BPOZ-2 directly binds to eEF1A1 to promote eEF1A1 ubiquitylation and degradation and prevent translation

Genes Cells. 2008 Jun;13(6):593-607. doi: 10.1111/j.1365-2443.2008.01191.x. Epub 2008 Mar 4.

Abstract

Bood POZ containing gene type 2 (BPOZ-2), which contains ankyrin repeats, NLS, BTB/POZ domains and LXXLL motifs, is an adaptor protein for the E3 ubiquitin ligase scaffold protein CUL3. We isolated a cDNA encoding eukaryotic elongation factor 1A1 (eEF1A1) as a BPOZ-2 binding protein by screening a human thymus cDNA library using a yeast two-hybrid system. eEF1A1 is essential for translation and is also involved in the 26S proteasome-dependent degradation of misfolded or unfolded proteins. The binding between BPOZ-2 and eEF1A1 was confirmed by pull-down and immunoprecipitation assays in vitro and in vivo, respectively. BPOZ-2 binds to eEF1A1 through the ankyrin repeats and both BTB/POZ domains in BPOZ-2 and Domains I and III in eEF1A1. BPOZ-2 and eEF1A1 over-expressed in HEK 293T cells co-localized as speckles within the cytoplasm. BPOZ-2 promoted eEF1A1 ubiquitylation and degradation, suggesting that eEF1A1 is a substrate of BPOZ-2. BPOZ-2 inhibited GTP binding to eEF1A1 and prevented translation in in vitro translation assay using rabbit reticulocytes.

MeSH terms

  • Animals
  • COS Cells
  • Cattle
  • Cell Line
  • Cell-Free System
  • Chlorocebus aethiops
  • Humans
  • Mutagenesis, Site-Directed
  • Peptide Elongation Factor 1 / genetics
  • Peptide Elongation Factor 1 / metabolism*
  • Proteasome Endopeptidase Complex / metabolism
  • Protein Biosynthesis*
  • Repressor Proteins / metabolism*
  • Thymus Gland / metabolism
  • Transfection
  • Two-Hybrid System Techniques
  • Ubiquitination

Substances

  • ABTB1 protein, human
  • EEF1A1 protein, human
  • Peptide Elongation Factor 1
  • Repressor Proteins
  • Proteasome Endopeptidase Complex