BAG1 restores formation of functional DJ-1 L166P dimers and DJ-1 chaperone activity

2010 | journal article; research paper. A publication with affiliation to the University of Göttingen.

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​BAG1 restores formation of functional DJ-1 L166P dimers and DJ-1 chaperone activity​
Deeg, S. ; Gralle, M. ; Sroka, K. ; Bähr, M. ; Wouters, F. S.   & Kermer, P. ​ (2010) 
The Journal of Cell Biology188(4) pp. 505​-513​.​ DOI: 

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Deeg, Sebastian ; Gralle, Mathias ; Sroka, Kamila ; Bähr, Mathias ; Wouters, Fred Silvester ; Kermer, Pawel 
Mutations in the gene coding for DJ-1 protein lead to early-onset recessive forms of Parkinson's disease. It is believed that loss of DJ-1 function is causative for disease, although the function of DJ-1 still remains a matter of controversy. We show that DJ-1 is localized in the cytosol and is associated with membranes and organelles in the form of homodimers. The disease-related mutation L166P shifts its subcellular distribution to the nucleus and decreases its ability to dimerize, impairing cell survival. Using an intracellular foldase biosensor, we found that wild-type DJ-1 possesses chaperone activity, which is abolished by the L166P mutation. We observed that this aberrant phenotype can be reversed by the expression of the cochaperone BAG1 (Bcl-2-associated athanogene 1), restoring DJ-1 subcellular distribution, dimer formation, and chaperone activity and ameliorating cell survival.
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The Journal of Cell Biology 



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