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. 2011 Sep;6(3):311–323. doi: 10.2174/157489211796957757

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© 2011 Bentham Science Publishers

This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.5/), which permits unrestrictive use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. (2) — TRAIL signaling at the receptor level. A, TRAIL ligand induces aggregation of the TRAIL receptor at the membrane and activates the apoptotic cascade. B, TRAIL-R3 competes for TRAIL binding, sequestering TRAIL in lipid rafts. C, TRAIL-R4 forms heteromeric complexes with TRAIL-R2, inhibiting caspase-8 activation. D, Tentative model of inhibition of caspase-8 activation by TRAIL-R4. Upon engagement of TRAIL, the receptors aggregate into a highly regular array, whose minimal arrangement is represented as a side view in the white square. This tetrameric interaction module is composed of FADD-TRAIL-R2/Caspase-8 (Yellow and Red circles). Modular arrangement of this module into a platform enhances the proximity-induced dimerization and activation of caspase-8. Recruitment of TRAILR4 (lower panel, grey circles) disrupts caspase-8 arrangement, and thus limits caspase-8 activation. E-F, receptor specific agonistic antibodies engage TRAIL DISC, irrespective of TRAIL-R3 or TRAIL-R4 expression.