Effect of N-glycosylated of SIDT1 on gene expression of human embryonic kidney (HEK293T) cells

The mammalian SID-1 transmembrane family member 1 (SIDT1), are multi-pass transmembrane proteins that mediate the cellular uptake and intracellular trafficking of nucleic acids, playing important roles in the immune response and tumorigenesis. We here report N-glycosylation as a key regulator of SIDT1-mediated RNA transport activities. To identify regulators whose expression was induced by N-glycan-deficient SIDT1, we further performed gene expression analysis on wild-type SIDT1 and non-N-glycosylated SIDT1overexpression HEK293F cells. Samples were subjected to RNA sequencing (RNA-seq) to reveal genes differences in SIDT1 overexpressing cells versus SIDT1?N-glycan overexpressing cells. Our results indicate that the non-N-glycosylated SIDT1 is severely misfolded. These severely misfolded non-N-glycosylated SIDT1 may cause ER stress, leading to the induction of the unfolded protein response (UPR) and regulated by the ERQC system. Overall design: To identify regulators whose expression was induced by N-glycan-deficient SIDT1, we performed gene expression analysis on empty vector pcDNA3.1(+), wild-type SIDT1, and non-N-glycosylated SIDT1 (SIDT1DN-glycan) overexpression HEK293F cells.