首页|RNPS1 stabilizes NAT10 protein to facilitate translation in cancer via tRNA ac4C modification
RNPS1 stabilizes NAT10 protein to facilitate translation in cancer via tRNA ac4C modification
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国家科技期刊平台
NETL
NSTL
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Existing studies have underscored the pivotal role of N-acetyltransferase 10(NAT10)in various cancers.However,the outcomes of protein-protein interactions between NAT10 and its protein partners in head and neck squamous cell carcinoma(HNSCC)remain unexplored.In this study,we identified a significant upregulation of RNA-binding protein with serine-rich domain 1(RNPS1)in HNSCC,where RNPS1 inhibits the ubiquitination degradation of NAT10 by E3 ubiquitin ligase,zinc finger SWIM domain-containing protein 6(ZSWIM6),through direct protein interaction,thereby promoting high NAT10 expression in HNSCC.This upregulated NAT10 stability mediates the enhancement of specific tRNA ac4C modifications,subsequently boosting the translation process of genes involved in pathways such as IL-6 signaling,IL-8 signaling,and PTEN signaling that play roles in regulating HNSCC malignant progression,ultimately influencing the survival and prognosis of HNSCC patients.Additionally,we pioneered the development of TRMC-seq,leading to the discovery of novel tRNA-ac4C modification sites,thereby providing a potent sequencing tool for tRNA-ac4C research.Our findings expand the repertoire of tRNA ac4C modifications and identify a role of tRNA ac4C in the regulation of mRNA translation in HNSCC.
Center For Translational Medicine,The First Affiliated Hospital,Sun Yat-sen University,Guangzhou,China
Institute for Advanced Study,Shenzhen University,Shenzhen,China
Hospital of Stomatology,Sun Yatsen UniversityNational Natural Science Foundation of ChinaNational Natural Science Foundation of ChinaGuangdong Basic and Applied Basic Research Foundation
国家科技期刊平台
NSTL
万方数据
