Related Experiment Video
Updated: Apr 12, 2026

Analysis of Translation Initiation During Stress Conditions by Polysome Profiling
Published on: May 19, 2014
Therapeutic potential of targeting IRES-dependent c-myc translation in multiple myeloma cells during ER stress
1Division of Hematology-Oncology, UCLA-Greater Los Angeles VA Healthcare Center and Jonsson Comprehensive Cancer Center, VA West LA Hospital/Hematology-Oncology, W111H, West LA VA Hospital, Los Angeles, CA, USA.
Abstract:
Protein translation is inhibited by the unfolded protein response (UPR)-induced eIF-2α phosphorylation to protect against endoplasmic reticulum (ER) stress. In addition, we found additional inhibition of protein translation owing to diminished mTORC1 (mammalian target of rapamycin complex1) activity in ER-stressed multiple myeloma (MM) cells. However, c-myc protein levels and myc translation was maintained. To ascertain how c-myc was maintained, we studied myc IRES (internal ribosome entry site) function, which does not require mTORC1 activity. Myc IRES activity was upregulated in MM cells during ER stress induced by thapsigargin, tunicamycin or the myeloma therapeutic bortezomib. IRES activity was dependent on upstream MAPK (mitogen-activated protein kinase) and MNK1 (MAPK-interacting serine/threonine kinase 1) signaling. A screen identified hnRNP A1 (A1) and RPS25 as IRES-binding trans-acting factors required for ER stress-activated activity. A1 associated with RPS25 during ER stress and this was prevented by an MNK inhibitor. In a proof of principle, we identified a compound that prevented binding of A1 to the myc IRES and specifically inhibited myc IRES activity in MM cells. This compound, when used alone, was not cytotoxic nor did it inhibit myc translation or protein expression. However, when combined with ER stress inducers, especially bortezomib, a remarkable synergistic cytotoxicity ensued with associated inhibition of myc translation and expression. These results underscore the potential for targeting A1-mediated myc IRES activity in MM cells during ER stress.
Insights
Endoplasmic reticulum stress in multiple myeloma cells maintains c-myc translation via upregulated internal ribosome entry site (IRES) activity. Targeting this pathway with specific compounds synergizes with bortezomib, offering a novel therapeutic strategy.
Area of Science:
- Molecular Biology
- Cancer Biology
- Cellular Stress Response
Background:
- Protein translation is typically inhibited by the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress.
- Multiple myeloma (MM) cells exhibit diminished mTORC1 activity under ER stress, yet maintain c-myc protein levels.
- The mechanism for maintaining c-myc translation during ER stress in MM cells remains unclear.
Purpose of the Study:
- To investigate the mechanism by which c-myc translation is maintained in ER-stressed multiple myeloma (MM) cells.
- To explore the role of myc internal ribosome entry site (IRES) function in this process.
- To identify potential therapeutic targets for MM by modulating c-myc IRES activity.
Main Methods:
- Assessed myc IRES activity in MM cells under various ER stress conditions (thapsigargin, tunicamycin, bortezomib).
- Investigated the involvement of MAPK and MNK1 signaling pathways in regulating IRES activity.
- Utilized a screening approach to identify IRES-binding trans-acting factors, including hnRNP A1 (A1) and RPS25.
- Developed and tested a compound targeting A1 binding to the myc IRES.
Main Results:
- Myc IRES activity was significantly upregulated in MM cells experiencing ER stress.
- MAPK and MNK1 signaling pathways were found to be critical for ER stress-induced IRES activation.
- hnRNP A1 (A1) and RPS25 were identified as essential IRES-binding factors, with A1 association dependent on MNK1.
- A specific inhibitor compound blocked A1-myc IRES binding and activity without affecting basal myc translation.
- Combination therapy of the inhibitor with ER stress inducers, particularly bortezomib, resulted in synergistic cytotoxicity.
Conclusions:
- Myc IRES activity is a key mechanism for maintaining c-myc translation during ER stress in MM cells.
- The A1-RPS25 complex, regulated by MNK1, is crucial for ER stress-mediated myc IRES function.
- Targeting A1-mediated myc IRES activity presents a promising synergistic therapeutic strategy for multiple myeloma, especially in combination with bortezomib.
Related Concept Videos
Regulation of the Unfolded Protein Response
Induced Pluripotent Stem Cells
Somatic...
Targeted Cancer Therapies
There are several types of targeted therapies against...
Mitogens and the Cell Cycle
mTOR Signaling and Cancer Progression
The mTOR pathway or the...
Treatment Resistant Cancers

