HECT ubiquitin ligase Smurf1 targets the tumor suppressor ING2 for ubiquitination and degradation

FEBS Letters
Jing NieLingqiang Zhang

Abstract

Inhibitor of growth 2 (ING2) gene encodes a candidate tumor suppressor and is frequently reduced in many tumors. However, the mechanisms underlying the regulation of ING2, in particular its protein stability, are still unclear. Here we show that the homologous to E6AP carboxyl terminus (HECT)-type ubiquitin ligase Smad ubiquitination regulatory factor 1 (Smurf1) interacts with and targets ING2 for poly-ubiquitination and proteasomal degradation. Intriguingly, the ING2 binding domain in Smurf1 was mapped to the catalytic HECT domain. Furthermore, the C-terminal PHD domain of ING2 was required for Smurf1-mediated degradation. This study provided the first evidence that the stability of ING2 could be regulated by ubiquitin-mediated degradation.

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Citations

Jun 10, 2011·Journal of Medicinal Chemistry·Michael D ShultzPeter Atadja
Aug 14, 2010·Carcinogenesis·Alberto MorenoIgnacio Palmero
Sep 26, 2012·Cellular and Molecular Life Sciences : CMLS·Yu Cao, Lingqiang Zhang
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Mar 23, 2018·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Fan HuLingqiang Zhang
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Mar 16, 2021·Frontiers in Oncology·Longtao YangHui Lin
Jan 24, 2019·Cancer Letters·Marjorie GournayRémy Pedeux

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