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

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.

Pubmed ID: 18718448

Authors

  • Lee TL
  • Shyu YC
  • Hsu TY
  • Shen CK

Journal

Biochemical and biophysical research communications

Publication Data

October 24, 2008

Associated Grants

None

Mesh Terms

  • Cell Line
  • Cytoplasm
  • Humans
  • Lysine
  • NF-E2 Transcription Factor, p45 Subunit
  • Polyubiquitin
  • Repressor Proteins
  • Transcriptional Activation
  • Ubiquitin-Protein Ligases
  • Ubiquitination