Hip2 interacts with and destabilizes Smac/DIABLO

Yoonhee Bae; Chang Won Kho; Soo Young Lee; Hyangshuk Rhim; Seongman Kang

doi:10.1016/j.bbrc.2010.06.016

Hip2 interacts with and destabilizes Smac/DIABLO

Yoonhee Bae, Chang Won Kho, Soo Young Lee, Hyangshuk Rhim, Seongman Kang

Department of Life Science

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

Hip2 is a ubiquitin-conjugating enzyme that is involved in the cell cycle and suppression of cell death. To understand its role further, we tried to identify proteins that interact with Hip2. Using the immunoprecipitation technique and one-dimensional gel electrophoresis, we identified Smac/DIABLO, a proapoptotic molecule, as a protein that interacts with Hip2. The interaction of Hip2 and Smac was confirmed through in vivo and in vitro experiments. Hip2 promoted degradation of mature Smac through the ubiquitin proteasome pathway. As a result, Hip2 significantly blocked cell death induced by staurosporine and Smac. This study suggests that Hip2 might be involved in the regulation of Smac-mediated apoptosis.

Original language	English
Pages (from-to)	718-723
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	397
Issue number	4
DOIs	https://doi.org/10.1016/j.bbrc.2010.06.016
State	Published - Jul 2010

Bibliographical note

Funding Information:
This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (200601742), (2007-0055395) and a grant from the Korea Healthcare Technology R&D Project, Ministry for Health, Welfare and Family Affairs, Republic of Korea (A084358).

Keywords

Apoptosis
Hip2
Smac
Ubiquitination

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10.1016/j.bbrc.2010.06.016

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title = "Hip2 interacts with and destabilizes Smac/DIABLO",

abstract = "Hip2 is a ubiquitin-conjugating enzyme that is involved in the cell cycle and suppression of cell death. To understand its role further, we tried to identify proteins that interact with Hip2. Using the immunoprecipitation technique and one-dimensional gel electrophoresis, we identified Smac/DIABLO, a proapoptotic molecule, as a protein that interacts with Hip2. The interaction of Hip2 and Smac was confirmed through in vivo and in vitro experiments. Hip2 promoted degradation of mature Smac through the ubiquitin proteasome pathway. As a result, Hip2 significantly blocked cell death induced by staurosporine and Smac. This study suggests that Hip2 might be involved in the regulation of Smac-mediated apoptosis.",

keywords = "Apoptosis, Hip2, Smac, Ubiquitination",

author = "Yoonhee Bae and Kho, {Chang Won} and Lee, {Soo Young} and Hyangshuk Rhim and Seongman Kang",

note = "Funding Information: This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (200601742), (2007-0055395) and a grant from the Korea Healthcare Technology R&D Project, Ministry for Health, Welfare and Family Affairs, Republic of Korea (A084358). ",

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doi = "10.1016/j.bbrc.2010.06.016",

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T1 - Hip2 interacts with and destabilizes Smac/DIABLO

AU - Bae, Yoonhee

AU - Kho, Chang Won

AU - Lee, Soo Young

AU - Rhim, Hyangshuk

AU - Kang, Seongman

N1 - Funding Information: This work was supported by the National Research Foundation of Korea (NRF) grant funded by the Korea government (200601742), (2007-0055395) and a grant from the Korea Healthcare Technology R&D Project, Ministry for Health, Welfare and Family Affairs, Republic of Korea (A084358).

PY - 2010/7

Y1 - 2010/7

N2 - Hip2 is a ubiquitin-conjugating enzyme that is involved in the cell cycle and suppression of cell death. To understand its role further, we tried to identify proteins that interact with Hip2. Using the immunoprecipitation technique and one-dimensional gel electrophoresis, we identified Smac/DIABLO, a proapoptotic molecule, as a protein that interacts with Hip2. The interaction of Hip2 and Smac was confirmed through in vivo and in vitro experiments. Hip2 promoted degradation of mature Smac through the ubiquitin proteasome pathway. As a result, Hip2 significantly blocked cell death induced by staurosporine and Smac. This study suggests that Hip2 might be involved in the regulation of Smac-mediated apoptosis.

AB - Hip2 is a ubiquitin-conjugating enzyme that is involved in the cell cycle and suppression of cell death. To understand its role further, we tried to identify proteins that interact with Hip2. Using the immunoprecipitation technique and one-dimensional gel electrophoresis, we identified Smac/DIABLO, a proapoptotic molecule, as a protein that interacts with Hip2. The interaction of Hip2 and Smac was confirmed through in vivo and in vitro experiments. Hip2 promoted degradation of mature Smac through the ubiquitin proteasome pathway. As a result, Hip2 significantly blocked cell death induced by staurosporine and Smac. This study suggests that Hip2 might be involved in the regulation of Smac-mediated apoptosis.

KW - Apoptosis

KW - Hip2

KW - Smac

KW - Ubiquitination

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 4

ER -

Hip2 interacts with and destabilizes Smac/DIABLO

Abstract

Bibliographical note

Keywords

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