Fan, X.-J. | Search bioRxiv

bioRxiv2025

StCEL-based platform enables detection and sequencing of native sialoglycoRNA

Glycosylated RNAs (glycoRNAs) are an emerging class of biomolecules characterized by glycans attached to RNA molecules. Currently, glycoRNA detection remains largely confined to cellular models, substantially impeding its functional characterization and clinical translation. Here, we developed sialyltransferase-mediated chemical enzymatic labeling (StCEL), in which azido-modified sialic acid was transferred to the natural sialic acid on sialoglycoRNA, enabling the detection of native sialoglycoRNA across diverse biological samples with high specificity and sensitivity. Using StCEL, we found that sialoglycoRNA was significantly upregulated in multiple cancer types. StCEL combined with a microplate reader was applied to detect sialoglycoRNA in large-scale samples, revealing that elevated sialoglycoRNA levels correlate positively with tumor malignancy and poor patient prognosis. Furthermore, StCEL-based sialoglycoRNA enrichment and sequencing identified dysregulated sialoglycoRNAs in tumor tissues. Collectively, StCEL establishes a multifunctional platform that enables sensitive and specific detection of sialoglycoRNA, alongside sequencing analysis, demonstrating significant potential for clinical translation.

molecular biology↗

bioRxiv2019

A systematic survey of PRMT interactomes reveals the key roles of arginine methylation in the global control of RNA splicing and translation

Thousands of proteins undergo arginine methylation, a widespread post-translational modification catalyzed by various protein arginine methyltransferases (PRMTs). However, a full picture of the catalytic network for each PRMT is lacking and the global understanding of their biological roles remains limited. Here we systematically identified interacting proteins for all human PRMTs and demonstrated that they are functionally important for mRNA splicing and translation. We showed that the interactomes of human PRMTs are significantly overlapped with the known methylarginine containing proteins, and different PRMTs are functionally complementary with a high degree of overlap in their substrates and high similarities between their putative methylation motifs. Importantly, arginine methylation is significantly enriched in RNA binding proteins involved in regulating RNA splicing and translation, and inhibition of PRMTs leads to global alteration of alternative splicing and suppression of translation. In particular, ribosomal proteins are pervasively modified with methylarginine, and mutations on their methylation sites suppress ribosome assembly, translation, and eventually cell growth. Collectively, our study provides a novel global view of different PRMT networks and uncovers critical functions of arginine methylation in the regulation of mRNA splicing and translation.

molecular biology↗