Identification of a novel antiapoptotic protein that antagonizes ASK1 and CAD activities

Ssang Goo Cho; Jin Woo Kim; Yong Hee Lee; Hyun Sub Hwang; Mi Sung Kim; Kanghyun Ryoo; Myung Jin Kim; Kyung Tae Noh; Eun Kyung Kim; Jun Ho Cho; Kyoung Wan Yoon; Eun Gyung Cho; Hee Sae Park; Sung Wook Chi; Min Jae Lee; Sang Sun Kang; Hidenori Ichijo; Eui Ju Choi

doi:10.1083/jcb.200303003

Identification of a novel antiapoptotic protein that antagonizes ASK1 and CAD activities

Ssang Goo Cho, Jin Woo Kim, Yong Hee Lee, Hyun Sub Hwang, Mi Sung Kim, Kanghyun Ryoo, Myung Jin Kim, Kyung Tae Noh, Eun Kyung Kim, Jun Ho Cho, Kyoung Wan Yoon, Eun Gyung Cho, Hee Sae Park, Sung Wook Chi, Min Jae Lee, Sang Sun Kang, Hidenori Ichijo, Eui Ju Choi

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

38 Citations (Scopus)

Abstract

Diverse stimuli initiate the activation of apoptotic signaling pathways that often causes nuclear DNA fragmentation. Here, we report a new antiapoptotic protein, a caspase-activated DNase (CAD) inhibitor that interacts with ASK1 (CIIA). CIIA, by binding to apoptosis signal-regulating kinase 1 (ASK1), inhibits oligomerization-induced ASK1 activation. CIIA also associates with CAD and inhibits the nuclease activity of CAD without affecting caspase-3-mediated ICAD cleavage. Overexpressed CIIA reduces H₂O ₂- and tumor necrosis factor-α-induced apoptosis. CIIA antisense oligonucleotides, which abolish expression of endogenous CIIA in murine L929 cells, block the inhibitory effect of CIIA on ASK1 activation, deoxyribonucleic acid fragmentation, and apoptosis. These findings suggest that CIIA is an endogenous antagonist of both ASK1 - and CAD-mediated signaling.

Original language	English
Pages (from-to)	71-81
Number of pages	11
Journal	Journal of Cell Biology
Volume	163
Issue number	1
DOIs	https://doi.org/10.1083/jcb.200303003
Publication status	Published - 2003 Oct 13

Keywords

Apoptosis
Apoptosis signal-regulating kinase 1
C-Jun NH-terminal kinase
Caspase-activated DNase
Stress-activated protein kinase

ASJC Scopus subject areas

Cell Biology

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10.1083/jcb.200303003

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Cho, S. G., Kim, J. W., Lee, Y. H., Hwang, H. S., Kim, M. S., Ryoo, K., Kim, M. J., Noh, K. T., Kim, E. K., Cho, J. H., Yoon, K. W., Cho, E. G., Park, H. S., Chi, S. W., Lee, M. J., Kang, S. S., Ichijo, H., & Choi, E. J. (2003). Identification of a novel antiapoptotic protein that antagonizes ASK1 and CAD activities. Journal of Cell Biology, 163(1), 71-81. https://doi.org/10.1083/jcb.200303003

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abstract = "Diverse stimuli initiate the activation of apoptotic signaling pathways that often causes nuclear DNA fragmentation. Here, we report a new antiapoptotic protein, a caspase-activated DNase (CAD) inhibitor that interacts with ASK1 (CIIA). CIIA, by binding to apoptosis signal-regulating kinase 1 (ASK1), inhibits oligomerization-induced ASK1 activation. CIIA also associates with CAD and inhibits the nuclease activity of CAD without affecting caspase-3-mediated ICAD cleavage. Overexpressed CIIA reduces H2O 2- and tumor necrosis factor-α-induced apoptosis. CIIA antisense oligonucleotides, which abolish expression of endogenous CIIA in murine L929 cells, block the inhibitory effect of CIIA on ASK1 activation, deoxyribonucleic acid fragmentation, and apoptosis. These findings suggest that CIIA is an endogenous antagonist of both ASK1 - and CAD-mediated signaling.",

keywords = "Apoptosis, Apoptosis signal-regulating kinase 1, C-Jun NH-terminal kinase, Caspase-activated DNase, Stress-activated protein kinase",

author = "Cho, {Ssang Goo} and Kim, {Jin Woo} and Lee, {Yong Hee} and Hwang, {Hyun Sub} and Kim, {Mi Sung} and Kanghyun Ryoo and Kim, {Myung Jin} and Noh, {Kyung Tae} and Kim, {Eun Kyung} and Cho, {Jun Ho} and Yoon, {Kyoung Wan} and Cho, {Eun Gyung} and Park, {Hee Sae} and Chi, {Sung Wook} and Lee, {Min Jae} and Kang, {Sang Sun} and Hidenori Ichijo and Choi, {Eui Ju}",

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AU - Kim, Mi Sung

AU - Ryoo, Kanghyun

AU - Kim, Myung Jin

AU - Noh, Kyung Tae

AU - Kim, Eun Kyung

AU - Cho, Jun Ho

AU - Yoon, Kyoung Wan

AU - Cho, Eun Gyung

AU - Park, Hee Sae

AU - Chi, Sung Wook

AU - Lee, Min Jae

AU - Kang, Sang Sun

AU - Ichijo, Hidenori

AU - Choi, Eui Ju

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N2 - Diverse stimuli initiate the activation of apoptotic signaling pathways that often causes nuclear DNA fragmentation. Here, we report a new antiapoptotic protein, a caspase-activated DNase (CAD) inhibitor that interacts with ASK1 (CIIA). CIIA, by binding to apoptosis signal-regulating kinase 1 (ASK1), inhibits oligomerization-induced ASK1 activation. CIIA also associates with CAD and inhibits the nuclease activity of CAD without affecting caspase-3-mediated ICAD cleavage. Overexpressed CIIA reduces H2O 2- and tumor necrosis factor-α-induced apoptosis. CIIA antisense oligonucleotides, which abolish expression of endogenous CIIA in murine L929 cells, block the inhibitory effect of CIIA on ASK1 activation, deoxyribonucleic acid fragmentation, and apoptosis. These findings suggest that CIIA is an endogenous antagonist of both ASK1 - and CAD-mediated signaling.

AB - Diverse stimuli initiate the activation of apoptotic signaling pathways that often causes nuclear DNA fragmentation. Here, we report a new antiapoptotic protein, a caspase-activated DNase (CAD) inhibitor that interacts with ASK1 (CIIA). CIIA, by binding to apoptosis signal-regulating kinase 1 (ASK1), inhibits oligomerization-induced ASK1 activation. CIIA also associates with CAD and inhibits the nuclease activity of CAD without affecting caspase-3-mediated ICAD cleavage. Overexpressed CIIA reduces H2O 2- and tumor necrosis factor-α-induced apoptosis. CIIA antisense oligonucleotides, which abolish expression of endogenous CIIA in murine L929 cells, block the inhibitory effect of CIIA on ASK1 activation, deoxyribonucleic acid fragmentation, and apoptosis. These findings suggest that CIIA is an endogenous antagonist of both ASK1 - and CAD-mediated signaling.

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Identification of a novel antiapoptotic protein that antagonizes ASK1 and CAD activities

Abstract

Keywords

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