期刊
FEBS LETTERS
卷 584, 期 14, 页码 3005-3012出版社
WILEY
DOI: 10.1016/j.febslet.2010.05.033
关键词
Inhibitor of growth 2; Tumor suppressor; Smad ubiquitination regulatory factor 1; Ubiquitination; Protein degradation
资金
- Program of China [2007CB914601, 2006CB910802, 2009CB918402, 2010CB912202]
- National Natural Science Foundation [30970601]
- National Key Technologies R&D Program for New Drugs [2009ZX09503-002, 2009ZX09301-002]
- State Key Laboratory of Proteomics [K200802]
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. Structured summary: MINT-7894271: ING2 (uniprotkb:Q9H160) binds (MI:0407) to Smurf1 (uniprotkb:Q9HCE7) by pull-down (MI:0096) MINT-7894319, MINT-7894339: ING2 (uniprotkb:Q9H160) physically interacts (MI:0915) with Smurf1 (uniprotkb:Q9HCE7) by anti tag co-immunoprecipitation (MI:0007) MINT-7894301: Smurf1 (uniprotkb:Q9HCE7) physically interacts (MI:0915) with ING2 (uniprotkb: Q9H160) by anti bait co-immunoprecipitation (MI:0006) MINT-7894358: ING1b (uniprotkb:Q9UK53-2) physically interacts (MI:0915) with Smurf1 (uniprotkb: Q9HCE7) by anti tag co-immunoprecipitation (MI:0007) MINT-7894249: ING2 (uniprotkb:Q9H160) physically interacts (MI:0915) with ubiquitin (uniprotkb: P62988) by anti tag co-immunoprecipitation (MI:0007) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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