Caspase recruitment domain of procaspase-2 could be a target for SUMO-1 modification through Ubc9

Hiromi Shirakura, Naoko Hayashi, Shin Ichi Ogino, Kazuhiro Tsuruma, Takashi Uehara, Yasuyuki Nomura

Research output: Contribution to journalArticle

16 Citations (Scopus)


To identify the binding proteins that regulate the function of procaspase-2, we screened for proteins using the yeast two-hybrid method and isolated human Ubc9 and SUMO-1 as the candidates. Ubc9 and SUMO-1 interacted with the caspase recruitment domain of procaspase-2 in its N-terminal. We elucidated the covalent modification of procaspase-2 by SUMO-1 in mammalian cells by immunoprecipitation followed by Western blot analysis. Procaspase-2 and SUMO-1 were co-localized by dot-like structures in the nucleus that are related to promyelocytic leukemia bodies. Interestingly, a conjugation-deficient mutant (K60R) procaspase-2 resulted in a delay of its enzyme maturation (appearance of p12 subunit) compared to that of wild-type. Thus, the modification with SUMO-1 may play a critical role in the nuclear localization and the activation (maturation) of procaspase-2.

Original languageEnglish
Pages (from-to)1007-1015
Number of pages9
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - Jun 17 2005
Externally publishedYes



  • Apoptosis
  • Caspase-2
  • Dot-like structure
  • Nuclear localization
  • SUMO-1
  • Ubc9

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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