Lecture 'Stress-induced clustering of the stress sensor IRE1α is driven by the intrinsically disordered regions within its ER lumenal domain'

For whom
Alumni , Business , Employees , Students
27-01-2023 from 11:30 to 12:30
UGent-VIB-onderzoeksgebouw, Technologiepark 71, 9052 Zwijnaarde
VIB-UGent Center for Inflammation Research

The unfolded protein response sensor, IRE1, signals by clustering in the endoplasmic reticulum. How this clustering takes place, will be explained.

Elif Karagoz (Medical University of Vienna, Austria) is our guest speaker. Protein-folding homeostasis in the endoplasmic reticulum (ER) is maintained by the unfolded protein response (UPR). IRE1 is the most conserved UPR sensor/transducer. During ER stress, IRE1 forms clusters on the ER membrane to initiate signaling. IRE1 clustering is driven by its ER lumenal domain (LD). However, how IRE1’s LD precipitates into oligomers remains largely unknown. By biochemical and cell biological approaches, we found that weak multivalent interactions between intrinsically disordered regions (IDRs) in IRE1α LD regulate its clustering. We propose that ER membrane and unfolded ligand polypeptides act as assembly platforms guiding dynamic IRE1 assemblies into active oligomers.

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