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Research Article

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Mol. Cells 2008; 25(1): 86-90

Published online January 1, 1970

© The Korean Society for Molecular and Cellular Biology

HS 1-Associated Protein X-1 Is Cleaved by Caspase-3 During Apoptosis

Ah Young Lee, Yoora Lee, Yun Kyung Park, Kwang-Hee Bae, Sayeon Cho and Do Hee Lee

Abstract

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Caspase-3 (CASP3) plays a key role in apoptosis. In this study, HAX-1 was identified as a new substrate of CASP3 during apoptosis. HAX-1 was cleaved by CASP3 during etoposide-(ETO) induced apoptosis, and this event was inhibited by a CASP3-specific inhibitor. The cleavage site of HAX-1, at Asp127, was located using N-terminal amino acid sequencing of in vitro cleavage products of recombinant HAX-1. Overexpression of HAX-1 inhibited ETO-induced apoptotic cell death. It also inhibited CASP3 activity. Together, these results suggest that HAX-1, a substrate of CASP3, inhibits the apoptotic process by inhibiting CASP3 activity.

Keywords Apoptosis, Caspase-3, HAX-1

Article

Research Article

Mol. Cells 2008; 25(1): 86-90

Published online February 29, 2008

Copyright © The Korean Society for Molecular and Cellular Biology.

HS 1-Associated Protein X-1 Is Cleaved by Caspase-3 During Apoptosis

Ah Young Lee, Yoora Lee, Yun Kyung Park, Kwang-Hee Bae, Sayeon Cho and Do Hee Lee

Abstract

Caspase-3 (CASP3) plays a key role in apoptosis. In this study, HAX-1 was identified as a new substrate of CASP3 during apoptosis. HAX-1 was cleaved by CASP3 during etoposide-(ETO) induced apoptosis, and this event was inhibited by a CASP3-specific inhibitor. The cleavage site of HAX-1, at Asp127, was located using N-terminal amino acid sequencing of in vitro cleavage products of recombinant HAX-1. Overexpression of HAX-1 inhibited ETO-induced apoptotic cell death. It also inhibited CASP3 activity. Together, these results suggest that HAX-1, a substrate of CASP3, inhibits the apoptotic process by inhibiting CASP3 activity.

Keywords: Apoptosis, Caspase-3, HAX-1

Mol. Cells
Jun 30, 2023 Vol.46 No.6, pp. 329~398
COVER PICTURE
The cellular proteostasis network is adaptively modulated upon cellular stress, thereby protecting cells from proteostasis collapse. Heat shock induces the translocation of misfolded proteins and the chaperone protein HSP70 into nucleolus, where nuclear protein quality control primarily occurs. Nuclear RNA export factor 1 (green), nucleolar protein fibrillarin (red), and nuclei (blue) were visualized in NIH3T3 cells under basal (left) and heat shock (right) conditions (Park et al., pp. 374-386).
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