Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions
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Abstract
(Molecular Cell, Vol. 15, 901–912; September 24, 2004) We, the editors of Molecular Cell, were contacted by the corresponding author, Dr. Richard Kitsis, and a concerned reader, who informed us about a duplication in Figure 7A of the above paper. Dr. Kitsis apologized for the inadvertent side-by-side duplication of the α-tubulin loading control. The authors no longer have access to the original data published 16 years ago and could not determine how the error arose. They note, however, that the data in lanes 1–3 of Figure 7B show independently that ARC levels in H9c2 cells decrease with hydrogen peroxide treatment. Without access to the original data for Figure 7A, a Correction is not possible. Given the age of the paper and that the duplication does not compromise the conclusions of the paper, based on the information available to us at this time, we believe that no further action is warranted. Inhibition of Both the Extrinsic and Intrinsic Death Pathways through Nonhomotypic Death-Fold InteractionsNam et al.Molecular CellSeptember 24, 2004In BriefDeath-fold domains constitute an evolutionarily conserved superfamily that mediates apoptotic signaling. These motifs, including CARD (caspase recruitment domain), DD (death domain), and DED (death effector domain), are believed to exert their effects solely through homotypic interactions. Herein we demonstrate that the CARD-containing protein ARC engages in nontraditional death-fold interactions to suppress both extrinsic and intrinsic death pathways. The extrinsic pathway is disrupted by heterotypic interactions between ARC's CARD and the DDs of Fas and FADD, which inhibit Fas-FADD binding and assembly of the death-inducing signaling complex (DISC). Full-Text PDF Open Archive