Accumulation of misfolded proteins results in the activation of the unfolded protein response (UPR) in the endoplasmic reticulum. Ire1 is important in this pathway and functions as a kinase and endoribonuclease. This paper solves the crystal structure of Ire1 kinase and shows that it undergoes spontaneous assembly into a rod-shaped oligomer. This arrangement positions the kinase domains for trans-autophosphorylation, orders the RNase domains and creates an interaction site for mRNA substrate binding.
- Alexei V. Korennykh
- Pascal F. Egea
- Peter Walter
