RBM39 Modulates UPR Signaling Through Regulation of IRE1α Alternative Splicing. Kim and Behera et al.
收藏DataCite Commons2026-04-28 更新2026-05-04 收录
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资源简介：
The unfolded protein response (UPR) maintains endoplasmic reticulum proteostasis through signaling branches, including the IRE1α-XBP1 axis, which promotes cell survival via non-canonical XBP1 splicing. Upstream regulators of this pathway remain incompletely defined. Using CRASP-Seq, a scalable RNA-based CRISPR screening platform, we identified RBM39, a U2 snRNP auxiliary factor, as essential for XBP1 non-canonical splicing. RBM39 perturbation triggers ERN1 exon-18 skipping, destabilizing IRE1α and generating a dominant-negative isoform that impairs XBP1 splicing. Heat shock reduces RBM39 activity and induces ERN1 exon-18 skipping, revealing a stress-responsive mechanism that suppresses the IRE1α-XBP1 axis. These results uncover a previously unrecognized layer of UPR regulation.
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Mendeley Data
创建时间：
2026-04-28
