Ontology highlight
ABSTRACT:
SUBMITTER: Falsone SF
PROVIDER: S-EPMC2781518 | biostudies-literature | 2009 Nov
REPOSITORIES: biostudies-literature
Falsone S Fabio SF Kungl Andreas J AJ Rek Angelika A Cappai Roberto R Zangger Klaus K
The Journal of biological chemistry 20090915 45
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 for ...[more]