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Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme.
J Biol Chem. 2004 Dec 24; 279(52):54097-102.JB

Abstract

Ornithine decarboxylase (ODC) is the most notable example of a protein degraded by the 26 S proteasome without ubiquitination. Instead, ODC is targeted to degradation by direct binding to a polyamine-induced protein termed antizyme (Az). Antizyme inhibitor (AzI) is an ODC-related protein that does not retain enzymatic activity yet binds Az with higher affinity than ODC. We show here that like ODC, AzI is also a short-lived protein that undergoes proteasomal degradation. However, in contrast to ODC degradation, the degradation of AzI is ubiquitin-dependent and does not require interaction with Az. Moreover, Az binding actually stabilizes AzI by inhibiting its ubiquitination. Substituting the C terminus of AzI with that of ODC, which together with Az constitutes the complete degradation signal of ODC, does not subvert AzI degradation from the ubiquitin-dependent mode to the Az-dependent mode, suggesting dominance of the ubiquitination signal. Our results suggest opposing roles of Az in regulating the degradation of AzI and ODC.

Authors+Show Affiliations

Department of Molecular Genetics, The Weizmann Institute of Science, Rehovot 76100, Israel.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15491992

Citation

Bercovich, Zippi, and Chaim Kahana. "Degradation of Antizyme Inhibitor, an Ornithine Decarboxylase Homologous Protein, Is Ubiquitin-dependent and Is Inhibited By Antizyme." The Journal of Biological Chemistry, vol. 279, no. 52, 2004, pp. 54097-102.
Bercovich Z, Kahana C. Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme. J Biol Chem. 2004;279(52):54097-102.
Bercovich, Z., & Kahana, C. (2004). Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme. The Journal of Biological Chemistry, 279(52), 54097-102.
Bercovich Z, Kahana C. Degradation of Antizyme Inhibitor, an Ornithine Decarboxylase Homologous Protein, Is Ubiquitin-dependent and Is Inhibited By Antizyme. J Biol Chem. 2004 Dec 24;279(52):54097-102. PubMed PMID: 15491992.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Degradation of antizyme inhibitor, an ornithine decarboxylase homologous protein, is ubiquitin-dependent and is inhibited by antizyme. AU - Bercovich,Zippi, AU - Kahana,Chaim, Y1 - 2004/10/18/ PY - 2004/10/20/pubmed PY - 2005/3/15/medline PY - 2004/10/20/entrez SP - 54097 EP - 102 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 279 IS - 52 N2 - Ornithine decarboxylase (ODC) is the most notable example of a protein degraded by the 26 S proteasome without ubiquitination. Instead, ODC is targeted to degradation by direct binding to a polyamine-induced protein termed antizyme (Az). Antizyme inhibitor (AzI) is an ODC-related protein that does not retain enzymatic activity yet binds Az with higher affinity than ODC. We show here that like ODC, AzI is also a short-lived protein that undergoes proteasomal degradation. However, in contrast to ODC degradation, the degradation of AzI is ubiquitin-dependent and does not require interaction with Az. Moreover, Az binding actually stabilizes AzI by inhibiting its ubiquitination. Substituting the C terminus of AzI with that of ODC, which together with Az constitutes the complete degradation signal of ODC, does not subvert AzI degradation from the ubiquitin-dependent mode to the Az-dependent mode, suggesting dominance of the ubiquitination signal. Our results suggest opposing roles of Az in regulating the degradation of AzI and ODC. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/15491992/Degradation_of_antizyme_inhibitor_an_ornithine_decarboxylase_homologous_protein_is_ubiquitin_dependent_and_is_inhibited_by_antizyme_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=15491992 DB - PRIME DP - Unbound Medicine ER -