Article (Scientific journals)
Caspase-8 Cleaves Histone Deacetylase 7 And Abolishes Its Transcription Repressor Function
Scott, Fl.; Fuchs, Gj.; Boyd, Se. et al.
2008In Journal of Biological Chemistry, 283 (28)
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Keywords :
caspase; apoptosis; thymocytes; transcription; hdac; hdac7; nur77; acetylation; chromatin; shuttling
Abstract :
[en] Caspase-8 is the initiator caspase of the extrinsic apoptosis pathway and also has a role in non-apoptotic physiologies. Identifying endogenous substrates for caspase-8 by using integrated bioinformatics and biological approaches is required to delineate the diverse roles of this caspase. We describe a number of novel putative caspase-8 substrates using the Prediction of Protease Specificity (PoPS) program, one of which is histone deacetylase 7 (HDAC7). HDAC7 is cleaved faster than any other caspase-8 substrate described to date. It is also cleaved in primary CD4+CD8+ thymocytes undergoing extrinsic apoptosis. By using naturally occurring caspase inhibitors that have evolved exquisite specificity at concentrations found within the cell, we could unequivocally assign the cleavage activity to caspase-8. Importantly, cleavage of HDAC7 alters its subcellular localization and abrogates its Nur77 repressor function. Thus we demonstrate a direct role for initiator caspase-mediated proteolysis in promoting gene transcription.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Scott, Fl.
Fuchs, Gj.
Boyd, Se.
Denault, Jb.
Hawkins, Cj.
Dequiedt, Franck  ;  Université de Liège - ULiège > Gembloux Agro-Bio Tech et GIGA-Research
Salvesen, Gs.
Language :
English
Title :
Caspase-8 Cleaves Histone Deacetylase 7 And Abolishes Its Transcription Repressor Function
Publication date :
2008
Journal title :
Journal of Biological Chemistry
ISSN :
0021-9258
eISSN :
1083-351X
Publisher :
American Society for Biochemistry and Molecular Biology, United States - Maryland
Volume :
283
Issue :
28
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 07 December 2009

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