Ensuring cellular protein homeostasis, or proteostasis, requires precise control of protein
synthesis, folding, conformational maintenance, and degradation. A complex and adaptive …

BACKGROUND Proteins are synthesized on ribosomes as linear chains of amino acids and
must fold into unique three-dimensional structures to fulfill their biological functions. Protein …

The stalling of ribosomes during protein synthesis results in the production of truncated
polypeptides that can have deleterious effects on cells and therefore must be eliminated. In …

Ubiquitylation is an essential posttranslational modification that controls cell division,
differentiation, and survival in all eukaryotes. By combining multiple E3 ligases (writers) …

Heat causes protein misfolding and aggregation and, in eukaryotic cells, triggers
aggregation of proteins and RNA into stress granules. We have carried out extensive …

Mammalian cells remove misfolded proteins using various proteolytic systems, including the
ubiquitin (Ub)-proteasome system (UPS), chaperone mediated autophagy (CMA) and …

Cells possess an extensive network of components to safeguard proteome integrity and
maintain protein homeostasis (proteostasis). When this proteostasis network (PN) declines …

Protein homeostasis (proteostasis) requires the timely degradation of misfolded proteins and
their aggregates by protein quality control (PQC), of which molecular chaperones are an …

Mistakes are part of our world and constantly occurring. Due to transcriptional and
translational failures, genomic mutations or diverse stress conditions like oxidation or heat …

This article is part of a Minifocus on Ubiquitin. For further reading, please see related
articles: ʻUbiquitin and SUMO in DNA repair at a glanceʼ by Helle D. Ulrich (J. Cell Sci …