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AbstractThe Endoplasmic Reticulum (ER)-resident intramembrane rhomboid protease RHBDL4 generates metastable protein fragments and together with the ER-associated degradation (ERAD) machinery provides a clearance mechanism for aberrant and surplus proteins. However, the endogenous substrate spectrum and with that the role of RHBDL4 in physiological ERAD is mainly unknown. Here, we use quantitative proteomics to identify physiological RHBDL4 substrates. This revealed oligosacharyltransferasedoi:10.1101/850776 fatcat:o5gtooiysna7blobjljblhrlpu