FEBS Letters
Volume 584, Issue 13 , Pages 2772-2778, 2 July 2010

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

Edited by Veli-Pekka Lehto

  • Gang Wu

      Affiliations

    • State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China
    • The authors contributed equally to this work.
    • ,
  • Meiqian Sun

      Affiliations

    • State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China
    • The authors contributed equally to this work.
    • ,
  • Liping Zhang

      Affiliations

    • State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China
    • ,
  • Juan Zhou

      Affiliations

    • State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China
    • ,
  • Yi Wang

      Affiliations

    • Department of Pathology, Shanghai Tenth People’s Hospital, Tongji University, Shanghai 200072, China
    • ,
  • Keke Huo

      Affiliations

    • State Key Laboratory of Genetic Engineering, Institute of Genetics, School of Life Sciences, Fudan University, Shanghai 200433, China
    • Corresponding Author InformationCorresponding author. Fax: +86 21 55664526.

Received 6 November 2009; received in revised form 13 April 2010; accepted 27 April 2010. published online 07 May 2010.

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.

Structured summary

MINT-7889990: NTKLBP1 (uniprotkb: Q5T7V8) physically interacts (MI:0915) with Pirh2b (uniprotkb:Q2KN33) by two-hybrid (MI:0018)

MINT-7890105: hPirh2b (uniprotkb:Q2KN33) physically interacts (MI:0915) with p53 (uniprotkb:P04637) by anti tag coimmunoprecipitation (MI:0007)

Abbreviations: hPirh2, human p53-induced RING-H2 protein, HCC, human hepatocellular carcinoma, ARNIP, androgen receptor N-terminal interacting protein, TMA, tissue microarray

Keywords: Pirh2, Splicing variant, Hepatocellular carcinoma, p53, Ubiquitin ligase

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PII: S0014-5793(10)00389-3

doi:10.1016/j.febslet.2010.04.075

FEBS Letters
Volume 584, Issue 13 , Pages 2772-2778, 2 July 2010

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