Affinage

RHOT2

Mitochondrial Rho GTPase 2 · UniProt Q8IXI1

Round 2 corrected
Length
618 aa
Mass
68.1 kDa
Annotated
2026-04-28
48 papers in source corpus 21 papers cited in narrative 21 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

RHOT2 (Miro2) is an atypical outer mitochondrial membrane Rho GTPase that integrates Ca²⁺ sensing, organelle trafficking, mitochondrial quality control, and stress signaling. Its tandem GTPase domains flanking two EF-hand Ca²⁺-binding motifs enable Ca²⁺-dependent arrest of mitochondrial motility and coordinate both microtubule-based transport (via TRAK adaptor–kinesin/dynein complexes) and actin-based transport (as a direct receptor for myosin XIX), while also localizing to peroxisomes to negatively regulate Drp1-dependent fission (PMID:12482879, PMID:19098100, PMID:30111583, PMID:31894645). Upon mitochondrial damage, PINK1 phosphorylates Miro2 at Ser325/Ser430, triggering its demultimerization and Parkin-dependent ubiquitination and degradation, which arrests damaged mitochondria and provides a platform for Parkin translocation during mitophagy; Miro2 knockout mice display lactic acidosis, reticulocyte maturation defects, and cardiac dysfunction (PMID:22078885, PMID:23503661, PMID:36659543). Beyond trafficking, Miro2 engages GCN1 to activate GCN2–ATF4 stress signaling under hypoxia, promotes cancer invasion through MYO9B-mediated suppression of RhoA, and drives intercellular mitochondrial transfer that induces cancer-associated fibroblast differentiation (PMID:34992146, PMID:39723893, PMID:40877413).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2002 High

    Identification of Miro-1 and Miro-2 as a novel class of mitochondria-localized atypical Rho GTPases with tandem GTPase domains and EF-hand motifs established a new gene family dedicated to mitochondrial homeostasis rather than canonical Rho signaling.

    Evidence Immunolocalization and constitutively active mutant overexpression in NIH3T3/COS7 cells with apoptosis readout

    PMID:12482879

    Open questions at the time
    • No direct biochemical measurement of GTPase activity
    • Functional distinction between Miro-1 and Miro-2 not resolved
  2. 2006 High

    Discovery that Miro GTPases physically interact with TRAK-family kinesin adaptors (GRIF-1/OIP106) linked outer mitochondrial membrane anchoring to the microtubule motor transport machinery, answering how mitochondria are connected to cytoskeletal motors.

    Evidence Co-immunoprecipitation and domain mutagenesis with mitochondrial morphology analysis

    PMID:16630562

    Open questions at the time
    • Direct reconstitution of Miro–TRAK–kinesin complex not yet achieved
    • Relative contribution of Miro-1 vs Miro-2 unclear
  3. 2008 High

    EF-hand mutagenesis demonstrated that Miro GTPases act as Ca²⁺-sensitive molecular switches: low Ca²⁺ promotes motility and suppresses Drp1-mediated fission, while elevated Ca²⁺ arrests transport and activates fission, resolving how calcium signals are transduced to mitochondrial dynamics.

    Evidence Live-cell imaging of mitochondrial motility with EF-hand mutants and Ca²⁺ manipulation in H9c2 cells and primary neurons

    PMID:19098100

    Open questions at the time
    • Direct Ca²⁺ binding affinity of individual EF-hands not measured
    • Mechanism by which Miro communicates with Drp1 undefined
  4. 2009 High

    The finding that PINK1 forms a complex with Miro and Milton placed Miro within the PINK1 Parkinson's disease pathway, raising the question of whether Miro is a direct PINK1 substrate.

    Evidence Affinity purification/mass spectrometry, Co-IP, and genetic epistasis (Miro/Milton rescue of PINK1 loss-of-function morphology)

    PMID:19152501

    Open questions at the time
    • Phosphorylation sites not mapped
    • Parkin involvement not yet established
  5. 2011 High

    Demonstration that PINK1 phosphorylates Miro to trigger Parkin-dependent proteasomal degradation, detaching kinesin and arresting mitochondrial motility, established the molecular mechanism by which damaged mitochondria are quarantined before mitophagy.

    Evidence In vitro PINK1 kinase assay on Miro, Parkin-dependent ubiquitination, proteasome inhibitor rescue, live imaging in neurons

    PMID:22078885

    Open questions at the time
    • Specific phosphorylation sites on Miro-2 not identified in this study
    • Contribution of Miro-2 vs Miro-1 to this pathway not dissected
  6. 2013 High

    Quantitative diGly proteomics confirmed Miro-2 as a direct Parkin ubiquitination substrate upon depolarization, providing site-level evidence for its regulated turnover during mitophagy.

