Lin, Hung WeiHung WeiLinLee, Jin YuJin YuLeeChou, Nai LinNai LinChouShih, Ting WeiTing WeiShihMAU-SUN CHANG2021-09-142021-09-142021-08-0119326203https://scholars.lib.ntu.edu.tw/handle/123456789/582869Human PUF-A/PUM3 is a RNA and DNA binding protein participating in the nucleolar processing of 7S to 5.8S rRNA. The nucleolar localization of PUF-A redistributes to the nucleoplasm upon the exposure to genotoxic agents in cells. However, little is known regarding the roles of PUF-A in tumor progression. Phosphoprotein database analysis revealed that Y259 phosphorylation of PUF-A is the most prevalent residue modified. Here, we reported the importance of PUF-A's phosphorylation on Y259 in tumorigenesis. PUF-A gene was knocked out by the Crispr/Cas9 method in human cervix epithelial HeLa cells. Loss of PUF-A in HeLa cells resulted in reduced clonogenic and lower transwell invasion capacity. Introduction of PUF-AY259F to PUF-A deficient HeLa cells was unable to restore colony formation. In addition, the unphosphorylated mutant of PUF-A, PUF-AY259F, attenuated PUF-A protein stability. Our results suggest the important role of Y259 phosphorylation of PUF-A in cell proliferation.[SDGs]SDG3minor histocompatibility antigen; phosphoprotein; PUM3 protein, human; tyrosine; book; carcinogenesis; cell motion; cell proliferation; CRISPR Cas system; female; gene deletion; genetic database; genetics; HeLa cell line; human; metabolism; mortality; mutation; neoplasm; nucleolus; pathology; phosphorylation; protein processing; protein stability; survival analysis; Atlases as Topic; Carcinogenesis; Cell Movement; Cell Nucleolus; Cell Proliferation; CRISPR-Cas Systems; Databases, Genetic; Female; Gene Deletion; HeLa Cells; Humans; Minor Histocompatibility Antigens; Mutation; Neoplasms; Phosphoproteins; Phosphorylation; Protein Processing, Post-Translational; Protein Stability; Survival Analysis; Tyrosinejournal article10.1371/journal.pone.02562822-s2.0-85113328199https://api.elsevier.com/content/abstract/scopus_id/85113328199