Phosphorylation of PUF-A/PUM3 on Y259 modulates PUF-A stability and cell proliferation

Autor: Nai-Lin Chou, Mau-Sun Chang, Ting-Wei Shih, Jin-Yu Lee, Hung-Wei Lin
Rok vydání: 2021
Předmět:
Carcinogenesis
Nucleolus
Cultured tumor cells
Biochemistry
HeLa
Aromatic Amino Acids
Cell Movement
Neoplasms
Databases
Genetic
Medicine and Health Sciences
Phosphorylation
Post-Translational Modification
Amino Acids
Multidisciplinary
biology
Protein Stability
Organic Compounds
Chemistry
Liver Diseases
Transfection
Precipitation Techniques
Cell biology
Nucleic acids
Ribosomal RNA
Oncology
Physical Sciences
Cell lines
Medicine
Female
Cellular Structures and Organelles
Biological cultures
Cell Nucleolus
Research Article
Science
Gastroenterology and Hepatology
Minor Histocompatibility Antigens
Atlases as Topic
Hydroxyl Amino Acids
Gastrointestinal Tumors
Humans
Immunoprecipitation
HeLa cells
Molecular Biology Techniques
Non-coding RNA
Clonogenic assay
Molecular Biology
Cell Proliferation
Cell Nucleus
Nucleoplasm
Cell growth
Carcinoma
Organic Chemistry
Chemical Compounds
Biology and Life Sciences
Proteins
Cancers and Neoplasms
Cell Biology
Hepatocellular Carcinoma
Phosphoproteins
Cell cultures
biology.organism_classification
Survival Analysis
Research and analysis methods
Phosphoprotein
Mutation
Tyrosine
RNA
CRISPR-Cas Systems
Protein Processing
Post-Translational
Ribosomes
Gene Deletion
Zdroj: PLoS ONE, Vol 16, Iss 8, p e0256282 (2021)
PLoS ONE
ISSN: 1932-6203
Popis: 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.
Databáze: OpenAIRE
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