Inhibition of both the extrinsic and intrinsic death pathways through nonhomotypic death-fold interactions.

Abstract:

:Death-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). The intrinsic pathway is antagonized by ARC-Bax binding, involving ARC's CARD and the Bax C terminus. This inhibits Bax activation and translocation to the mitochondria. Knockdown of endogenous ARC facilitates DISC assembly and triggers spontaneous Bax activation and apoptosis. Conversely, physiological levels of ARC suppress these events. These studies establish a critical role for nonhomotypic death-fold interactions in the regulation of apoptosis.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Nam YJ,Mani K,Ashton AW,Peng CF,Krishnamurthy B,Hayakawa Y,Lee P,Korsmeyer SJ,Kitsis RN

doi

10.1016/j.molcel.2004.08.020

subject

Has Abstract

pub_date

2004-09-24 00:00:00

pages

901-12

issue

6

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(04)00482-4

journal_volume

15

pub_type

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