ArticleiScience2026
The UFSP2-C1orf27 complex positions nascent GPCRs to the ufmylation system for ER export control.
Article in iScience, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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6 authors.
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Abstract
The ufmylation system is implicated in multiple cellular processes and human diseases; our recent study has identified its function in protein trafficking, but detailed mechanisms remain elusive. Here, we reveal cooperative actions of ufmylation protease UFSP2 and endoplasmic reticulum (ER)-anchored protein C1orf27 on ER-to-Golgi transport of some G protein-coupled receptors (GPCRs). UFSP2 interacts with C1orf27 for ER recruitment, and its activation is dispensable for recruitment but essential for ER export of GPCRs. Structural analysis suggests that UFSP2 and C1orf27 are diverged from a
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