Journal
CELL STEM CELL
Volume 11, Issue 6, Pages 783-798Publisher
CELL PRESS
DOI: 10.1016/j.stem.2012.09.011
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Funding
- National Institutes of Health [NIH]/National Cancer Institute [NCI) [P30 CA016087-30]
- NIH [RO1CA133379, RO1CA105129, RO1CA149655, RO1GM088847, 1U19A1091175-01, 1S10 RR023680-1]
- NYSTEM program of the New York State Health Department
- NYU Hematology/Oncology NIH training grant [5T32HL007151-33]
- NIH institutional training grant [1T32CA160002-01]
- Alexander von Humboldt Foundation
- NYSTEM institutional NYU Stem Cell training grant [C026880]
- Howard Hughes Medical Institute
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Although transcriptional regulation of stem cell pluripotency and differentiation has been extensively studied, only a small number of studies have addressed the roles for posttranslational modifications in these processes. A key mechanism of posttranslational modification is ubiquitination by the ubiquitin-proteasome system (UPS). Here, using shotgun proteomics, we map the ubiquitinated protein landscape during embryonic stem cell (ESC) differentiation and induced pluripotency. Moreover, using UPS-targeted RNAi screens, we identify additional 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 ESC pluripotency and cellular reprogramming. This global characterization of the UPS as a key regulator of stem cell pluripotency opens the way for future studies that focus on specific UPS enzymes or ubiquitinated substrates.
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