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

被引：0

作者：

Hemel, Irene M. G. M. ^{[1
]}

Steen, Carlijn ^{[1
]}

Denil, Simon L. I. J. ^{[2
]}

Ertaylan, Gokhan ^{[2
]}

Kutmon, Martina ^{[1
]}

Adriaens, Michiel ^{[1
]}

Gerards, Mike ^{[1
]}

机构：

[1] Maastricht Univ, Maastricht Ctr Syst Biol MaCSBio, NL-6229 EN Maastricht, Netherlands

[2] Flemish Inst Technol Res VITO, B-2400 Mol, Belgium

来源：

MITOCHONDRION | 2025年 / 81卷

关键词：

Mitochondria; Mitochondrial dynamics; Protein-protein interactions; Intermediate filaments; Network analysis; ABNORMAL INTERACTION; AMYLOID-BETA; VIMENTIN; FUSION; DYNAMICS; FISSION; EXPRESSION; DRP1; DYSFUNCTION; MYOPATHY;

D O I：

10.1016/j.mito.2025.102008

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

引用

页数：12

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