    Evidence Quantitative ubiquitin-remnant capture proteomics in PARKIN-expressing cells treated with CCCP

    PMID:23503661

    Open questions at the time
    • Functional consequence of individual ubiquitination sites not tested
  7. 2018 High

    Identification of Miro1/2 as direct receptors for myosin XIX, regulated by the nucleotide state of the N-terminal GTPase domain, revealed that Miro coordinates both microtubule- and actin-based mitochondrial transport through competitive adaptor binding (TRAK vs Myo19).

    Evidence BioID proximity labeling, in vitro pulldown with purified fragments, protein stability assays upon Miro knockdown

    PMID:30111583

    Open questions at the time
    • Structural basis of the Miro–Myo19 interface unresolved
    • Whether TRAK and Myo19 binding is mutually exclusive on the same Miro molecule not formally proven
  8. 2019 High

    Miro2 was shown to regulate inter-mitochondrial nanotunnel communication in cardiomyocytes, with Parkin-mediated Miro2 degradation during cardiac hypertrophy impairing this communication, expanding Miro2's role beyond transport to mitochondrial network coordination in the heart.

    Evidence Photoactivatable GFP content transfer assay, adenoviral and transgenic Miro2 overexpression, transverse aortic constriction model

    PMID:31455181

    Open questions at the time
    • Molecular mechanism of nanotunnel formation by Miro2 undefined
    • Whether Miro1 has redundant roles in cardiac nanotunneling untested
  9. 2019 High

    Biochemical demonstration that Miro2 undergoes PINK1-dependent demultimerization (tetramer to monomer) upon depolarization, requiring Ser325/Ser430 phosphorylation and EF2-hand Ca²⁺ binding, resolved how Miro2 conformational changes serve as a platform for Parkin translocation; Miro2 knockout mice exhibited lactic acidosis and cardiac disorders.

    Evidence Native PAGE for oligomeric state, CCCP-induced mitophagy, phosphosite and EF-hand mutagenesis, Miro2 KO mouse phenotyping

    PMID:36659543

    Open questions at the time
    • Structural basis of the tetramer and monomer forms not determined at atomic resolution
    • Whether disease-associated mutations alter oligomerization in patients not tested directly
  10. 2020 High

    Discovery that Miro1/2 localize to peroxisomes via Pex19-mediated transmembrane domain insertion and negatively regulate Drp1-dependent peroxisomal fission extended Miro function beyond mitochondria to a second organelle.

    Evidence Fluorescence microscopy, GTPase domain mutants, Co-IP of Miro TM domain with Pex19, peroxisomal morphology upon Miro knockdown

    PMID:31894645

    Open questions at the time
    • Fraction of total Miro pool on peroxisomes vs mitochondria not quantified
    • Whether peroxisomal Miro participates in Ca²⁺ sensing unknown
  11. 2022 Medium

    MIRO2 was found to interact with GCN1 and activate the GCN2–ATF4 integrated stress response in hypoxic tumor regions, revealing a non-trafficking function as a mitochondrial stress signaling scaffold that supports tumor growth.

    Evidence Co-IP, siRNA knockdown, patient mutation functional analysis, xenograft mouse model, GCN2 kinase and ATF4 induction assays

    PMID:34992146

    Open questions at the time
    • Whether GCN1 binding is direct or within a larger complex not established by reconstitution
    • Structural basis of the Miro2–GCN1 interaction unknown
    • Not independently replicated
  12. 2024 High

    Two parallel studies expanded Miro2 effector biology: CBS-derived H₂S sulfhydrates Miro2 at Cys185/Cys504 to maintain mitochondrial dynamics and cytotrophoblast invasion, and Miro2 cooperates with MYO9B to suppress RhoA and promote cancer invasion and metastasis, establishing Miro2 as a signaling node linking mitochondrial state to cell motility and tumor progression.

