Wdr26 regulates nuclear condensation in developing erythroblasts

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journal

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Author(s)

  • Ru Zhen
  • Zhenzhen Zhao
  • Mengying Chen
  • He Feng
  • Xiaojun Zheng
  • Caiyong Chen

Detail(s)

Original languageEnglish
Pages (from-to)208–219
Journal / PublicationBlood
Volume135
Issue number3
Online published7 Nov 2019
Publication statusPublished - 16 Jan 2020

Abstract

Mammalian red blood cells lack nuclei. The molecular mechanisms underlying erythroblast nuclear condensation and enucleation, however, remain poorly understood. Here we show that Wdr26, a gene upregulated during terminal erythropoiesis, plays an essential role in regulating nuclear condensation in differentiating erythroblasts. Loss of Wdr26 induces anemia in zebrafish and enucleation defects in mouse erythroblasts because of impaired erythroblast nuclear condensation. As part of the glucose-induced degradation-deficient ubiquitin ligase complex, Wdr26 regulates the ubiquitination and degradation of nuclear proteins, including lamin B. Failure of lamin B degradation blocks nuclear opening formation leading to impaired clearance of nuclear proteins and delayed nuclear condensation. Collectively, our study reveals an unprecedented role of an E3 ubiquitin ligase in regulating nuclear condensation and enucleation during terminal erythropoiesis. Our results provide mechanistic insights into nuclear protein homeostasis and vertebrate red blood cell development.

Citation Format(s)

Wdr26 regulates nuclear condensation in developing erythroblasts. / Zhen, Ru; Moo, Chingyee; Zhao, Zhenzhen; Chen, Mengying; Feng, He; Zheng, Xiaojun; Zhang, Liang; Shi, Jiahai; Chen, Caiyong.

In: Blood, Vol. 135, No. 3, 16.01.2020, p. 208–219.

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journal