Induction of cap-independent BiP (hsp-3) and Bcl-2 (ced-9) translation in response to eIF4G (IFG-1) depletion in C. elegans

Translation
J Kaitlin MorrisonBrett D Keiper

Abstract

During apoptosis, activated caspases cleave the translation initiation factor eIF4G. This cleavage disrupts cap-dependent mRNA translation initiation within the cell. However, a specific subset of mRNAs can still be recruited for protein synthesis in a cap-independent manner by the residual initiation machinery. Many of these mRNAs, including cell death related mRNAs, contain internal ribosome entry sites (IRESes) that promote their enhanced translation during apoptosis. Still other mRNAs have little dependence on the cap recognition mechanism. The expression of the encoded proteins, both anti- and pro-apoptotic, allows for an initial period of attempted cell survival, then commitment to cell death when damage is extensive. In this study we address the translational regulation of the stress and apoptosis-related mRNAs in C. elegans: BiP (hsp-3) (hsp-4), Hif-1 (hif-1), p53 (cep-1), Bcl-2 (ced-9) and Apaf-1 (ced-4). Altered translational efficiency of these messages was observed upon depletion of cap-dependent translation and induction of apoptosis within the C. elegans gonad. Our findings suggest a physiological link between the cap-independent mechanism and the enhanced translation of hsp-3 and ced-9. This increase in the effic...Continue Reading

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Citations

Sep 12, 2015·BioMed Research International·Andrew J Friday, Brett D Keiper
Jan 10, 2019·International Journal of Molecular Sciences·Brett D Keiper
Aug 1, 2020·Frontiers in Cell and Developmental Biology·Hayden P Huggins, Brett D Keiper
Feb 23, 2019·International Journal of Molecular Sciences·Anne-Claire GodetAnne-Catherine Prats

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Methods Mentioned

BETA
protein folding
transgenic
Fluorescence
PCR
Assay
electrophoresis

Software Mentioned

ImageQuant TL

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