System-wide analysis reveals intrinsically disordered proteins are prone to ubiquitylation after misfolding stress.

ABSTRACT: Damaged and misfolded proteins that are no longer functional in the cell need to be eliminated. Failure to do so might lead to their accumulation and aggregation, a hallmark of many neurodegenerative diseases. Protein quality control pathways play a major role in the degradation of these proteins, which is mediated mainly by the ubiquitin proteasome system. Despite significant focus on identifying ubiquitin ligases involved in these pathways, along with their substrates, a systems-level understanding of these pathways has been lacking. For instance, as misfolded proteins are rapidly ubiquitylated, unconjugated ubiquitin is rapidly depleted from the cell upon misfolding stress; yet it is unknown whether certain targets compete more efficiently to be ubiquitylated. Using a system-wide approa

SUBMITTER: Ng AH 

PROVIDER: S-EPMC3769323 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature