| Literature DB >> 26292759 |
J Wang1, Y Zhang1, J Hou1, X Qian1, H Zhang1, Z Zhang1, M Li1, R Wang1, K Liao1, Y Wang1, Z Li1, D Zhong1, P Wan1, L Dong2, F Liu3, X Wang2, Y Wan3, W Xiao1, W W Zhang1.
Abstract
Sox2 has a critical role in embryonic stem (ES) cell maintenance and differentiation. Interestingly, its activity is highly dosage-dependent. Although transcriptional regulation of Sox2 has been extensively studied, the mechanisms orchestrating its degradation remain unclear. In this study, we identified ubiquitin-conjugating enzyme E2S (Ube2s) as a novel effector for Sox2 protein degradation. Ube2s mediates K11-linked polyubiquitin chain formation at the Sox2-K123 residue, thus marking it for proteasome-mediated degradation. Besides its role in fine-tuning the precise level of Sox2, Ube2s reinforces the self-renewing and pluripotent state of ES cells. Importantly, it also represses Sox2-mediated ES cell differentiation toward the neural ectodermal lineage.Entities:
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Year: 2015 PMID: 26292759 PMCID: PMC5072435 DOI: 10.1038/cdd.2015.106
Source DB: PubMed Journal: Cell Death Differ ISSN: 1350-9047 Impact factor: 15.828