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Comment
. 2013 Oct 8;110(41):16293-4.
doi: 10.1073/pnas.1315622110. Epub 2013 Sep 26.

Silencing synuclein at the synapse with PLK2

Brendan D Looyenga  1 , Patrik Brundin
Affiliations
Comment

Silencing synuclein at the synapse with PLK2

Brendan D Looyenga et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

Conflict of interest statement: P.B. is a paid consultant for H Lundbeck A/S, TEVA Pharmaceuticals, and Renovo Neural Inc. He is a cofounder of ParkCell AB and Acousort AB. He collaborates with Bioartic Neuroscience AB and has funded collaborations with Metabolic Development Solutions Company and Neuronova AB.

Figures

Fig. 1.
Fig. 1.
Dual function of PLK2 in the phosphorylation and degradation of neuronal α-syn. Coordinate expression of α-syn and PLK2 in the same neuronal compartment promotes specific phosphorylation of α-syn at S129 by the PLK2 kinase domain. Upon phosphorylation (p-S129), α-syn is bound by the PLK2 polo-box domain. Formation of this binary complex promotes trafficking of α-syn into the autophagy/lysosomal pathway, which ultimately leads to its degradation. Inhibition of lysosomal function may, however, promote the accumulation of phosphorylated α-syn. Neurons may deal with excess α-syn by storing it in the form of large intracellular aggregates (Lewy bodies) or by releasing into the extracellular space, thus leading to cell-to-cell transmission.
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Comment on

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