ArticleInternational journal of molecular sciences2018
Human Miro Proteins Act as NTP Hydrolases through a Novel, Non-Canonical Catalytic Mechanism.
Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Engineered bone-targetingMaterials today. Bio · 2026Article
- Structural basis of pseudoGTPase-mediated protein-protein interactions.Structure (London, England : 1993) · 2025Article
- MIRO1 controls energy production and proliferation of vascular smooth muscle cells.bioRxiv : the preprint server for biology · 2025Article
- Histidine containing dipeptides protect epithelial and endothelial cell barriers from methylglyoxal induced injury.Scientific reports · 2024Article
- Review
- Interaction between the mitochondrial adaptor MIRO and the motor adaptor TRAK.The Journal of biological chemistry · 2023Article
- Miro proteins and their role in mitochondrial transfer in cancer and beyond.Frontiers in cell and developmental biology · 2022Review
- Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.Journal of structural biology · 2020Article
- Review
- The pseudoGTPase group of pseudoenzymes.The FEBS journal · 2020Review
- Miro: A molecular switch at the center of mitochondrial regulation.Protein science : a publication of the Protein Society · 2020Review
- The MyMOMA domain of MYO19 encodes for distinct Miro-dependent and Miro-independent mechanisms of interaction with mitochondrial membranes.Cytoskeleton (Hoboken, N.J.) · 2020Article
- The Emerging Role ofFrontiers in neurology · 2020Review
- Review
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Authors and funding
5 authors.
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Abstract
Mitochondria are highly dynamic organelles that play a central role in multiple cellular processes, including energy metabolism, calcium homeostasis and apoptosis. Miro proteins (Miros) are "atypical" Ras superfamily GTPases that display unique domain architecture and subcellular localisation regulating mitochondrial transport, autophagy and calcium sensing. Here, we present systematic catalytic domain characterisation and structural analyses of human Miros. Despite lacking key conserved catalytic residues (equivalent to Ras Y32, T35, G60 and Q61), the Miro N-terminal GTPase domains display GTPase activity. Surprisingly, the C-terminal GTPase domains previously assumed to be "relic" domains were also active. Moreover, Miros show substrate promiscuity and function as NTPases. Molecular docking and structural analyses of Miros revealed unusual features in the Switch I and II regions, facilitating promiscuous substrate binding and suggesting the usage of a novel hydrolytic mechanism. The key substitution in position 13 in the Miros leads us to suggest the existence of an "internal arginine finger", allowing an unusual catalytic mechanism that does not require GAP protein. Together, the data presented here indicate novel catalytic functions of human Miro atypical GTPases through altered catalytic mechanisms.
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