OST component RPN1 is a novel regulator of IRE1 RNase activity that interacts with multiple distinct IRE1 and PERK complexes
Larburu, N.; Storer, F.; Ben-Khoud, Y.; Chen, C.-s.; Adams, C. J.; Southall, T.; Ali, M. M.
Show abstract
The unfolded protein response (UPR) is an essential cell signalling system that regulates ER protein homeostasis. IRE1 and PERK are receptor proteins that propagate the UPR signal from the ER to the cytosol. Both receptors are suggested to interact with various proteins from different biological pathways, although the scale and scope of such interactions are unclear. Previous reconstitution experiments have utilized purified isolated domains of IRE1 and PERK to understand mechanism. Here, we affinity purify full length IRE1 and PERK from mammalian cells and characterise the complexes they form by biochemical techniques and assess RNase function in vivo. We identify RPN1 as a novel interacting protein present in complexes with IRE1 and PERK. In the Drosophila eye, RNAi knockdown of RPN1 results in loss of IRE1 RNase activity. This work provides a basis for understanding of protein interaction networks for IRE1 and PERK and identifies OST subunit RPN1 as a novel regulator of IRE1 RNase activity.
Matching journals
The top 8 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Tagging allows faithful tracing of expression and enhances biochemical detection of Ran Binding Protein 9 in vivo and reveals its interaction with Nucleolin. 94%
- Identification of new interactors of eIF3f by endogenous proximity-dependent biotin labelling in human muscle cells. 93%
- NMDAR mediated dynamic changes in m6A inversely correlates with neuronal translation 93%
Similar papers in this journal
Similar papers in this journal
- Nanodiscs-based proteomics identify Caj1 as an Hsp40 with affinity for phosphatidic acid lipids 93%
- The unphosphorylated form of the PAQosome core subunit RPAP3 binds ribosomal preassembly complexes to modulate ribosome biogenesis. 93%
- Systematic Identification of Protein Phosphorylation-Mediated Interactions 92%
Similar papers in this journal
- mTOR-driven widespread exon skipping renders multifaceted gene regulation and proteome complexity 93%
- Big fish, little fish: N-terminal acetyltransferase Naa40p proteoforms caught in the act 92%
- A proximity complementation assay to identify small molecules that enhance the traffic of ABCA4 misfolding variants. 92%
Similar papers in this journal
- Characterizing the monomer-dimer equilibrium of UbcH8/Ube2L6: A combined SAXS and NMR study 91%
- Experimental characterization of in silico red-shift predicted iLOVL470T/Q489K and iLOVV392K/F410V/A426S mutants 91%
- Characterization of the SARS-CoV-2 S Protein: Biophysical, Biochemical, Structural, and Antigenic Analysis 91%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.