Journal
SCIENCE
Volume 357, Issue 6350, Pages -Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aan0218
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Funding
- NIH [5R21HL116210, 5R01HL125710, T32GM007753, HL124980, DK098285, U01 HD39372, R01 CA115503]
- Biogen-Idec [6780680-01]
- Diamond Blackfan Anemia Foundation
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During terminal differentiation, the global protein complement is remodeled, as epitomized by erythrocytes, whose cytosol is similar to 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.
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