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

doi:10.1016/j.bbrc.2005.04.019

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 journal › Article › peer-review

18 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	1007-1015
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	331
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2005.04.019
Publication status	Published - Jun 17 2005
Externally published	Yes

Keywords

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

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2005.04.019

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

abstract = "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.",

keywords = "Apoptosis, Caspase-2, Dot-like structure, Nuclear localization, SUMO-1, Ubc9",

author = "Hiromi Shirakura and Naoko Hayashi and Ogino, {Shin Ichi} and Kazuhiro Tsuruma and Takashi Uehara and Yasuyuki Nomura",

note = "Funding Information: We are grateful to Dr. Shinji Kamada and Prof. Yoshihide Tsujimoto (Osaka University) for providing us with the mutant procaspase-1 and -4 plasmid DNAs. We thank Prof. Hiroyoshi Ariga and Dr. Takahiro Taira (Hokkaido University) for providing us with the Ubc9 construct. This study was supported by a Grant-in-Aid for scientific research from the Ministry of Education, Science, Sports and Culture of Japan.",

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AU - Shirakura, Hiromi

AU - Hayashi, Naoko

AU - Ogino, Shin Ichi

AU - Tsuruma, Kazuhiro

AU - Uehara, Takashi

AU - Nomura, Yasuyuki

N1 - Funding Information: We are grateful to Dr. Shinji Kamada and Prof. Yoshihide Tsujimoto (Osaka University) for providing us with the mutant procaspase-1 and -4 plasmid DNAs. We thank Prof. Hiroyoshi Ariga and Dr. Takahiro Taira (Hokkaido University) for providing us with the Ubc9 construct. This study was supported by a Grant-in-Aid for scientific research from the Ministry of Education, Science, Sports and Culture of Japan.

PY - 2005/6/17

Y1 - 2005/6/17

N2 - 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.

AB - 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.

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

Abstract

Keywords

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