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

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.
Mesh Terms:
Blotting, Western, Caspase 2, Caspases, Enzyme Activation, SUMO-1 Protein, Two-Hybrid System Techniques, Ubiquitin-Conjugating Enzymes
Biochem. Biophys. Res. Commun. Jun. 17, 2005; 331(4);1007-15 [PUBMED:15882978]
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