Abstract
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.
| Original language | English |
|---|---|
| Article number | 102008 |
| Number of pages | 12 |
| Journal | Mitochondrion |
| Volume | 81 |
| DOIs | |
| Publication status | Published - 1 Mar 2025 |
Keywords
- Intermediate filaments
- Mitochondria
- Mitochondrial dynamics
- Network analysis
- Protein-protein interactions
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