UBE2O remodels the proteome during terminal erythroid differentiation.
Science
; 357(6350)2017 08 04.
Article
em En
| MEDLINE
| ID: mdl-28774900
ABSTRACT
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.
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Ribossômicas
/
Células Eritroides
/
Enzimas de Conjugação de Ubiquitina
/
Eritropoese
/
Ubiquitinação
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article