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Microb Cell. 2015 May 20;2(6):197-207. doi: 10.15698/mic2015.06.206.

Polyamines directly promote antizyme-mediated degradation of ornithine decarboxylase by the proteasome.

Microbial cell (Graz, Austria)

R R Beenukumar, Daniela Gödderz, R Palanimurugan, R J Dohmen

Affiliations

  1. Institute for Genetics, University of Cologne, Biocenter, Zülpicher Str. 47a, D-50674 Cologne, Germany.
  2. Institute for Genetics, University of Cologne, Biocenter, Zülpicher Str. 47a, D-50674 Cologne, Germany. ; Present address: Karolinska Institute, Department for Cell- and Molecular Biology, Von Eulers väg 3, 171 77 Stockholm.
  3. Institute for Genetics, University of Cologne, Biocenter, Zülpicher Str. 47a, D-50674 Cologne, Germany. ; Present address: Center for Cellular and Molecular Biology (CCMB), Uppal Road, Hyderabad 500007, India.

PMID: 28357293 PMCID: PMC5349141 DOI: 10.15698/mic2015.06.206

Abstract

Ornithine decarboxylase (ODC), a ubiquitin-independent substrate of the proteasome, is a homodimeric protein with a rate-limiting function in polyamine biosynthesis. Polyamines regulate ODC levels by a feedback mechanism mediated by ODC antizyme (OAZ). Higher cellular polyamine levels trigger the synthesis of OAZ and also inhibit its ubiquitin-dependent proteasomal degradation. OAZ binds ODC monomers and targets them to the proteasome. Here, we report that polyamines, aside from their role in the control of OAZ synthesis and stability, directly enhance OAZ-mediated ODC degradation by the proteasome. Using a stable mutant of OAZ, we show that polyamines promote ODC degradation in

Keywords: ODC; antizyme; polyamines; proteasome; ubiquitin

Conflict of interest statement

Conflict of interest: The authors declare no conflict of interest.

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