The CULt of Caspase-8 Ubiquitination

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The CULt of Caspase-8 Ubiquitination Miklós Békés, Guy S. Salvesen Cell Volume 137, Issue 4, Pages 604-606 (May 2009) DOI: 10.1016/j.cell.2009.04.052 Copyright © 2009 Elsevier Inc. Terms and Conditions

Figure 1 CUL3/RBX1-Mediated Ubiquitination of Activated Caspase-8 The proapoptotic ligand TRAIL binds to its receptor DR4/5, leading to the recruitment of the adaptor protein FADD (1). This initiates caspase-8 recruitment, dimerization, and activation. Caspase-8 is polyubiquitinated at the death-inducing signaling complex (DISC) by the neddylated form of CUL3/RBX1, permitting p62 binding (2). Autoprocessing of caspase-8 separates its recruitment and catalytic domains (3). The catalytic component is transported by p62 to ubiquitin (Ub)-rich “aggresomes” in the cytosol, where it maintains its activity through the stabilization of its dimeric conformation (4). Cell 2009 137, 604-606DOI: (10.1016/j.cell.2009.04.052) Copyright © 2009 Elsevier Inc. Terms and Conditions