A novel hPirh2 splicing variant without ubiquitin protein ligase activity interacts with p53 and is down-regulated in hepatocellular carcinoma

FEBS Lett. 2010 Jul 2;584(13):2772-8. doi: 10.1016/j.febslet.2010.04.075. Epub 2010 May 7.

Authors

Gang Wu¹, Meiqian Sun, Liping Zhang, Juan Zhou, Yi Wang, Keke Huo

Affiliation

¹ State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai, China.

PMID: 20452352
DOI: 10.1016/j.febslet.2010.04.075

Abstract

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Base Sequence
Blotting, Northern
Carcinoma, Hepatocellular / metabolism*
Glutathione Transferase / metabolism
HeLa Cells
Humans
Immunohistochemistry
Immunoprecipitation
Liver / metabolism
Liver Neoplasms / metabolism*
Molecular Sequence Data
Muscle, Skeletal / metabolism
Myocardium / metabolism
Pancreas / metabolism
Protein Binding
RNA Splicing / genetics
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Tumor Suppressor Protein p53 / genetics
Tumor Suppressor Protein p53 / metabolism*
Two-Hybrid System Techniques
Ubiquitin-Protein Ligases / chemistry
Ubiquitin-Protein Ligases / genetics
Ubiquitin-Protein Ligases / metabolism*

Substances

Tumor Suppressor Protein p53
RCHY1 protein, human
Ubiquitin-Protein Ligases
Glutathione Transferase