| First Author | Lee TL | Year | 2008 |
| Journal | Biochem Biophys Res Commun | Volume | 375 |
| Issue | 3 | Pages | 326-30 |
| PubMed ID | 18718448 | Mgi Jnum | J:141028 |
| Mgi Id | MGI:3815262 | Doi | 10.1016/j.bbrc.2008.07.164 |
| Citation | Lee TL, et al. (2008) Itch regulates p45/NF-E2 in vivo by Lys63-linked ubiquitination. Biochem Biophys Res Commun 375(3):326-30 |
| abstractText | 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. |
