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. 2007 Dec;17(12):1020-9.
doi: 10.1038/cr.2007.99.

Oncoprotein p28 GANK binds to RelA and retains NF-kappaB in the cytoplasm through nuclear export

Yao Chen  1 , Hong Hai Li, Jing Fu, Xue Feng Wang, Yi Bin Ren, Li Wei Dong, Shan Hua Tang, Shu Qing Liu, Meng Chao Wu, Hong Yang Wang
Affiliations

Oncoprotein p28 GANK binds to RelA and retains NF-kappaB in the cytoplasm through nuclear export

Yao Chen et al. Cell Res. 2007 Dec.

Abstract

p28(GANK) (also known as PSMD10, p28 and gankyrin) is an ankyrin repeat anti-apoptotic oncoprotein that is commonly overexpressed in hepatocellular carcinomas and increases the degradation of p53 and Rb. NF-kappaB (nuclear factor-kappaB) is known to be sequestered in the cytoplasm by I kappaB (inhibitor of NF-kappaB) proteins, but much less is known about the cytoplasmic retention of NF-kappaB by other cellular proteins. Here we show that p28(GANK) inhibits NF-kappaB activity. As a nuclear-cytoplasmic shuttling protein, p28(GANK) directly binds to NF-kappaB/RelA and exports RelA from nucleus through a chromosomal region maintenance-1 (CRM-1) dependent pathway, which results in the cytoplasmic retention of NF-kappaB/RelA. We demonstrate that all the ankyrin repeats of p28(GANK) are required for the interaction with RelA and that the N terminus of p28(GANK), which contains the nuclear export sequence (NES), is responsible for suppressing NF-kappaB/RelA nuclear translocation. These results suggest that overexpression of p28(GANK) prevents the nuclear localization and inhibits the activity of NF-kappaB/RelA.

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