AMPK-dependent phosphorylation of MTFR1L regulates mitochondrial morphology

• DOI: 10.1126/sciadv.abo7956
• Publication Date: 2022-11-11T18:58:20Z
• Authors: Lisa Tilokani; Fiona M. Russell; Stevie Hamilton; Daniel M. Virga; Mayuko Segawa; Vincent Paupe; Anja V. Gruszczyk; Margherita Protasoni; Luis-Carlos Tabara; Mark Johnson; Hanish Anand; Michael P. Murphy; D. Grahame Hardie; Franck Polleux; Julien Prudent
• Keywords: DNAJA3; Mitochondrial apoptosis-induced channel; AMP-Activated Protein Kinase

Mitochondria are dynamic organelles that undergo membrane remodeling events in response to metabolic alterations generate an adequate mitochondrial network. Here, we investigated the function of fission regulator 1-like protein (MTFR1L), uncharacterized has been identified phosphoproteomic screens as a potential AMP-activated kinase (AMPK) substrate. We showed MTFR1L is outer membrane-localized modulating morphology. Loss led elongation associated with increased fusion and levels protein, optic atrophy 1. Mechanistically, show phosphorylated by AMPK, which thereby controls regulating morphology both mammalian cell lines murine cortical neurons vivo. Furthermore, demonstrate required for stress-induced AMPK-dependent fragmentation. Together, these findings identify critical transducing changes through regulation dynamics.