Delayed Ras/PKA signaling augments the unfolded protein response

Delayed Ras/PKA signaling augments the unfolded protein response.

During environmental, developmental, or genetic stress, the cell's folding capacity can become overwhelmed, and misfolded proteins can accumulate in all cell compartments. Eukaryotes evolved the unfolded protein response (UPR) to counteract proteotoxic stress in the endoplasmic reticulum (ER). Although the UPR is vital to restoring homeostasis to protein folding in the ER, it has become evident...

Intracellular signaling by the unfolded protein response.

The unfolded protein response (UPR) is an intracellular signaling pathway that is activated by the accumulation of unfolded proteins in the endoplasmic reticulum (ER). UPR activation triggers an extensive transcriptional response, which adjusts the ER protein folding capacity according to need. As such, the UPR constitutes a paradigm of an intracellular control mechanism that adjusts organelle ...

Heterotrimeric G protein signaling in the Arabidopsis unfolded protein response.

We present evidence that heterotrimeric G protein signaling is involved in cell death associated with the unfolded protein response (UPR) in Arabidopsis. Seedlings of homozygous agb1-2 (Gbeta-null mutation) mutant plants are markedly more resistant to growth inhibition by the protein glycosylation inhibitor tunicamycin (Tm) than either wild-type plants or gpa1-4 (Galpha-null mutation) mutants. ...

Signaling the unfolded protein response from the endoplasmic reticulum.

The unfolded protein response

Where does the UPR function? Between the endoplasmic reticulum (ER) and the nucleus of eukaryotic cells. All secreted proteins and proteins that reside in secretory compartments translocate as nascent peptide chains into the ER, where they may undergo folding, modification and assembly before assuming their functional conformations. The ER maintains a specialized oxidizing environment to aid ch...