INITIATION FACTOR OF TRANSLATION EIF4GI AND OTHER CELLULAR PROTEINS
HIV PR also cleaves the initiation factor of translation eIF4GI and other cellular structure proteins such as actin, laminin B, desmin, and vimentin.20-27 Although these cellular proteins are not intrinsically apoptotic regulatory molecules, it is likely that they are involved in the decision of cells to die or remain viable.
For example, the morphological changes associated with apoptosis are controlled by cytoskeletal reorganization,28-30 as most cytoskeleton proteins are cleaved by activated caspases in the processes of apoptosis.16 Therefore, PR-mediated cleavage of these proteins may contribute to the phenotypic effects of apoptosis. Moreover, the cleavage of eIF4GI by HIV PR drastically impairs the translation of capped and uncapped mRNAs,25,26,31 which, in turn, leads to inhibition of protein synthesis, resulting in metabolic arrest, impaired cellular respiration, and consequent death. There are at least two HIV-1 PR cleavage sites on eIF4GI: one located at the N-terminus between positions 718 and 719 and another located at the C-terminus between positions 1126 and 1127.32 Teleogically, eIF4GI cleavage by PR, resulting in inhibition of protein synthesis, is consistent with the concept that HIV PR is cytotoxic.
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