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

Biochemical and Biophysical Research Communications
Tung-Liang LeeChe-Kun James Shen

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.

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Citations

Apr 17, 2013·The Journal of Experimental Medicine·Jonas S JutziHeike L Pahl
Oct 25, 2011·PloS One·Ana Leticia MaragnoChristine Tran Quang
Jun 13, 2015·Pulmonary Circulation·John Huetsch, Larissa A Shimoda
Jan 10, 2009·The EMBO Journal·Noula ShembadeEdward W Harhaj
Jun 19, 2015·Immunological Reviews·Daisuke AkiYun-Cai Liu
Feb 28, 2015·Cellular and Molecular Life Sciences : CMLS·Jadwiga J Gasiorek, Volker Blank
Jul 3, 2016·Journal of Translational Medicine·Yu-Chiau ShyuTing-Shuo Huang
Sep 20, 2018·Biomolecular NMR Assignments·Steven A BeasleyDonald E Spratt
Mar 14, 2020·Seminars in Cancer Biology·Qing YinLixin Wan
Jul 30, 2021·Frontiers in Oncology·Jinlu MaBo Xu

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