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PLK2 modulates α-synuclein aggregation in yeast and mammalian cells

Lookup NU author(s): Professor Tiago Outeiro

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Abstract

Phosphorylation of α-synuclein (aSyn) on serine 129 is one of the major post-translation modifications found in Lewy bodies, the typical pathological hallmark of Parkinson's disease. Here, we found that both PLK2 and PLK3 phosphorylate aSyn on serine 129 in yeast. However, only PLK2 increased aSyn cytotoxicity and the percentage of cells presenting cytoplasmic foci. Consistently, in mammalian cells, PLK2 induced aSyn phosphorylation on serine 129 and induced an increase in the size of the inclusions. Our study supports a role for PLK2 in the generation of aSyn inclusions by a mechanism that does not depend directly on serine 129 phosphorylation. © 2013 Springer Science+Business Media New York.


Publication metadata

Author(s): Basso E, Antas P, Marijanovic Z, Goncalves S, Tenreiro S, Outeiro TF

Publication type: Review

Publication status: Published

Journal: Molecular Neurobiology

Year: 2013

Volume: 48

Issue: 3

Pages: 854-862

Print publication date: 01/12/2013

Online publication date: 17/05/2013

ISSN (print): 0893-7648

ISSN (electronic): 1559-1182

URL: https://doi.org/10.1007/s12035-013-8473-z

DOI: 10.1007/s12035-013-8473-z

PubMed id: 23677647


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