Profiling the regulatory landscape of sialylation through miRNA targeting of CMP- sialic acid synthetase.

ABSTRACT: Cell surface sialic acid is an important glycan modification that contributes to both normal and pathological physiology. The enzyme cytidine monophosphate N-acetylneuraminic acid synthetase (CMAS) biosynthesizes the activated sugar donor cytidine monophosphate (CMP) sialic acid, which is required for all sialylation. CMAS levels impact sialylation with corresponding biological effects. The mechanisms that regulate CMAS are relatively uncharacterized. Herein, we use a high throughput genetically encoded fluorescence assay (miRFluR) to comprehensively profile the posttranscriptional regulation of CMAS by miRNA. These small non-coding RNAs have been found to impact glycosylation. Mapping the interactions of the human miRNAome with the 3'-untranslated region of CMAS, we identified miRNA whose

SUBMITTER: Jame-Chenarboo F 

PROVIDER: S-EPMC11982980 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature