A novel hPirh2 splicing variant without ubiquitin protein ligase activity interacts with p53 and is down-regulated in hepatocellular carcinoma.
A novel splice variant of hPirh2, named hPirh2b, was isolated from human fetal liver cDNA library. hPirh2b has a 38-nucleotide deletion and encodes a 188-amino acid protein with a truncated RING-H2 domain. It shows no ubiquitin protein ligase activity. A low level of expression of hPirh2 was found both at ... transcriptional and translational level in human hepatocellular carcinoma (HCC) when compared to non-cancerous tissue. Statistical analysis showed that the low expression is associated with lack of differentiation of HCC. In direct binding studies hPirh2b bound p53 indicating that RING-H2 domain is not needed for this interaction.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Blotting, Northern, Carcinoma, Hepatocellular, Glutathione Transferase, HeLa Cells, Humans, Immunohistochemistry, Immunoprecipitation, Liver, Liver Neoplasms, Molecular Sequence Data, Muscle, Skeletal, Myocardium, Pancreas, Protein Binding, RNA Splicing, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Tumor Suppressor Protein p53, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases
Amino Acid Sequence, Base Sequence, Blotting, Northern, Carcinoma, Hepatocellular, Glutathione Transferase, HeLa Cells, Humans, Immunohistochemistry, Immunoprecipitation, Liver, Liver Neoplasms, Molecular Sequence Data, Muscle, Skeletal, Myocardium, Pancreas, Protein Binding, RNA Splicing, Reverse Transcriptase Polymerase Chain Reaction, Sequence Homology, Amino Acid, Tumor Suppressor Protein p53, Two-Hybrid System Techniques, Ubiquitin-Protein Ligases
FEBS Lett.
Date: Jul. 02, 2010
PubMed ID: 20452352
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