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Regulation of Pluripotency and Cellular Reprogramming by the Ubiquitin-Proteasome System
Open accessAbstract
SUMMARY While transcriptional regulation of stem cell pluripotency and differentiation has been extensively studied, only a small number of studies have addressed the roles for post-translational modifications in these processes. A key mechanism of post-translational modification is ubiquitination by the ubiquitin-proteasome system (UPS). Here we map, using shotgun proteomics, the ubiquitinated protein landscape during ES cell differentiation and induced pluripotency. Moreover, using UPS-targeted RNAi screens, we identify novel regulators of pluripotency and differentiation. We focus on two of these proteins, the deubiquitinating enzyme, Psmd14, and the E3 ligase, Fbxw7, and characterize their importance in ES cell pluripotency and cellular reprogramming. This is the first global characterization of the UPS as a key regulator of stem cell pluripotency, opening the way for future studies that focus on specific UPS enzymes or ubiquitinated substrates.
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Metadata
- Authors
- Buckley, S. M., Aranda-Orgilles, B., Strikoudis, A., Apostolou, E., Loizou, E., Moran-Crusio, K., Farnsworth, C. L., Koller, A. A., Dasgupta, R., Silva, J. C., Stadtfeld, M., Hochedlinger, K., Chen, E. I., & Aifantis, I.
- Venue
- Cell Stem Cell
- Publisher
- Elsevier BV
- Published
- 2012-12
- Volume
- 11
- Issue
- 6
- Pages
- 783-798
- ISSN
- 1875-9777 (ISSN-L)
- 1934-5909
- OpenAlex
- W2024551920
- Cited by
- 272
- References
- 47
- FWCI
- 7.43
- Type
- journal article
- Language
- en
- Open access
- bronze
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