The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein.

@article{Falsone2009TheMC,
  title={The molecular chaperone Hsp90 modulates intermediate steps of amyloid assembly of the Parkinson-related protein alpha-synuclein.},
  author={S. Fabio Falsone and Andreas J. Kungl and Angelika Rek and Roberto Cappai and Klaus Zangger},
  journal={The Journal of biological chemistry},
  year={2009},
  volume={284 45},
  pages={
          31190-9
        }
}
Alpha-synuclein is an intrinsically unstructured protein that binds to membranes, forms fibrils, and is involved in neurodegeneration. We used a reconstituted in vitro system to show that the molecular chaperone Hsp90 influenced alpha-synuclein vesicle binding and amyloid fibril formation, two processes that are tightly coupled to alpha-synuclein folding. Binding of Hsp90 to monomeric alpha-synuclein occurred in the low micromolar range, involving regions of alpha-synuclein that are critical… CONTINUE READING
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