A close association of torsinA and alpha-synuclein in Lewy bodies - A fluorescence resonance energy transfer study

TorsinA, a novel protein In which a mutation causes dominant, early onset t orsion dystonia, may serve as a chaperone for misfolded proteins that requi re refolding or degradation. It has been hypothesized that misfolded alpha -synuclein, a protein in which two mutations cause autosomal dominantly inh erited Parkinson's disease, serves as a nidus for the development of a Lewy body. We hypothesized that torsinA plays a role in the cellular processing of alpha -synuclein. We demonstrate that anti-torsin antibodies stain Lewy bodies and Lewy neurites in the substantia nigra and cortex. Using sensiti ve fluorescent resonance energy transfer (FRET) techniques, we find evidenc e of a close association between torsinA and alpha -synuclein in Lewy bodie s.