Next Article in Journal
Conformational Switching in Bcl-xL: Enabling Non-Canonic Inhibition of Apoptosis Involves Multiple Intermediates and Lipid Interactions
Next Article in Special Issue
Targeting the Human 80S Ribosome in Cancer: From Structure to Function and Drug Design for Innovative Adjuvant Therapeutic Strategies
Previous Article in Journal / Special Issue
snoRNAs Offer Novel Insight and Promising Perspectives for Lung Cancer Understanding and Management
Open AccessReview

Translational Regulations in Response to Endoplasmic Reticulum Stress in Cancers

1
Inserm UMR1037, CRCT (Cancer Research Center of Toulouse), F-31037 Toulouse, France
2
Université Toulouse III Paul-Sabatier, F-31000 Toulouse, France
3
Barts Cancer Institute, Queen Mary University of London, London E1 4NS, UK
4
Inserm UMR1048, I2MC (Institut des Maladies Métaboliques et Cardiovasculaires), BP 84225, CEDEX 04, 31 432 Toulouse, France
5
CNRS ERL5294, CRCT, F-31037 Toulouse, France
*
Author to whom correspondence should be addressed.
These two authors contributed equally to this work.
Cells 2020, 9(3), 540; https://doi.org/10.3390/cells9030540
Received: 20 December 2019 / Revised: 18 February 2020 / Accepted: 24 February 2020 / Published: 26 February 2020
(This article belongs to the Special Issue Translational Machinery to Understand and Fight Cancer)
During carcinogenesis, almost all the biological processes are modified in one way or another. Among these biological processes affected, anomalies in protein synthesis are common in cancers. Indeed, cancer cells are subjected to a wide range of stresses, which include physical injuries, hypoxia, nutrient starvation, as well as mitotic, oxidative or genotoxic stresses. All of these stresses will cause the accumulation of unfolded proteins in the Endoplasmic Reticulum (ER), which is a major organelle that is involved in protein synthesis, preservation of cellular homeostasis, and adaptation to unfavourable environment. The accumulation of unfolded proteins in the endoplasmic reticulum causes stress triggering an unfolded protein response in order to promote cell survival or to induce apoptosis in case of chronic stress. Transcription and also translational reprogramming are tightly controlled during the unfolded protein response to ensure selective gene expression. The majority of stresses, including ER stress, induce firstly a decrease in global protein synthesis accompanied by the induction of alternative mechanisms for initiating the translation of mRNA, later followed by a translational recovery. After a presentation of ER stress and the UPR response, we will briefly present the different modes of translation initiation, then address the specific translational regulatory mechanisms acting during reticulum stress in cancers and highlight the importance of translational control by ER stress in tumours. View Full-Text
Keywords: translation initiation; ER stress; unfolded protein response (UPR); IRES; uORF translation initiation; ER stress; unfolded protein response (UPR); IRES; uORF
Show Figures

Figure 1

MDPI and ACS Style

Jaud, M.; Philippe, C.; Di Bella, D.; Tang, W.; Pyronnet, S.; Laurell, H.; Mazzolini, L.; Rouault-Pierre, K.; Touriol, C. Translational Regulations in Response to Endoplasmic Reticulum Stress in Cancers. Cells 2020, 9, 540.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop