The ETS protein MEF is regulated by phosphorylation-dependent proteolysis via the protein-ubiquitin ligase SCFSkp2

Mol Cell Biol. 2006 Apr;26(8):3114-23. doi: 10.1128/MCB.26.8.3114-3123.2006.

Abstract

MEF is an ETS-related transcription factor with strong transcriptional activating activity that affects hematopoietic stem cell behavior and is required for normal NK cell and NK T-cell development. The MEF (also known as ELF4) gene is repressed by several leukemia-associated fusion transcription factor proteins (PML-retinoic acid receptor alpha and AML1-ETO), but it is also activated by retroviral insertion in several cancer models. We have previously shown that cyclin A-dependent phosphorylation of MEF largely restricts its activity to the G(1) phase of the cell cycle; we now show that MEF is a short-lived protein whose expression level also peaks during late G(1) phase. Mutagenesis studies show that the rapid turnover of MEF in S phase is dependent on the specific phosphorylation of threonine 643 and serine 648 at the C terminus of MEF by cdk2 and on the Skp1/Cul1/F-box (SCF) E3 ubiquitin ligase complex SCF(Skp2), which targets MEF for ubiquitination and proteolysis. Overexpression of MEF drives cells through the G(1)/S transition, thereby promoting cell proliferation. The tight regulation of MEF levels during the cell cycle contributes to its effects on regulating cell cycle entry and cell proliferation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Cell Line, Tumor
  • Cysteine Proteinase Inhibitors / pharmacology
  • DNA-Binding Proteins / analysis
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism*
  • Gene Expression Regulation
  • Half-Life
  • Humans
  • Hydrolysis
  • Leupeptins / pharmacology
  • Ligases / genetics
  • Ligases / metabolism*
  • Mutagenesis, Site-Directed
  • Phosphorylation
  • Proteins / genetics
  • Proteins / metabolism*
  • Serine / metabolism
  • Threonine / metabolism
  • Transcription Factors / analysis
  • Transcription Factors / chemistry
  • Transcription Factors / metabolism*
  • Ubiquitin / analysis
  • Ubiquitin / metabolism*

Substances

  • Cysteine Proteinase Inhibitors
  • DNA-Binding Proteins
  • ELF4 protein, human
  • Leupeptins
  • Proteins
  • Transcription Factors
  • Ubiquitin
  • Threonine
  • Serine
  • Ligases
  • benzyloxycarbonylleucyl-leucyl-leucine aldehyde