Journal
MOLECULAR NEUROBIOLOGY
Volume 48, Issue 3, Pages 854-862Publisher
HUMANA PRESS INC
DOI: 10.1007/s12035-013-8473-z
Keywords
alpha-Synuclein; Parkinson's disease; Polo-like kinases; Aggregation; Serine 129; Phosphorylation
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Funding
- Fundacao para a Ciencia e Tecnologia [PTDC/SAU-NEU/105215/2008, PTDC/BIA-BCM/117975/2010, SFRH/BPD/65890/2009, SFRH/BPD/35767/2007, SFRH/BI/5177/2011, SFRH/BD/79337/2011]
- Marie Curie International Reintegration Grant
- EMBO Installation Grant
- EC Framework 7 Marie Curie Fellowship Training Network Grant (NEURASYNC)
- EU FP7 MEFOPA
- AXA Research Fund
- Fundação para a Ciência e a Tecnologia [SFRH/BPD/65890/2009, SFRH/BPD/35767/2007, SFRH/BD/79337/2011, PTDC/SAU-NEU/105215/2008, PTDC/BIA-BCM/117975/2010] Funding Source: FCT
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Phosphorylation of alpha-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.
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