Reversible acetylation of Lin28 mediated by PCAF and SIRT1
| Autor: | Ling-xia Wang, Yu-fei Shen, Ye Zhang, Ting-ting Qu, Jing Wang |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Lin28
Blotting Western Fluorescent Antibody Technique Biology Real-Time Polymerase Chain Reaction LIN28 medicine.disease_cause SIRT1 Sirtuin 1 PCAF Protein stability medicine Humans Immunoprecipitation p300-CBP Transcription Factors RNA Messenger Luciferases Molecular Biology Reverse Transcriptase Polymerase Chain Reaction RNA-Binding Proteins Acetylation Cell Biology Cold-shock domain Cell biology HEK293 Cells Mutation Mutagenesis Site-Directed Cancer research Stem cell Carcinogenesis Protein Processing Post-Translational Reprogramming Biogenesis |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1843:1188-1195 |
| ISSN: | 0167-4889 |
| Popis: | Lin28 is a small RNA-binding protein that plays an important role in regulating developmental timing, stem cell reprogramming, and oncogenesis. However, the significance of the effect of post-translational modifications on Lin28 activity is not fully understood. In this study, we demonstrated that PCAF directly interacted with and acetylated Lin28. We also showed that the acetylation of Lin28 can be specifically reversed by the deacetylase SIRT1. These findings suggest that the PCAF/SIRT1 balance plays an important role in regulating Lin28 activity. Furthermore, we found that the cold shock domain of Lin28 is the major target of PCAF-mediated acetylation, which leads to a severe reduction in the Lin28 protein levels and an increase in the level of mature let-7a. This study provides the first demonstration that post-translational modification regulates Lin28 activity during let-7a biogenesis and sheds light on the regulation of Lin28 in ES cells and carcinogenesis. |
| Databáze: | OpenAIRE |
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