| First Author | Nguyen AT | Year | 2017 |
| Journal | Science | Volume | 357 |
| Issue | 6350 | PubMed ID | 28774900 |
| Mgi Jnum | J:243727 | Mgi Id | MGI:5911050 |
| Doi | 10.1126/science.aan0218 | Citation | Nguyen AT, et al. (2017) UBE2O remodels the proteome during terminal erythroid differentiation. Science 357(6350) |
| abstractText | During terminal differentiation, the global protein complement is remodeled, as epitomized by erythrocytes, whose cytosol is ~98% globin. The erythroid proteome undergoes a rapid transition at the reticulocyte stage; however, the mechanisms driving programmed elimination of preexisting cytosolic proteins are unclear. We found that a mutation in the murine Ube2o gene, which encodes a ubiquitin-conjugating enzyme induced during erythropoiesis, results in anemia. Proteomic analysis suggested that UBE2O is a broad-spectrum ubiquitinating enzyme that remodels the erythroid proteome. In particular, ribosome elimination, a hallmark of reticulocyte differentiation, was defective in Ube2o-/- mutants. UBE2O recognized ribosomal proteins and other substrates directly, targeting them to proteasomes for degradation. Thus, in reticulocytes, the induction of ubiquitinating factors may drive the transition from a complex to a simple proteome. |
