Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1843, Issue 6, Pages 1188-1195Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2014.03.001
Keywords
Lin28; PCAF; SIRT1; Acetylation; Protein stability
Categories
Funding
- National Key Scientific Program of China [2011CB964902]
- National Natural Science Foundation of China [31171239]
- Special Funds of the State Key Laboratories [2060204]
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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. (C) 2014 Elsevier B.V. All rights reserved.
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