Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-12

AUTHORS

Ulf Dettmer, Andrew J. Newman, Frank Soldner, Eric S. Luth, Nora C. Kim, Victoria E. von Saucken, John B. Sanderson, Rudolf Jaenisch, Tim Bartels, Dennis Selkoe

ABSTRACT

β-Sheet-rich α-synuclein (αS) aggregates characterize Parkinson's disease (PD). αS was long believed to be a natively unfolded monomer, but recent work suggests it also occurs in α-helix-rich tetramers. Crosslinking traps principally tetrameric αS in intact normal neurons, but not after cell lysis, suggesting a dynamic equilibrium. Here we show that freshly biopsied normal human brain contains abundant αS tetramers. The PD-causing mutation A53T decreases tetramers in mouse brain. Neurons derived from an A53T patient have decreased tetramers. Neurons expressing E46K do also, and adding 1-2 E46K-like mutations into the canonical αS repeat motifs (KTKEGV) further reduces tetramers, decreases αS solubility and induces neurotoxicity and round inclusions. The other three fPD missense mutations likewise decrease tetramer:monomer ratios. The destabilization of physiological tetramers by PD-causing missense mutations and the neurotoxicity and inclusions induced by markedly decreasing tetramers suggest that decreased α-helical tetramers and increased unfolded monomers initiate pathogenesis. Tetramer-stabilizing compounds should prevent this. More... »

PAGES

7314

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms8314

DOI

http://dx.doi.org/10.1038/ncomms8314

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005526638

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26076669


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