Ubiquitination is involved in secondary growth, not initial formation of polyglutamine protein aggregates in C. elegans.

ABSTRACT:

Background

Protein misfolding and subsequent aggregation are hallmarks of several human diseases. The cell has a variety of mechanisms for coping with misfolded protein stress, including ubiquitin-mediated protein degradation. In fact, the presence of ubiquitin at protein aggregates is a common feature of protein misfolding diseases. Ubiquitin conjugating enzymes (UBCs) are part of the cascade of enzymes responsible for the regulated attachment of ubiquitin to protein substrates. The specific UBC used during ubiquitination can determine the type of polyubiquitin chain linkage, which in turn plays an important role in determining the fate of the ubiquitinated protein. Thus, UBCs may serve an important role in the cellular response to misfolded proteins and the fate of protein aggreg

SUBMITTER: Skibinski GA 

PROVIDER: S-EPMC3368771 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature