α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation

Tim Bartels, Joanna G. Choi and Dennis J. Selkoe ()
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Tim Bartels: Center for Neurologic Diseases, Brigham and Women’s Hospital and Harvard Medical School
Joanna G. Choi: Center for Neurologic Diseases, Brigham and Women’s Hospital and Harvard Medical School
Dennis J. Selkoe: Center for Neurologic Diseases, Brigham and Women’s Hospital and Harvard Medical School

Nature, 2011, vol. 477, issue 7362, 107-110

Abstract: A new look at α-synuclein Pathogenic aggregation of α-synuclein (αSyn) is implicated in Parkinson's disease and related disorders. αSyn has long been regarded as a natively unfolded monomer that acquires secondary structure only when it binds to its target. This model is the basis for a number of published studies, but Bartels et al. report that endogenous αSyn isolated under entirely non-denaturing conditions from brain tissue, cell lines and living human cells occurs principally as a folded tetramer. This finding suggests that destabilization of the αSyn tetramer precedes misfolding and aggregation in synucleinopathies, and that agents that stabilize the normal tetramer may reduce αSyn pathogenicity.

Date: 2011
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DOI: 10.1038/nature10324

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