Hemel Irene M G M, Steen Carlijn, Denil Simon L I J, Ertaylan Gökhan, Kutmon Martina, Adriaens Michiel, Gerards Mike
Maastricht Centre for Systems Biology (MaCSBio), Maastricht University, Maastricht 6229 EN the Netherlands.
Flemish Institute for Technological Research (VITO) 2400 Mol, Belgium.
Mitochondrion. 2025 Mar;81:102008. doi: 10.1016/j.mito.2025.102008. Epub 2025 Feb 3.
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.
线粒体动力学对于细胞稳态至关重要。然而，并非所有涉及的蛋白质都是已知的。利用蛋白质-蛋白质相互作用（PPI）方法，我们鉴定出ITPRIPL2参与线粒体动力学。在蛋白质模拟的支持下，ITPRIPL2与中间丝蛋白波形蛋白共定位。ITPRIPL2基因敲低显示线粒体延长，破坏波形蛋白加工、中间丝形成，并改变波形蛋白相关途径。有趣的是，波形蛋白基因敲低也导致线粒体延长。这些发现突出了ITPRIPL2作为波形蛋白相关蛋白对中间丝结构至关重要，并提示中间丝在线粒体形态中的作用。我们的研究表明，PPI分析是鉴定新型线粒体动力学蛋白的有力方法。
