Itch regulates p45/NF-E2 in vivo by Lys63-linked ubiquitination

Tung Liang Lee, Yu Chiau Shyu, Ting Yin Hsu, Che Kun James Shen

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The hematopoietic-specific transcription factor p45/NF-E2 is an important transcriptional activator in the erythroid and megakaryocytic lineages. We describe the first in vivo evidence for the interaction between p45/NF-E2 and the E3 ubiquitin ligase Itch, and the subsequent ubiquitination of p45/NF-E2 by Itch. Interestingly, Itch suppressed the transactivation activity of p45/NF-E2 by adding a Lys63-linked polyubiquitin chain. Confocal microscopy revealed that ubiquitinated p45/NF-E2 became localized in the cytoplasm when Itch was over-expressed. Thus, Itch-mediated ubiquitination of p45/NF-E2 does not target the protein for proteasomal degradation, but instead retains p45/NF-E2 in the cytoplasm, where it cannot function as a transactivator. Finally, we suggest that this Itch-dependent p45/NF-E2 ubiquitination mechanism may regulate NF-E2 function during the development of hematopoietic cell lineages.

Original languageEnglish
Pages (from-to)326-330
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume375
Issue number3
DOIs
Publication statusPublished - Oct 24 2008
Externally publishedYes

Keywords

  • E3 ligase
  • Erythroid
  • HECT
  • Hematopoiesis
  • Itch
  • Lys63-linkage
  • Megakaryocytic
  • NF-E2
  • p45
  • Ubiquitin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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