ING4 inhibits the translation of proto‐oncogene MYC by interacting with AUF1
Copyright policy )ING4 inhibits the translation of proto‐oncogene MYC by interacting with AUF1
The ING4 tumor suppressor plays a significant role in various cancer‐related cellular processes. AUF1 affects the stability and/or translation of multiple mRNAs via binding to an AU‐rich element in the 3′‐untranslated regions. In this study, we identify AUF1 as a novel and direct binding partner of ING4. mRNP immunoprecipitation assays indicated that ING4, AUF1 and MYC mRNA present in the same mRNP complex. ING4 suppressed MYC protein expression without altering MYC mRNA levels, and abolished the cell proliferation induced by AUF1 in K562 cells. These results suggest that ING4 may regulate MYC translation by its association with AUF1.
- Tongji University School of Medicine China (People's Republic of)
- Second Military Medical University China (People's Republic of)
- Chinese National Human Genome Center China (People's Republic of)
- Tongji University China (People's Republic of)
- Chinese National Human Genome Center at Shanghai China (People's Republic of)
Translation, Nuclear Localization Signals, Cell Cycle Proteins, MYC, Proto-Oncogene Mas, ING4, Proto-Oncogene Proteins c-myc, AUF1, Humans, Immunoprecipitation, Protein Isoforms, Heterogeneous Nuclear Ribonucleoprotein D0, Protein Interaction Domains and Motifs, RNA, Messenger, Heterogeneous-Nuclear Ribonucleoprotein D, Cell proliferation, Cell Proliferation, Homeodomain Proteins, HEK293 Cells, Gene Expression Regulation, Ribonucleoproteins, Protein Biosynthesis, K562 Cells, HeLa Cells, Protein Binding
Translation, Nuclear Localization Signals, Cell Cycle Proteins, MYC, Proto-Oncogene Mas, ING4, Proto-Oncogene Proteins c-myc, AUF1, Humans, Immunoprecipitation, Protein Isoforms, Heterogeneous Nuclear Ribonucleoprotein D0, Protein Interaction Domains and Motifs, RNA, Messenger, Heterogeneous-Nuclear Ribonucleoprotein D, Cell proliferation, Cell Proliferation, Homeodomain Proteins, HEK293 Cells, Gene Expression Regulation, Ribonucleoproteins, Protein Biosynthesis, K562 Cells, HeLa Cells, Protein Binding
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