RT Journal Article
SR Electronic
T1 Caspase-10-Mediated Heat Shock Protein 90β Cleavage Promotes UVB Irradiation-Induced Cell Apoptosis
JF Molecular and Cellular Biology
JO Mol. Cell. Biol.
FD American Society for Microbiology
SP 3657
OP 3664
DO 10.1128/MCB.01640-08
VO 29
IS 13
A1 Chen, Hehua
A1 Xia, Yan
A1 Fang, Dexing
A1 Hawke, David
A1 Lu, Zhimin
YR 2009
UL http://mcb.asm.org/content/29/13/3657.abstract
AB Heat shock protein 90β (Hsp90β) is involved in many cellular functions. However, the posttranslational modification of Hsp90β, especially in response to apoptotic stimulation, is not well understood. In this study, we found that Hsp90β was cleaved by activated caspase-10 under UVB irradiation. Caspase-10 activation, in turn, depended on caspase-8, which cleaved caspase-10 directly. Autocrine secretion of FAS ligand and upregulated FAS expression induced by UVB irradiation contributed to activation of caspase-10, which cleaved Hsp90β at D278, P293, and D294. The downregulation of Hsp90β mediated by caspase-8-dependent caspase-10 activation promoted UVB-induced cell apoptosis.