hnRNP R promotes O-GlcNAcylation of eIF4G and facilitates axonal protein synthesis

Abdolhossein Zare, Saeede Salehi, Jakob Bader, Cornelius Schneider, Utz Fischer, Alexander Veh, Panagiota Arampatzi, Matthias Mann, Michael Briese () and Michael Sendtner ()
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Abdolhossein Zare: University Hospital Wuerzburg
Saeede Salehi: University Hospital Wuerzburg
Jakob Bader: Max Planck Institute of Biochemistry
Cornelius Schneider: University of Wuerzburg
Utz Fischer: University of Wuerzburg
Alexander Veh: University Hospital Wuerzburg
Panagiota Arampatzi: University of Wuerzburg
Matthias Mann: Max Planck Institute of Biochemistry
Michael Briese: University Hospital Wuerzburg
Michael Sendtner: University Hospital Wuerzburg

Nature Communications, 2024, vol. 15, issue 1, 1-20

Abstract: Abstract Motoneurons critically depend on precise spatial and temporal control of translation for axon growth and the establishment and maintenance of neuromuscular connections. While defects in local translation have been implicated in the pathogenesis of motoneuron disorders, little is known about the mechanisms regulating axonal protein synthesis. Here, we report that motoneurons derived from Hnrnpr knockout mice show reduced axon growth accompanied by lowered synthesis of cytoskeletal and synaptic components in axons. Mutant mice display denervated neuromuscular junctions and impaired motor behavior. In axons, hnRNP R is a component of translation initiation complexes and, through interaction with O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (Ogt), modulates O-GlcNAcylation of eIF4G. Restoring axonal O-GlcNAc levels rescued local protein synthesis and axon growth defects of hnRNP R knockout motoneurons. Together, these findings demonstrate a function of hnRNP R in controlling the local production of key factors required for axon growth and formation of neuromuscular innervations.

Date: 2024
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DOI: 10.1038/s41467-024-51678-y

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