30.1_supplement.240.1View
Published (Version of record) Open Access

Abstract

Abstract only For several decades sequential metabolic enzymes had long been hypothesized to form multi‐enzyme complexes in cells to regulate metabolic flux. Single molecular fluorescence imaging in live cells of the six human enzymes involved in de novo purine biosynthesis uncovered the reversible formation of a metabolic multi‐enzyme complex, the “purinosome”. Purinosome formation was found to be sensitive to changes in purine demands and assisted by molecular chaperones. In cells lacking purine salvage enzymes, purinosome levels were enhanced. Despite the transient nature of this complex, the flux through the de novo pathway was increased in cells containing a high density of purinosomes, which is consistent with its function. Imaging experiments revealed the proximity of these complexes near mitochondria and along microtubules. The question then is to what extent are there relationships between these subcellular structures and the purinosome? I will discuss imaging analyses that explain the cellular dynamics of the purinosome near these structures in hopes to further understand how a cell responds to purine demand to fulfill its metabolic requirements. Support or Funding Information National Institutes of Health, #GM024129

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