On-site ribosome remodeling by locally synthesized ribosomal proteins in axons

bioRxiv preprint first posted online Dec. 19, 2018; doi: http://dx.doi.org/10.1101/500033. The copyright holder for this preprint (which was not peer-reviewed) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
Authors
Toshiaki Shigeoka, Max Koppers, Hovy Ho-Wai Wong, Julie Qiaojin Lin, Asha Dwivedy, Janaina de Freitas Nascimento, Roberta Cagnetta, Francesca van Tartwijk, Florian Strohl, Jean-Michel Cioni, Mark Carrington, Clemens F. Kaminski, William A. Harris, Hosung Jung, Christine E. Holt
01-16-2019 HSW1057
12:00pm
PST
Categories
Ribosome Biogenesis & Modification
Speaker
Lorenzo Calviello
Abstract

 

Ribosomes are known to be assembled in the nucleolus, yet recent studies have revealed robust enrichment and translation of mRNAs encoding ribosomal proteins (RPs) in axons, far away from neuronal cell bodies. Using subcellular proteomics and live-imaging, we show that locally synthesized RPs incorporate into axonal ribosomes in a nucleolus-independent fashion. We revealed that axonal RP translation is regulated through a novel sequence motif, CUIC, that forms a RNA-loop structure in the region immediately upstream of the initiation codon. Inhibition of axonal CUIC-regulated RP translation leads to defects in local translation activity and axon branching, demonstrating the physiological relevance of the axonal ribosome remodeling. These results indicate that axonal translation supplies cytoplasmic RPs to maintain/modify local ribosomal function far from the nucleolus.