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Proceedings Paper

PUMA promotes Bax translocation by competitive binding to Bcl-Xl during UV-induced apoptosis
Author(s): Yingjie Zhang; Da Xing; Yinyuan Wu; Lei Liu
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Paper Abstract

Ultraviolet (UV) irradiation can induce apoptosis through both the membrane death receptor and the intrinsic apoptotic signaling pathways as DNA-damaging agents. PUMA, a BH3-only Bcl-2 family protein, plays an essential role in DNA damage-induced apoptosis. Bax, also a Bcl-2 family member, translocates from the cytosol to the mitochondrial membrane during UV-induced apoptosis. However, the regulation of Bax activation induced by UV irradiation remains poorly understood. In this study, the FRET (fluorescence resonance energy transfer) technique was used to study the interactions of Bax, Bcl-Xl, and PUMA in ASTC-a-1 cells. The results show that Bax translocated from the cytosol to the mitochondrial membrane at about 7 h after UV irradiation, and the translocation can not be blocked completely when overexpressed Bcl-xl. Moreover, The interaction of Bax and Bcl-Xl weakened markedly. In addition, Co-immunoprecipitation shows that PUMA released Bax by directly binding to Bcl-XL after UV irradiation in ASTC-a-1 cells. Taken together, these results indicated that PUMA can promote Bax translocation by binding to Bcl-Xl during UV-induced apoptosis.

Paper Details

Date Published: 18 February 2008
PDF: 10 pages
Proc. SPIE 6857, Biophotonics and Immune Responses III, 68570N (18 February 2008); doi: 10.1117/12.762028
Show Author Affiliations
Yingjie Zhang, South China Normal Univ. (China)
Da Xing, South China Normal Univ. (China)
Yinyuan Wu, South China Normal Univ. (China)
Lei Liu, South China Normal Univ. (China)

Published in SPIE Proceedings Vol. 6857:
Biophotonics and Immune Responses III
Wei R. Chen, Editor(s)

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