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Sci. STKE, 28 January 2003
Vol. 2003, Issue 167, p. pl1
[DOI: 10.1126/stke.2003.167.pl1]

PROTOCOLS

Activation of Procaspases by FK506 Binding Protein-Mediated Oligomerization

David W. Chang and Xiaolu Yang*

Abramson Family Cancer Research Institute and Department of Cancer Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

Abstract: Oligomerization is an important biological mechanism for regulating signal transduction. Activation of caspases during apoptosis is triggered by adaptor protein-mediated oligomerization of initiator procaspases. To facilitate the study of initiator caspase activation, a system that allows inducible activation of various caspases both in vitro and in vivo is highly desired. Here we describe such a caspase activation system that is based on FK506 binding protein (FKBP)-mediated oligomerization. The NH2-terminal prodomains of initiator procaspases that facilitate the interaction between procaspases and their adaptor proteins are replaced by a derivative of FKBP called Fv. The Fv-caspase fusions can then be dimerized by a synthetic divalent Fv ligand, AP20187, which binds strongly to Fv but weakly to the endogenous FKBPs. This FKBP-based system may be widely applicable to the study of the regulation and functions of caspases.

*Corresponding author. E-mail: xyang{at}mail.med.upenn.edu

Citation: D. W. Chang, X. Yang, Activation of Procaspases by FK506 Binding Protein-Mediated Oligomerization. Sci. STKE 2003, pl1 (2003).

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