The caspase-cleaved DAP5 protein supports internal ribosome entry site-mediated translation of death proteins.

ABSTRACT: Apoptosis is characterized by a translation switch from cap-dependent to internal ribosome entry site (IRES)-mediated protein translation. During apoptosis, several members of the eukaryotic initiation factor (eIF)4G family are cleaved specifically by caspases. Here we investigated which of the caspase-cleaved eIF4G family members could support cap-independent translation through IRES elements that retain activity in the dying cell. We focused on two major fragments arising from the cleavage of eIF4GI and death-associated protein 5 (DAP5) proteins (eIF4GI M-FAG/p76 and DAP5/p86, respectively), because they are the only potential candidates to preserve the minimal scaffold function needed to mediate translation. Transfection-based experiments in cell cultures indicated that expression of DA

SUBMITTER: Henis-Korenblit S 

PROVIDER: S-EPMC122781 | biostudies-literature | 2002 Apr

REPOSITORIES: biostudies-literature