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Title 

Molecular interaction between HAX-1 and XIAP inhibits apoptosis

Authors 

Y J KangMi JangY K ParkSunghyun KangKwang-Hee BaeS ChoC K LeeByoung Chul ParkSeung-Wook ChiSung Goo Park

Publisher 

Elsevier

Issue Date 

2010

Citation 

Biochemical and Biophysical Research Communications, vol. 393, no. 4, pp. 794-799

Keywords 

ApoptosisHAX-1Protein interactionXIAP

Abstract 

Caspase-3 is an important executor caspase that plays an essential role in apoptosis. Recently, HS1-associated protein X1 (HAX-1) was found to be a substrate of caspase-3. Although HAX-1 has serve multifunctional roles in cellular functions such as cell survival and calcium homeostasis, the detailed functional mechanism of HAX-1 remains still unclear. In this study, we performed proteomic experiments to identify the HAX-1 interactome. Through immunoprecipitation and 2D gel electrophoresis, we identified X-linked inhibitor of apoptosis protein (XIAP) as a novel HAX-1-interacting protein. By performing the GST pull-down assay, we defined the interaction domains in HAX-1 and XIAP, showing that HAX-1 binds to the BIR2 and BIR3 domains of XIAP whereas XIAP binds to the C-terminal domain of HAX-1. In addition, surface plasma resonance experiments showed that both BIR2 and BIR3 domains of XIAP bind to HAX-1 with affinity similar to that of full-length XIAP, indicating that either domain is necessary and sufficient for tight binding to HAX-1. Taken together with the observation that HAX-1 suppresses the polyubiquitination of XIAP, the cell viability assay results suggest that the formation of the HAX-1-XIAP complex inhibits apoptosis by enhancing the stability of XIAP against proteosomal degradation.

ISSN 

0006-291X

Link 

http://dx.doi.org/10.1016/j.bbrc.2010.02.084

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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