Peter Walter

Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus.

On the mechanism of sensing unfolded protein in the endoplasmic reticulum

Unfolded proteins in the endoplasmic reticulum (ER) activate the ER transmembrane sensor Ire1 to trigger the unfolded protein response (UPR), a homeostatic signaling pathway tha...

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 activ...

Bypassing a Kinase Activity with an ATP-Competitive Drug

Unfolded proteins in the endoplasmic reticulum cause trans-autophosphorylation of the bifunctional transmembrane kinase Ire1, which induces its endoribonuclease activity. The en...

IRE1-Independent Gain Control of the Unfolded Protein Response

Nonconventional splicing of the gene encoding the Hac1p transcription activator regulates the unfolded protein response (UPR) in Saccharomyces cerevisiae. This simple on/off swi...

Genome-scale approaches for discovering novel nonconventional splicing substrates of the Ire1 nuclease

Abstract Background The unfolded protein response (UPR) allows intracellular feedback regulation that adjusts the protein-folding capacity of the endoplasmic reticulum (ER) acco...

The integrated stress response: From mechanism to disease

Proteostasis dISRupted Despite their importance, many crucial networks for protein quality control within cells diminish with age. The resulting loss of proteostasis, the proces...

Signal integration in the endoplasmic reticulum unfolded protein response