Cell cycle-dependent expression of mammalian E2-C regulated by the anaphase-promoting complex/cyclosome

A. Yamanaka, S. Hatakeyama, K. I. Kominami, M. Kitagawa, M. Matsumoto, K. I. Nakayama

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46 Citations (Scopus)


Progression through mitosis requires the precisely timed ubiquitin-dependent degradation of specific substrates. E2-C is a ubiquitin-conjugating enzyme that plays a critical role with anaphase-promoting complex/cyclosome (APC/C) in progression of and exit from M phase. Here we report that mammalian E2-C is expressed in late G2/M phase and is degraded as cells exit from M phase. The mammalian E2-C shows an autoubiquitinating activity leading to covalent conjugation to itself with several ubiquitins. The ubiquitination of E2-C is strongly enhanced by APC/C, resulting in the formation of a polyubiquitin chain. The polyubiquitination of mammalian E2-C occurs only when cells exit from M phase. Furthermore, mammalian E2-C contains two putative destruction boxes that are believed to act as recognition motifs for APC/C. The mutation of this motif reduced the polyubiquitination of mammalian E2-C, resulting in its stabilization. These results suggest that mammalian E2-C is itself a substrate of the APC/C-dependent proteolysis machinery, and that the periodic expression of mammalian E2-C may be a novel autoregulatory system for the control of the APC/C activity and its substrate specificity.

Original languageEnglish
Pages (from-to)2821-2831
Number of pages11
JournalMolecular biology of the cell
Issue number8
Publication statusPublished - 2000

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology


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