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A microscopy-based screen identifies cellular kinases modulating mitochondrial translation

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Hansohn,  Carina
Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Rehling,  Peter
MPI-NAT Fellow Mitochondrial Biogenesis and Assembly of membrane Protein Complexes, Max Planck Institute for Multidisciplinary Sciences, Max Planck Society;

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Citation

Yousefi, R., Cruz-Zaragoza, L., Valpadashi, A., Hansohn, C., Dahal, D., Richter-Dennerlein, R., et al. (2025). A microscopy-based screen identifies cellular kinases modulating mitochondrial translation. Cell Reports, 44(1): 115143. doi:10.1016/j.celrep.2024.115143.


Cite as: https://hdl.handle.net/21.11116/0000-0010-62A7-3
Abstract
Mitochondrial DNA encodes 13 subunits of the oxidative phosphorylation (OXPHOS) system, which are synthesized inside the organelle and essential for cellular energy supply. How mitochondrial gene expression is regulated and integrated into cellular physiology is little understood. Here, we perform a high-throughput screen combining fluorescent labeling of mitochondrial translation products with small interfering RNA (siRNA)-mediated knockdown to identify cellular kinases regulating translation. As proof of principle, the screen identifies known kinases that affect mitochondrial translation, and it also reveals several kinases not yet linked to this process. Among the latter, we focus on the primarily cytosolic kinase, fructosamine 3 kinase (FN3K), which localizes partially to the mitochondria to support translation. FN3K interacts with the mitochondrial ribosome and modulates its assembly, thereby affecting translation. Overall, our work provides a reliable approach to identify protein functions for mitochondrial gene expression in a high-throughput manner.