AI Article Synopsis
- PUF-A/PUM3 is a crucial RNA and DNA binding protein involved in the processing of rRNA, with its localization shifting from the nucleolus to the nucleoplasm in response to DNA damage.
- The study highlights that phosphorylation at residue Y259 of PUF-A is significant for tumor progression, as knocking out PUF-A in HeLa cells led to decreased growth and invasive capabilities.
- The introduction of a mutant PUF-A that could not be phosphorylated (PUF-AY259F) failed to restore colony formation and reduced the protein's stability, indicating that Y259 phosphorylation is vital for cell proliferation.
Article Abstract
Human 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.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8372891 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0256282 | PLOS |
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