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Journal Article

Metabolic control of adult neural stem cell self-renewal by the mitochondrial protease YME1L

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Sprenger,  Hans-Georg
Sprenger – Molecular Metabolism & Energy Homeostasis, Max Planck Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Chandragiri,  S.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Giavalisco,  P.
Metabolomics, Core Facilities, Max Planck Institute for Biology of Ageing, Max Planck Society;

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Langer,  T.
Department Langer - Mitochondrial Proteostasis, Max Planck Institute for Biology of Ageing, Max Planck Society;

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https://www.ncbi.nlm.nih.gov/pubmed/35172139
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Citation

Wani, G. A., Sprenger, H.-G., Ndoci, K., Chandragiri, S., Acton, R. J., Schatton, D., et al. (2022). Metabolic control of adult neural stem cell self-renewal by the mitochondrial protease YME1L. Cell Rep, 38(7), 110370. doi:10.1016/j.celrep.2022.110370.


Cite as: https://hdl.handle.net/21.11116/0000-000B-B682-4
Abstract
The transition between quiescence and activation in neural stem and progenitor cells (NSPCs) is coupled with reversible changes in energy metabolism with key implications for lifelong NSPC self-renewal and neurogenesis. How this metabolic plasticity is ensured between NSPC activity states is unclear. We find that a state-specific rewiring of the mitochondrial proteome by the i-AAA peptidase YME1L is required to preserve NSPC self-renewal. YME1L controls the abundance of numerous mitochondrial substrates in quiescent NSPCs, and its deletion activates a differentiation program characterized by broad metabolic changes causing the irreversible shift away from a fatty-acid-oxidation-dependent state. Conditional Yme1l deletion in adult NSPCs in vivo results in defective self-renewal and premature differentiation, ultimately leading to NSPC pool depletion. Our results disclose an important role for YME1L in coordinating the switch between metabolic states of NSPCs and suggest that NSPC fate is regulated by compartmentalized changes in protein network dynamics.