The accumulation of unfolded proteins in the lumen of the endoplasmic reticulum (ER) induces
a coordinated adaptive program called the unfolded protein response (UPR). The UPR …

Cells respond to the accumulation of unfolded proteins by activating signal transduction
cascades that improve protein folding. One example of such a cascade is the unfolded protein …

… Work in the laboratory of DT Rutkowski is supported by the National Institutes of Health (grant
DK084058) and the Carver Trust Medical Research Initiative. Work in the laboratory of RS …

… UGGT1 deficiency leads to embryonic lethality approximately 12.5 dpc (DT Rutkowski,
SM Arnold, RJ Kaufman, unpublished data); however, MEFs were isolated that showed no …

Regulated intramembrane proteolysis (RIP) of endoplasmic reticulum (ER) membrane-anchored
transcription factors is known to maintain sterol homeostasis and to mediate the …

In vertebrates, three proteins—PERK, IRE1α, and ATF6α—sense protein-misfolding stress
in the ER and initiate ER-to-nucleus signaling cascades to improve cellular function. The …

The unfolded protein response (UPR) is linked to metabolic dysfunction, yet it is not known
how endoplasmic reticulum (ER) disruption might influence metabolic pathways. Using a …

Exercise has been shown to be effective for treating obesity and type 2 diabetes. However,
the molecular mechanisms for adaptation to exercise training are not fully understood. …

The preemptive quality control (pQC) pathway protects cells from acute endoplasmic
reticulum (ER) stress by attenuating translocation of nascent proteins despite their targeting to …

Multiple intracellular stress pathways converge on a single event—phosphorylation of the
translation initiation factor eIF2α and subsequent translational activation of the transcription …