西亚试剂：BAG1 restores formation of functional DJ-1 L166P dimers and

BAG1 restores formation of functional DJ-1 L166P dimers and DJ-1 chaperone activity
Sebastian Deeg1, Mathias Gralle2, Kamila Sroka1, Mathias B?hr1,3, Fred Silvester Wouters2,3, and Pawel Kermer1,3

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  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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