Interaction between the Ret finger protein and the Int-6 gene product and co-localisation into nuclear bodies

J Cell Sci. 1999 Oct:112 ( Pt 19):3331-42. doi: 10.1242/jcs.112.19.3331.

Abstract

The mouse int-6 gene was identified in mammary tumors as an integration site for the mouse mammary tumor virus. Its human counterpart encodes a product that interacts with the Tax viral oncoprotein of the human T cell leukaemia virus type 1. This interaction impedes the localisation of over-expressed Int-6 in nuclear bodies containing the promyelocytic leukaemia gene product (PML). In this study, Int-6 is characterised as a 52 kDa protein that is localised within nuclear bodies in primary lymphocytes. Screening of a human B cell cDNA library for proteins that interact with Int-6 led to isolation of four clones coding for the p110 subunit of eIF3, in accordance with previous detection of Int-6 in purified forms of this translation initiation factor. Another clone was interesting with respect to the subcellular localisation of Int-6. It encodes the Ret finger protein (Rfp) which interacts with PML and localises within a subset of PML nuclear bodies. The interaction of Rfp with Int-6 is mediated through a region in Rfp designated 'Rfp domain', distinct from that involved in the interaction with PML. Int-6 and Rfp are co-localised in certain PML nuclear bodies in lymphocytes and transfection studies in HeLa cells strongly suggest that Rfp triggers translocation of Int-6 to nuclear bodies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Animals
  • COS Cells
  • Cell Nucleus / chemistry*
  • Cell Nucleus / genetics
  • DNA-Binding Proteins*
  • Eukaryotic Initiation Factor-3
  • Fluorescent Antibody Technique
  • Gene Deletion
  • HeLa Cells
  • Humans
  • Mice
  • Molecular Sequence Data
  • Mutagenesis / physiology
  • Nuclear Proteins / chemistry
  • Nuclear Proteins / genetics*
  • Nuclear Proteins / metabolism*
  • Protein Structure, Tertiary
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins / genetics*
  • Proto-Oncogene Proteins / metabolism*
  • Sequence Homology, Amino Acid
  • Transfection
  • Two-Hybrid System Techniques
  • Ubiquitin-Protein Ligases

Substances

  • DNA-Binding Proteins
  • Eukaryotic Initiation Factor-3
  • Nuclear Proteins
  • Proto-Oncogene Proteins
  • TRIM27 protein, human
  • Trim27 protein, mouse
  • Ubiquitin-Protein Ligases