Lysosomal Aspartylglucosaminidase Couples Glycoprotein Catabolism to Cell-Surface GlycoRNA Production
Cao, W.; Yang, Z.; Zhang, C.; Yi, L.; Miao, Y.; Zhao, S.; Yu, C.; Zhou, X.; Li, T.; Zhou, Y.; Lu, T.; Zhang, Y.; Dou, Y.; Fujita, M.; Xie, Y.; Liu, Y.-S.; Xie, R.
Show abstract
GlycoRNAs, small non-coding RNAs covalently linked to N-glycans, reveal an unexpected intersection between RNA biology and glycosylation, with potential roles in immunity and cell-cell communication. The origins and biogenesis of their glycans remain unclear. Using CRISPR-Cas9 screening, metabolic labeling, and lysosome-targeted proteomics, we reconfirm canonical N-glycosylation enzymes (STT3A/B) and identify components of the mannose-6-phosphate (M6P) lysosomal sorting pathway (GNPTAB, M6PR) as essential contributors. Strikingly, lysosomal aspartylglucosaminidase (AGA) acts as a rate-limiting regulator, linking glycoprotein catabolism to glycoRNA formation. Loss of AGA collapses both abundance and diversity of RNA-linked N-glycans, while pulse-chase tracing shows glycoprotein-derived glycans are repurposed for RNA glycosylation. These findings position lysosomes as active participants in RNA modification and define glycoRNA biogenesis as a metabolically integrated process.
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