SLC33A1 exports oxidized glutathione to maintain endoplasmic reticulum redox homeostasis [ERIP_RNASeq]
The endoplasmic reticulum (ER) is the primary site of synthesis of secretory and membrane proteins, suggesting that specific mRNAs may be enriched at the ER surface. To characterize ER-associated transcripts, ER fractions were isolated using ER immunoprecipitation (ER-IP) and RNA was extracted from ER-bound material and whole-cell lysates. RNA sequencing was performed to compare transcript composition between ER-associated and total cellular RNA. ER-IP RNA sequencing revealed enrichment of transcripts encoding proteins localized to the plasma membrane, ER, Golgi apparatus, lysosome, and extracellular space. This dataset provides transcriptomic profiling of ER-associated RNA and corresponding whole-cell controls. Overall design: ER-associated RNA was isolated by ER immunoprecipitation in the presence of RNase inhibitor. RNA was extracted from ER-IP material and from whole-cell lysates collected prior to ER purification. Libraries were prepared and sequenced to compare ER-associated transcripts with total cellular RNA. Biological replicates were analyzed for each condition. Sequencing reads were pseudoaligned using Salmon and differential enrichment was analyzed using limma-voom.