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Toxicity mechanism identified for Parkinson's disease
Date:1/1/2009

nother laboratory on disposal of alpha-synuclein by chaperone-mediated autophagy (CMA).

During CMA, certain selected proteins are funneled into lysosomes, compartments of the cell devoted to chewing up discarded proteins. Mao and colleagues found that lysosomes isolated from cells will absorb MEF2D protein, and interfering with CMA chemically causes MEF2D levels to rise.

MEF2D is a transcription factor, a protein that controls whether several genes are turned on or off. Previous studies have shown MEF2D is needed for proper development and survival of brain cells. To function, MEF2D must be able to bind DNA.

The authors found that when CMA is disrupted, most of the accumulated MEF2D can't bind DNA. This may indicate that the protein is improperly folded or otherwise modified.

"Even though there's a lot of it, something is making the MEF2D protein inactive," Mao says.

Mao and his colleagues found that mice that artificially overproduce alpha-synuclein (a model of Parkinson's disease) have elevated levels of apparently inactive MEF2D in their brains. In addition, MEF2D protein levels were higher in the brains of Parkinson's patients than in controls.

Following the influence of alpha-synuclein on MEF2D may be a way to connect the various genetic and environmental risk factors for Parkinson's, even if CMA is not the sole mechanism, Mao says.

"It may be that various stresses impact MEF2D in different ways," he says. "We think this work provides an explanation that ties several important observations together."


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Contact: Holly Korschun
hkorsch@emory.edu
404-727-3990
Emory University
Source:Eurekalert

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