Description
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 SIDT1N-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.
Curator
yq_pan