6285f15c96e8245c5153b4f1418326c9 303850.pdf 5ac25607c05e8e4eb391b6d0a9e4749c6f955bdf 303850.pdf 61f3895f92d9842d77ade15060971033e062991d1aad3be22e879cb539ec2822 303850.pdf Title: Mechanisms of Modulation of Mitochondrial Architecture Subject: Mitochondrial network architecture plays a critical role in cellular physiology. Indeed, alterations in the shape of mitochondria upon exposure to cellular stress can cause the dysfunction of these organelles. In this scenario, mitochondrial dynamics proteins and the phospholipid composition of the mitochondrial membrane are key for fine-tuning the modulation of mitochondrial architecture. In addition, several factors including post-translational modifications such as the phosphorylation, acetylation, SUMOylation, and o-GlcNAcylation of mitochondrial dynamics proteins contribute to shaping the plasticity of this architecture. In this regard, several studies have evidenced that, upon metabolic stress, mitochondrial dynamics proteins are post-translationally modified, leading to the alteration of mitochondrial architecture. Interestingly, several proteins that sustain the mitochondrial lipid composition also modulate mitochondrial morphology and organelle communication. In this context, pharmacological studies have revealed that the modulation of mitochondrial shape and function emerges as a potential therapeutic strategy for metabolic diseases. Here, we review the factors that modulate mitochondrial architecture. Keywords: mitochondria; metabolism; mitochondrial dynamics; pharmacology; lipids; metabolic disease; membrane contact sites (MCSs); tethers; post-translational modification Author: Juan Pablo Muñoz, Fernanda Luisa Basei, María Laura Rojas, David Galvis and Antonio Zorzano Creator: LaTeX with hyperref Producer: pdfTeX-1.40.21 CreationDate: Tue Aug 8 11:05:37 2023 CEST ModDate: Tue Aug 8 11:09:00 2023 CEST Custom Metadata: no Metadata Stream: no Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 46 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 2986246 bytes Optimized: no PDF version: 1.7 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- XOPHNR+URWPalladioL-Bold Type 1 Custom yes yes no 10 0 TLJDRR+URWPalladioL-Roma Type 1 Custom yes yes no 15 0 EQCGZS+URWPalladioL-Ital Type 1 Custom yes yes no 19 0 NJGGUQ+VnURWPalladioL Type 1 Custom yes yes no 23 0 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Item: Title: DRP1 Destination: subsubsection.2.1.1 Item: Title: MFF Destination: subsubsection.2.1.2 Item: Title: FIS1 Destination: subsubsection.2.1.3 Item: Title: MiD49 and MiD51 Destination: subsubsection.2.1.4 Item: Title: Mitochondrial Fission Protein Phosphorylation Destination: subsection.2.2 Children: Item: Title: DRP1 Phosphorylation Destination: subsubsection.2.2.1 Item: Title: MFF Phosphorylation Destination: subsubsection.2.2.2 Item: Title: FIS1 Phosphorylation Destination: subsubsection.2.2.3 Item: Title: Mitochondrial Fusion Proteins Destination: subsection.2.3 Children: Item: Title: Mitofusin 1 Destination: subsubsection.2.3.1 Item: Title: Mitofusin 2 Destination: subsubsection.2.3.2 Item: Title: OPA1 Destination: subsubsection.2.3.3 Item: Title: Mitochondrial Fusion Protein Phosphorylation Destination: subsection.2.4 Item: Title: Other Post-Translational Modifications of Mitochondrial Dynamics Proteins Destination: section.3 Children: Item: Title: Mitochondrial Dynamics Protein Acetylation Destination: subsection.3.1 Item: Title: SUMOylation of Mitochondrial Dynamics Proteins Destination: subsection.3.2 Item: Title: O-GlcNAcylation of Mitochondrial Dynamics Proteins Destination: subsection.3.3 Item: Title: Participation of Lipids in Mitochondrial Morphology Destination: section.4 Children: Item: Title: Mitochondrial Phospholipids Destination: subsection.4.1 Item: Title: Mitochondrial Phospholipid Composition Destination: subsection.4.2 Item: Title: Lipid Transfer Proteins Destination: subsection.4.3 Item: Title: Phospholipid Scramblases Destination: subsection.4.4 Item: Title: Pharmacological Approaches to Modulate Mitochondrial Architecture Destination: section.5 Item: Title: References Destination: section.6 Info: Title: Mechanisms of Modulation of Mitochondrial Architecture Author: Juan Pablo Muñoz, Fernanda Luisa Basei, María Laura Rojas, David Galvis and Antonio Zorzano Subject: Mitochondrial network architecture plays a critical role in cellular physiology. Indeed, alterations in the shape of mitochondria upon exposure to cellular stress can cause the dysfunction of these organelles. In this scenario, mitochondrial dynamics proteins and the phospholipid composition of the mitochondrial membrane are key for fine-tuning the modulation of mitochondrial architecture. In addition, several factors including post-translational modifications such as the phosphorylation, acetylation, SUMOylation, and o-GlcNAcylation of mitochondrial dynamics proteins contribute to shaping the plasticity of this architecture. In this regard, several studies have evidenced that, upon metabolic stress, mitochondrial dynamics proteins are post-translationally modified, leading to the alteration of mitochondrial architecture. Interestingly, several proteins that sustain the mitochondrial lipid composition also modulate mitochondrial morphology and organelle communication. In this context, pharmacological studies have revealed that the modulation of mitochondrial shape and function emerges as a potential therapeutic strategy for metabolic diseases. Here, we review the factors that modulate mitochondrial architecture. 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