Drugging the unfolded protein response in acute leukemias

Drugging the unfolded protein response in acute leukemias

The unfolded protein response (UPR), an endoplasmic reticulum (ER) stress-induced signaling cascade, is mediated by three major stress sensors IRE-1α, PERK, and ATF6α. Studies described the UPR as a critical network in selection, adaptation, and survival of cancer cells. While previous reviews focused mainly on solid cancer cells, in this review, we summarize the recent findings focusing on acu...

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...

The unfolded protein response.

The endoplasmic reticulum (ER) is a principal site for folding and maturation of transmembrane, secretory and ERresident proteins. Perturbations that alter ER homeostasis can lead to accumulation of unfolded proteins (UPs), which is a threat to all living cells. To cope with the stress, cells activate an intracellular signaling pathway – the unfolded protein response (UPR). The UPR is an integr...

SnapShot: The Unfolded Protein Response

Unpacking the Unfolded Protein Response

This year, the Albert Lasker Basic Medical Research Award will be shared by Peter Walter and Kazutoshi Mori for discoveries revealing the molecular mechanism of the unfolded protein response, an intracellular quality control system that detects harmful misfolded proteins in the endoplasmic reticulum and then signals the nucleus to carry out corrective measures.