Work

The unusual suspect: A novel role for intermediate filament proteins in mitochondrial morphology

Year: 2025

Type: article

Abstract: • Protein-protein interaction network analysis has identified proteins linked to mitochondrial dynamics. • ITPRIPL2 is associated with vimentin containing intermediate filament structure and required to modify the vimentin protein. • Maintenance of intermediate filament structure is essential for mitochondrial fission. Mitochondrial dynamics is crucial for cellular homeostasis. However, not all proteins involved are known. Using a protein–protein interaction (PPI) approach, we identified ITPRIPL2 for involvement in mitochondrial dynamics. ITPRIPL2 co-localizes with intermediate filament protein vimentin, supported by protein simulations. ITPRIPL2 knockdown reveals mitochondrial elongation, disrupts vimentin processing, intermediate filament formation, and alters vimentin-related pathways. Interestingly, vimentin knockdown also leads to mitochondrial elongation. These findings highlight ITPRIPL2 as vimentin-associated protein essential for intermediate filament structure and suggest a role for intermediate filaments in mitochondrial morphology. Our study demonstrates that PPI analysis is a powerful approach for identifying novel mitochondrial dynamics proteins.

Source: Mitochondrion

DOI: 10.1016/j.mito.2025.102008