Small heat shock proteins (sHsps) constitute a diverse chaperone family that shares the α-
crystallin domain, which is flanked by variable, disordered N-and C-terminal extensions …

Numerous nascent proteins undergo folding and maturation within the luminal and
membrane compartments of the endoplasmic reticulum (ER). Despite the presence of …

Maintenance of cellular proteostasis is achieved by a multi-layered quality control network,
which counteracts the accumulation of misfolded proteins by refolding and degradation …

Spatial sorting to discrete quality control sites in the cell is a process harnessing the toxicity
of aberrant proteins. We show that the yeast t-snare phosphoprotein syntaxin5 (Sed5) acts …

Since the discovery of ubiquitin conjugation as a cellular mechanism that triggers
proteasomal degradation, the mode of substrate recognition by the ubiquitin-ligation system …

DNAJC12, a type III member of the HSP40/DNAJ family, has been identified as the specific
co‐chaperone of phenylalanine hydroxylase (PAH) and the other aromatic amino acid …

Uridylation-dependent RNA decay is a widespread eukaryotic pathway modulating RNA
homeostasis. Terminal uridylyltransferases (Tutases) add untemplated uridyl residues to …

Cells have elaborated a complex strategy to maintain protein homeostasis under
physiological as well as stress conditions with the aim to ensure the smooth functioning of …

When proteostasis is disrupted by stresses such as heat shock, the heat stress response will
be stimulated, leading to up-regulation of molecular chaperones by transcriptional activation …

This work provides new insights not only into Brucella pathogenesis, but also places effector
targeting of the endoplasmic reticulum quality control machinery at the center of bacterial …