ArticleProtein science : a publication of the Protein Society2015
Crystal structure and functional analysis of MiD49, a receptor for the mitochondrial fission protein Drp1.
Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Article
- Subcellular Stress Markers in Epithelial Ovarian Cancer.International journal of molecular sciences · 2025Review
- Mitochondrial fission - changing perspectives for future progress.Journal of cell science · 2025Review
- Mitochondrial dynamics at the intersection of macrophage polarization and metabolism.Frontiers in immunology · 2025Review
- Regulation of mitochondrial fission by fatty acyl-coenzyme A.Nature cell biology · 2024Article
- Fatty acyl-coenzyme A activates mitochondrial division through oligomerization of MiD49 and MiD51.Nature cell biology · 2024Article
- A potential therapeutic approach for ulcerative colitis: targeted regulation of mitochondrial dynamics and mitophagy through phytochemicals.Frontiers in immunology · 2024Review
- The mystery of phospho-Drp1 with four adaptors in cell cycle: when mitochondrial fission couples to cell fate decisions.Cell cycle (Georgetown, Tex.) · 2023Article
- Convergent and divergent mechanisms of peroxisomal and mitochondrial division.The Journal of cell biology · 2023Article
- Review
- The Drp1-Mediated Mitochondrial Fission Protein Interactome as an Emerging Core Player in Mitochondrial Dynamics and Cardiovascular Disease Therapy.International journal of molecular sciences · 2023Review
- Selective inhibitors targeting Fis1/Mid51 protein-protein interactions protect against hypoxia-induced damage in cardiomyocytes.Frontiers in pharmacology · 2023Article
- Mitochondrial dynamics and its impact on human health and diseases: inside the DRP1 blackbox.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Review
- MIEF1/2 orchestrate mitochondrial dynamics through direct engagement with both the fission and fusion machineries.BMC biology · 2021Article
- Review
- Review
- Players in Mitochondrial Dynamics and Female Reproduction.Frontiers in molecular biosciences · 2021Review
- Downregulation of MiD49 contributes to tumor growth and metastasis of human pancreatic cancer.Oncology reports · 2020Article
- Review
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Authors and funding
6 authors.
Funding
Abstract
Mitochondrial fission requires recruitment of dynamin-related protein 1 (Drp1) to the mitochondrial surface, where assembly leads to activation of its GTP-dependent scission function. MiD49 and MiD51 are two receptors on the mitochondrial outer membrane that can recruit Drp1 to facilitate mitochondrial fission. Structural studies indicated that MiD51 has a variant nucleotidyl transferase fold that binds an ADP co-factor essential for activation of Drp1 function. MiD49 shares sequence homology with MiD51 and regulates Drp1 function. However, it is unknown if MiD49 binds an analogous co-factor. Because MiD49 does not readily crystallize, we used structural predictions and biochemical screening to identify a surface entropy reduction mutant that facilitated crystallization. Using molecular replacement, we determined the atomic structure of MiD49 to 2.4 Å. Like MiD51, MiD49 contains a nucleotidyl transferase domain; however, the electron density provides no evidence for a small-molecule ligand. Structural changes in the putative nucleotide-binding pocket make MiD49 incompatible with an extended ligand like ADP, and critical nucleotide-binding residues found in MiD51 are not conserved. MiD49 contains a surface loop that physically interacts with Drp1 and is necessary for Drp1 recruitment to the mitochondrial surface. Our results suggest a structural basis for the differential regulation of MiD51- versus MiD49-mediated fission.
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