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

Journal Article · Fri Jun 17 04:00:00 EDT 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.04.019· OSTI ID:20710796

Shirakura, Hiromi ^[1]; Hayashi, Naoko ^[1]; Ogino, Shin-ichi ^[1]; Tsuruma, Kazuhiro ^[1]; Uehara, Takashi ^[1]; Nomura, Yasuyuki ^[1]

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1. Department of Pharmacology, Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812 (Japan)

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.

• OSTI ID: 20710796
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 4 Vol. 331; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

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