Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 375, Issue 3, Pages 326-330Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2008.07.164
Keywords
Itch; NF-E2; p45; Lys63-linkage; ubiquitin; HECT; E3 ligase; hematopoiesis; megakaryocytic; erythroid
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Funding
- National Health Research Institute (NHRI)
- Academia Sinica (AS), Taipei, Taiwan, ROC
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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. (C) 2008 Elsevier Inc. All rights reserved.
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