Submitted by Penny Peck on Tue, 20/12/2022 - 16:09
Mitochondria are dynamic organelles that undergo membrane remodeling events in response to metabolic alterations to generate an adequate mitochondrial network. These dynamic shape transitions are regulated by cycles of fusion and fission events and are critical to maintain cellular homeostasis.
A research article published in Science Advances and led by Dr Lisa Tilokani from Dr Julien Prudent's group, in collaboration with researchers from the MBU, the University of Dundee (UK) and Columbia university (US), revealed MTFR1L, a previously uncharacterised protein, as an outer membrane mitochondrial protein modulating mitochondrial morphology by controlling mitochondrial fusion. They showed that MTFR1L is a substrate of AMPK, an essential kinase that senses cellular energy status or nutrient availability, and that MTFR1L’s phosphorylation was not only required to regulate mitochondrial morphology both in mammalian cell lines and in murine cortical neurons in vivo but also to ensure AMPK-dependent stress-induced mitochondrial fragmentation. Together, these findings identify MTFR1L as a critical mitochondrial protein transducing AMPK-dependent metabolic changes through regulation of mitochondrial dynamics.
Publication reference: Tilokani et al., Sci. Adv.8, eabo7956 (2022) doi: 10.1126/sciadv.abo7956
https://www.science.org/doi/10.1126/sciadv.abo7956