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eLife Volume 7 ,2018-07-01
Dual roles for ATP in the regulation of phase separated protein aggregates in Xenopus oocyte nucleoli
Cell Biology
Michael H Hayes 1 Elizabeth H Peuchen 2 Norman J Dovichi 2 Daniel L Weeks 1 , 3
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Received 2018-01-19, accepted for publication 2018-07-01, Published 2018-07-01

10.7554/eLife.35224.001For many proteins, aggregation is one part of a structural equilibrium that can occur. Balancing productive aggregation versus pathogenic aggregation that leads to toxicity is critical and known to involve adenosine triphosphate (ATP) dependent action of chaperones and disaggregases. Recently a second activity of ATP was identified, that of a hydrotrope which, independent of hydrolysis, was sufficient to solubilize aggregated proteins in vitro. This novel function of ATP was postulated to help regulate proteostasis in vivo. We tested this hypothesis on aggregates found in Xenopus oocyte nucleoli. Our results indicate that ATP has dual roles in the maintenance of protein solubility. We provide evidence of endogenous hydrotropic action of ATP but show that hydrotropic solubilization of nucleolar aggregates is preceded by a destabilizing event. Destabilization is accomplished through an energy dependent process, reliant upon ATP and one or more soluble nuclear factors, or by disruption of a co-aggregate like RNA.


Xenopus;ATP;oocyte;nucleus;nucleolus;protein aggregation


© 2018, Hayes et al
http://creativecommons.org/licenses/by/4.0/This article is distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use and redistribution provided that the original author and source are credited.


Michael H Hayes,Elizabeth H Peuchen,Norman J Dovichi,Daniel L Weeks. Dual roles for ATP in the regulation of phase separated protein aggregates in Xenopus oocyte nucleoli. eLife ,Vol.7(2018)



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