Spermidine cures yeast of prions
Authors:Shaun H. Speldewinde, and Chris M. Grant
doi: 10.15698/mic2016.01.474
Volume 3, pp. 46 to 48, published 25/12/2015.
University of Manchester, Faculty of Life Sciences, The Michael Smith Building, Oxford Road, Manchester, M13 9PT, UK.
Keywords:
autophagy, oxidative stress, prions, spermidine, yeast.
Corresponding Author(s):
Conflict of interest statement:
None of the authors have any competing interests.
Please cite this article as:
Shaun H. Speldewinde, and Chris M. Grant (2015). Spermidine cures yeast of prions. Microbial Cell 3(1): 46-48. doi: 10.15698/mic2016.01.474
© 2015 Speldewinde and Grant. This is an open-access article released under the terms of the Creative Commons Attribution (CC BY) license, which allows the unrestricted use, distribution, and reproduction in any medium, provided the original author and source are acknowledged.
Abstract:
Prions are self-perpetuating amyloid protein aggregates which underlie various neurodegenerative diseases in mammals. The molecular basis underlying their conversion from a normally soluble protein into the prion form remains largely unknown. Studies aimed at uncovering these mechanism(s) are therefore essential if we are to develop effective therapeutic strategies to counteract these disease-causing entities. Autophagy is a cellular degradation system which has predominantly been considered as a non-selective bulk degradation process which recycles macromolecules in response to starvation conditions. We now know that autophagy also serves as a protein quality control mechanism which selectively degrades protein aggregates and damaged organelles. These are commonly accumulated in various neurodegenerative disorders including prion diseases. In our recent study [Speldewinde et al. Mol. Biol. Cell. (2015)] we used the well-established yeast [PSI+]/Sup35 and [PIN+]/Rnq1 prion models to show that autophagy prevents sporadic prion formation. Importantly, we found that spermidine, a polyamine that has been used to increase autophagic flux, acts as a protective agent which prevents spontaneous prion formation.