ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2015
Miro's N-terminal GTPase domain is required for transport of mitochondria into axons and dendrites.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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48 citing papers in PubMed, 70 citations in OpenAlex.
- Mitochondrial Transport in Bone Metabolism Homeostasis: Molecular Mechanisms and Targeted Therapeutic Strategies.International journal of molecular sciences · 2026Review
- Chromatin- and actin-mediated mitochondrial streaming leads to patterning of mitochondrial distribution in oocytes.Nature communications · 2026Article
- An optogenetic assay of Drosophila larval motor neuron performance in vivo.Journal of neuroscience methods · 2026Article
- mRNA trafficking directs cell-size-scaling of mitochondria distribution and function.Nature communications · 2025Article
- Structural-functional characterization of the MIRO1-TRAK1 complex.Nature communications · 2025Article
- Expression Pattern of the AB1-Gal4 Driver inInternational journal of molecular sciences · 2025Article
- Restoration of Miro1's N-terminal GTPase function alleviates prenatal stress-induced mitochondrial fission via Drp1 modulation.Cell communication and signaling : CCS · 2025Article
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- Interaction between the mitochondrial adaptor MIRO and the motor adaptor TRAK.The Journal of biological chemistry · 2023Article
- Optogenetic cleavage of the Miro GTPase reveals the direct consequences of real-time loss of function in Drosophila.PLoS biology · 2023Article
- Mitochondria as central hubs in synaptic modulation.Cellular and molecular life sciences : CMLS · 2023Review
- TRAK adaptors regulate the recruitment and activation of dynein and kinesin in mitochondrial transport.Nature communications · 2023Article
- Miro GTPase domains regulate the assembly of the mitochondrial motor-adaptor complex.Life science alliance · 2023Article
- NMR resonance assignment of the N-terminal GTPase domain of human Miro2 Bound to GTP.Biomolecular NMR assignments · 2022Article
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- Article
- Dietary Alterations in Impaired Mitochondrial Dynamics Due to Neurodegeneration.Frontiers in aging neuroscience · 2022Article
- Mitochondrial adaptor TRAK2 activates and functionally links opposing kinesin and dynein motors.Nature communications · 2021Article
- Motor proteins at the mitochondria-cytoskeleton interface.Journal of cell science · 2021Review
- Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.Journal of structural biology · 2020Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Mitochondria are dynamically transported in and out of neuronal processes to maintain neuronal excitability and synaptic function. In higher eukaryotes, the mitochondrial GTPase Miro binds Milton/TRAK adaptor proteins linking microtubule motors to mitochondria. Here we show that Drosophila Miro (dMiro), which has previously been shown to be required for kinesin-driven axonal transport, is also critically required for the dynein-driven distribution of mitochondria into dendrites. In addition, we used the loss-of-function mutations dMiroT25N and dMiroT460N to determine the significance of dMiro's N-terminal and C-terminal GTPase domains, respectively. Expression of dMiroT25N in the absence of endogenous dMiro caused premature lethality and arrested development at a pupal stage. dMiroT25N accumulated mitochondria in the soma of larval motor and sensory neurons, and prevented their kinesin-dependent and dynein-dependent distribution into axons and dendrites, respectively. dMiroT25N mutant mitochondria also were severely fragmented and exhibited reduced kinesin and dynein motility in axons. In contrast, dMiroT460N did not impair viability, mitochondrial size, or the distribution of mitochondria. However, dMiroT460N reduced dynein motility during retrograde mitochondrial transport in axons. Finally, we show that substitutions analogous to the constitutively active Ras-G12V mutation in dMiro's N-terminal and C-terminal GTPase domains cause neomorphic phenotypic effects that are likely unrelated to the normal function of each GTPase domain. Overall, our analysis indicates that dMiro's N-terminal GTPase domain is critically required for viability, mitochondrial size, and the distribution of mitochondria out of the neuronal soma regardless of the employed motor, likely by promoting the transition from a stationary to a motile state.
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