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Experimental Genetics Group

Bolleke Abstract   Pijltje
Components Enhancing a-synuclein Aggregation and Toxicity in a Humanized Yeast.

New trends in Alzheimer and Parkinson related disorders: ADPD 2005.

Pellens K1*, Zabrocki P1*, Vanhelmont T1, Vandebroek T2, Griffioen G3, Wera S3, Van Leuven F2, Winderickx J1.

1Functional Biology, Katholieke Universiteit Leuven, Leuven, Belgium.
2LEGT_EGG, Katholoieke Universiteit Leuven, Leuven, Belgium.
3N.V. reMYND, Leuven, Belgium.
*These authors equally contribued to this work.

We developed a humanized yeast model to investigate the pathogenic mechanisms of a-synuclein (aSYN). Our data demonstrate that aSYN aggregation is a nucleation-elongation process initiated at the plasma membrane. It can be enhanced by treatment with DMSO and even drugs that influence autophagic and proteasomal clearance have dramatic effects. Moreover, aggregation of aSYN interferes with endocytosis. Co-expression of aSYN and protein tau is synergistically toxic for yeast cells and this led us to use our yeast model to screen a human hippocampus cDNA library to identify novel components that enhance toxicity of aSYN in yeast.

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