HS 1-associated protein X-1 is cleaved by caspase-3 during apoptosis.
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 Asp(127), 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.
Lee
Ah Young
AY
Translational Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Korea.
Lee
Yoora
Y
Park
Yun Kyung
YK
Bae
Kwang-Hee
KH
Cho
Sayeon
S
Lee
Do Hee
DH
Park
Byoung Chul
BC
Kang
Sunghyun
S
Park
Sung Goo
SG
D048868:Adaptor Proteins, Signal Transducing; D017209:Apoptosis / Q000502:physiology*; D001224:Aspartic Acid / Q000378:metabolism; D001798:Blood Proteins / Q000235:genetics / Q000378:metabolism*; D053148:Caspase 3 / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D006801:Humans; D011506:Proteins / Q000235:genetics / Q000378:metabolism*
D048868:Adaptor Proteins, Signal Transducing; D001798:Blood Proteins; C104759:HAX1 protein, human; C061909:HCLS1 protein, human; D011506:Proteins; D001224:Aspartic Acid; D053148:Caspase 3