Journal
DEVELOPMENTAL CELL
Volume 55, Issue 3, Pages 298-+Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2020.10.006
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Funding
- Medical Research Council (United Kingdom) Career Development Award [MR/P009417/1]
- Barts Charity grant [MGU0346]
- European Research Council grant (European Union) under the EU's Seventh Framework Programme [617837-Translate]
- MRC [MR/P009417/1] Funding Source: UKRI
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Translation of ribosomal protein-coding mRNAs (RP-mRNAs) constitutes a key step in ribosome biogenesis, but the mechanisms that modulate RP-mRNA translation in coordination with other cellular processes are poorly defined. Here, we show that subcellular localization of RP-mRNAs acts as a key regulator of their translation during cell migration. As cells migrate into their surroundings, RP-mRNAs localize to the actin-rich cell protrusions. This localization is mediated by La-related protein 6 (LARP6), an RNA-binding protein that is enriched in protrusions. Protrusions act as hotspots of translation for RP-mRNAs, enhancing RP synthesis, ribosome biogenesis, and the overall protein synthesis in migratory cells. In human breast carcinomas, epithelial-to-mesenchymal transition (EMT) upregulates LARP6 expression to enhance protein synthesis and support invasive growth. Our findings reveal LARP6-mediated mRNA localization as a key regulator of ribosome biogenesis during cell migration and demonstrate a role for this process in cancer progression downstream of EMT.
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