Redox-mediated modification of PLZF by SUMO-1 and ubiquitin

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17 Citations (Scopus)


Earlier, we reported that the transcriptional repressor promyelocytic leukemia zinc-finger protein (PLZF) is sumoylated at position K242, and the sumoylation regulated its biological function. Here, we show that the sumoylation site can be modified by ubiquitin. The stability and nuclear localization of PLZF were regulated by the antagonistic relationship between sumoylation and ubiquitination. We observed the antagonistic effects of ubiquitin and SUMO-1 on PLZF under oxidative stress induced by serum deprivation. Thus, the choice between modification of PLZF by SUMO or ubiquitin was determined by the intracellular level of ROS, which was generated by serum deprivation that inactivated the SUMO-conjugating enzymes Uba2 and Ubc9, and resulted in decrease of sumoylation. The ubiquitination was increased under these conditions. The expression of BID, a known transcriptional target protein of PLZF, was decreased, and the consequent apoptosis was induced by the ROS generated during serum starvation. On the basis of these results, we propose that PLZF post-translational modification is controlled by intracellular ROS, and the biological function of PLZF is regulated by sumoylation and ubiquitination.

Original languageEnglish
Pages (from-to)1209-1214
Number of pages6
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2008 May 16

Bibliographical note

Funding Information:
We thank Dr. J.D. Licht and Dr. R.T. Hay for plasmid constructs and advice. We thank Dr. M. Ruthardt for plasmid constructs and discussion. This work was supported by a Korea Science and Engineering Foundation (KOSEF) grant funded by the Korea Government (MOST) (R01-2007-000-10505-0) and by a special intramural grant from Korea University.


  • PLZF
  • ROS
  • SUMO
  • Serum deprivation
  • Ubiquitin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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