RNF38 encodes a nuclear ubiquitin protein ligase that modifies p53

Biochem Biophys Res Commun. 2013 Nov 1;440(4):473-8. doi: 10.1016/j.bbrc.2013.08.031. Epub 2013 Aug 22.

Abstract

The RNF38 gene encodes a RING finger protein of unknown function. Here we demonstrate that RNF38 is a functional ubiquitin protein ligase (E3). We show that RNF38 isoform 1 is localized to the nucleus by a bipartite nuclear localization sequence (NLS). We confirm that RNF38 is a binding partner of p53 and demonstrate that RNF38 can ubiquitinate p53 in vitro and in vivo. Finally, we show that overexpression of RNF38 in HEK293T cells results in relocalization of p53 to discrete foci associated with PML nuclear bodies. These results suggest RNF38 is an E3 ubiquitin ligase that may play a role in regulating p53.

Keywords: E3; PML nuclear bodies; RNF38; Ubiquitin protein ligase; p53.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Nucleus / enzymology*
  • HEK293 Cells
  • Humans
  • Intranuclear Inclusion Bodies / enzymology
  • Molecular Sequence Data
  • Nuclear Localization Signals / genetics
  • Nuclear Localization Signals / metabolism
  • Nuclear Proteins / metabolism
  • Promyelocytic Leukemia Protein
  • Transcription Factors / metabolism
  • Tumor Suppressor Proteins / metabolism
  • Ubiquitin-Protein Ligases / genetics
  • Ubiquitin-Protein Ligases / metabolism*
  • Ubiquitination
  • Zinc Fingers

Substances

  • Carrier Proteins
  • Nuclear Localization Signals
  • Nuclear Proteins
  • Promyelocytic Leukemia Protein
  • RNF38 protein, human
  • Transcription Factors
  • Tumor Suppressor Proteins
  • PML protein, human
  • Ubiquitin-Protein Ligases