Data from The Ubiquitin-specific Protease USP36 Associates with the Microprocessor Complex and Regulates miRNA Biogenesis by SUMOylating DGCR8

• DOI: 10.1158/2767-9764.c.6551239
• Publication Date: 2023-04-04T19:07:57Z
• Authors: Yanping Li; Timothy S. Carey; Catherine H. Feng; Hong-Ming Zhu; Xiao-Xin Sun; Mu-Shui Dai
• Keywords: Drosha; ribosome biogenesis; Dicer

<div><p>miRNA biogenesis is a cellular process that produces mature miRNAs from their primary transcripts, pri-miRNAs, via two RNAse III enzyme complexes: the Drosha-DGCR8 microprocessor complex in nucleus and Dicer-TRBP cytoplasm. Emerging evidence suggests miRNA tightly regulated by posttranscriptional posttranslational modifications aberrant associated with various human diseases including cancer. DGCR8 has been shown to be modified SUMOylation. Yet, SUMO ligase mediating SUMOylation currently unknown. Here, we report USP36, nucleolar ubiquitin-specific protease essential for ribosome biogenesis, novel regulator of DGCR8. USP36 interacts promotes SUMOylation, specifically SUMO2. USP36-mediated does not affect levels formation complex, but binding pri-miRNAs. Consistently, abolishing significantly attenuates its pri-miRNAs knockdown pri-miRNA processing, resulting marked reduction tested miRNAs. Induced expression SUMOylation-defective mutant inhibits cell proliferation. Together, these results suggest plays an important role regulating SUMOylating DGCR8.</p>Significance:<p>This study identifies mediates SUMO2 critical biogenesis. As frequently overexpressed cancers, our deregulated USP36-miRNA pathway may contribute tumorigenesis.</p></div>