EKLF/KLF1 is ubiquitinated in vivo and its stability is regulated by activation domain sequences through the 26S proteasome

Karen J. Quadrini, James J. Bieker

Research output: Contribution to journalArticlepeer-review

24 Scopus citations

Abstract

Erythroid Krüppel-like factor (EKLF/KLF1) is an erythroid specific, C2H2 zinc finger transcription factor that is essential for the proper chromatin structure and expression of the adult β-globin gene. Herein, we determine that 26S proteasome inhibitors lead to an accumulation of EKLF protein in murine erythroleukemia (MEL) cells. In addition, EKLF half-life in both MEL cells (<3 h) and fetal liver cells (between 6 and 9 h) is stabilized in the presence of these inhibitors. EKLF is ubiquitinated in vivo, however its modification does not rely on a particular internal lysine. Finally, EKLF contains two PEST sequences within its N-terminus that have no effect on the ability of EKLF to be ubiquitinated but contribute to its destabilization.

Original languageEnglish
Pages (from-to)2285-2293
Number of pages9
JournalFEBS Letters
Volume580
Issue number9
DOIs
StatePublished - 17 Apr 2006

Keywords

  • Erythroid cells
  • PEST sequence
  • Transcription factor
  • Ubiquitin
  • Zinc finger protein

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