Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans.

ABSTRACT: Protein aggregation is associated with a wide range of degenerative human diseases with devastating consequences, as exemplified by Alzheimer's, Parkinson's, and Huntington's diseases. In vitro kinetic studies have provided a mechanistic understanding of the aggregation process at the molecular level. However, it has so far remained largely unclear to what extent the biophysical principles of amyloid formation learned in vitro translate to the complex environment of living organisms. Here, we take advantage of the unique properties of a Caenorhabditis elegans model expressing a fluorescently tagged polyglutamine (polyQ) protein, which aggregates into discrete micrometer-sized inclusions that can be directly visualized in real time. We provide a quantitative analysis of protein aggregation

SUBMITTER: Sinnige T 

PROVIDER: S-EPMC7980373 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature