Nuclear LYRIC/AEG-1 interacts with PLZF and relieves PLZF-mediated repression

Oncogene. 2009 Oct 15;28(41):3663-70. doi: 10.1038/onc.2009.223. Epub 2009 Aug 3.

Abstract

LYRIC/AEG-1 and its altered expression have been linked to carcinogenesis in prostate, brain and melanoma as well as promoting chemoresistance and metastasis in breast cancer. LYRIC/AEG-1 function remains unclear, although LYRIC/AEG-1 is activated by oncogenic HA-RAS, through binding of c-myc to its promoter, which in turn regulates the key components of the PI3-kinase and nuclear factor-kappaB pathways. We have identified the transcriptional repressor PLZF as an interacting protein of LYRIC/AEG through a yeast two-hybrid screen. PLZF regulates the expression of genes involved in cell growth and apoptosis including c-myc. Coexpression of LYRIC/AEG-1 with PLZF leads to a reduction in PLZF-mediated repression by reducing PLZF binding to promoters. We have confirmed that nuclear LYRIC/AEG-1 and PLZF interact in mammalian cells via the N- and C termini of LYRIC/AEG-1 and a region C terminal to the RD2 domain of PLZF. Both proteins colocalize to nuclear bodies containing histone deacetylases, which are known to promote PLZF-mediated repression. Our data suggest one mechanism for cells with altered LYRIC/AEG-1 expression to evade apoptosis and increase cell growth during tumourigenesis through the regulation of PLZF repression.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Adhesion Molecules / metabolism*
  • Cell Nucleus / metabolism*
  • Gene Expression Regulation
  • HeLa Cells
  • Histone Deacetylases / metabolism
  • Humans
  • Kruppel-Like Transcription Factors / chemistry
  • Kruppel-Like Transcription Factors / genetics
  • Kruppel-Like Transcription Factors / metabolism*
  • Membrane Proteins
  • Promyelocytic Leukemia Zinc Finger Protein
  • Protein Structure, Tertiary
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA-Binding Proteins
  • Transcription, Genetic

Substances

  • Cell Adhesion Molecules
  • Kruppel-Like Transcription Factors
  • MTDH protein, human
  • Membrane Proteins
  • Promyelocytic Leukemia Zinc Finger Protein
  • RNA, Messenger
  • RNA-Binding Proteins
  • ZBTB16 protein, human
  • Histone Deacetylases