AIG1 is a novel Pirh2-interacting protein that activates the NFAT signaling pathway.

Pirh2 is an E3 ligase that negatively regulates p53 through both direct physical interaction and ubiquitin-mediated proteolysis. Here, we identified a novel Pirh2-interacting protein, AIG1, by yeast two-hybrid screening and confirmed its interaction with p53 both in vitro and in vivo. Quantitative real-time reverse transcription-PCR analysis showed that AIG1 expression ...
levels were reduced in 50 out of 79 (63%) human hepatocellular carcinomas (HCCs) when compared to matched, non-cancerous liver tissue; levels were significantly different between HCCs with or without lymph node metastasis. Kaplan-Meier analysis indicated that the survival time of HCC patients down-regulated for AIG1 is much shorter than it is for patients up-regulated for AIG1 expression (p = 0.0313 as determined by the Log-rank test). Finally, AIG1 activated the nuclear factor of activated T cells (NFAT) signaling pathway in a dose-dependent manner when over-expressed in HEK293T cells. Our results suggest AIG1 could serve as a new biomarker for the diagnosis and prognostic evaluation of HCCs.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Cell Line, DNA Primers, Female, Humans, Male, Membrane Proteins, Middle Aged, Molecular Sequence Data, NFATC Transcription Factors, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Signal Transduction, Subcellular Fractions, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases, Ubiquitination
Front Biosci (Elite Ed)
Date: May. 31, 2011
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