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Updated: May 11, 2026

Assaying the Kinase Activity of LRRK2 in vitro
Published on: January 18, 2012
PLK2 modulates α-synuclein aggregation in yeast and mammalian cells
Elisa Basso1, Pedro Antas, Zrinka Marijanovic
1Cell and Molecular Neuroscience Unit, Instituto de Medicina Molecular, Lisbon, Portugal.
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.