    Evidence Site-directed mutagenesis (C185S/C504S) with sulfhydration assays and invasion rescue (PMID:39461943); reciprocal Co-IP, epistasis (MIRO2/RhoA double knockout), and mouse metastasis models (PMID:39723893)

    PMID:39461943 PMID:39723893

    Open questions at the time
    • Sulfhydration at Cys185/Cys504 not yet confirmed by mass spectrometry with site identification
    • Whether MYO9B interaction depends on GTPase domain nucleotide state unknown
  13. 2025 High

    Miro2 was shown to drive intercellular mitochondrial transfer from cancer cells to fibroblasts, inducing CAF differentiation and a protumorigenic secretome, and to selectively control mitochondrial positioning and glucagon secretion in pancreatic alpha cells, revealing tissue-specific trafficking functions.

    Evidence Co-culture transfer assays and xenograft models (PMID:40877413); siRNA knockdown in mouse islets with secretion and ATP/ADP subcellular measurements (PMID:41308986)

    PMID:40877413 PMID:41308986

    Open questions at the time
    • Mechanism of selective Miro2 (vs Miro1) requirement in alpha cells not defined
    • Molecular machinery mediating intercellular mitochondrial transfer downstream of Miro2 unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Major unresolved questions include the atomic structure of full-length Miro2 (including the linker and EF-hands), how Miro2 partitions between mitochondrial and peroxisomal membranes, whether Miro2's stress-signaling (GCN1) and trafficking roles are coordinated or independent, and the extent to which Miro1 and Miro2 are functionally redundant in vivo.
  • No full-length Miro2 structure determined
  • Functional redundancy with Miro1 not systematically tested across tissues
  • Integration of stress-signaling and trafficking functions uncharacterized

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003924 GTPase activity 3 GO:0060090 molecular adaptor activity 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005739 mitochondrion 8 GO:0005777 peroxisome 1 GO:0005886 plasma membrane 1
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 4 R-HSA-9612973 Autophagy 4 R-HSA-1643685 Disease 3 R-HSA-8953897 Cellular responses to stimuli 3 R-HSA-9609507 Protein localization 3
Partners
CISD1GCN1MYO19MYO9BPINK1PRKNTRAK1TRAK2
Complex memberships
Miro–Myo19 actin transport complexMiro–TRAK–kinesin/dynein transport complexPINK1–Miro–Parkin mitophagy complex

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 Miro-1 and Miro-2 (RHOT1/RHOT2) were identified as a new family of atypical Rho GTPases localized to mitochondria, containing tandem GTP-binding domains flanking EF-hand calcium-binding motifs and a C-terminal transmembrane domain. Overexpression of constitutively active Miro-1 induced mitochondrial network aggregation and increased apoptotic rate, indicating a role in mitochondrial homeostasis. Immunolocalization of transfected and endogenous Miro in NIH3T3 and COS7 cells; constitutively active mutant overexpression with apoptosis readout The Journal of biological chemistry High 12482879
2004 Miro-2 localizes to mitochondria and, unlike other Rho GTPases, has no major influence on actin filament organization, consistent with its dedicated mitochondrial role. Transfection into porcine aortic endothelial cells with actin filament staining and immunolocalization The Biochemical journal Medium 14521508
2004 Mouse Arht2 (ortholog of human RHOT2/Miro-2) is ubiquitously expressed and in testis shows expression in residual bodies and during spermiogenesis, suggesting a role in testis differentiation; it maps to mouse chromosome 17A3.3 and comprises 19 exons. RT-PCR across developmental stages, in situ hybridization in mouse testis, genomic mapping Cytogenetic and genome research Low 15218247
2006 Miro-1 and Miro-2 interact with kinesin-binding adaptor proteins GRIF-1 and OIP106 (TRAK family), establishing that the Miro GTPases form a physical link between mitochondria and the microtubule trafficking apparatus. The first GTPase domain of Miro-1 is required for mitochondrial clustering, whereas Miro-2 induces only aggregation and not thread-like mitochondria. Co-immunoprecipitation, overexpression of constitutively active mutants, mitochondrial morphology analysis Biochemical and biophysical research communications High 16630562
2008 Miro GTPases (Miro-1 and Miro-2) act as Ca2+-sensitive switches for mitochondrial motility: overexpression of Miro enhances mitochondrial movement at resting Ca2+, whereas elevated Ca2+ arrests mitochondrial motility in an EF-hand-dependent manner. Miro also regulates mitochondrial fusion/fission balance by suppressing Drp1 at low Ca2+ and activating Drp1 at high Ca2+, and increases dendritic mitochondrial mass in primary neurons. Miro overexpression and EF-hand mutants in H9c2 cells and primary neurons; live-cell imaging of mitochondrial motility; Ca2+ manipulation experiments Proceedings of the National Academy of Sciences of the United States of America High 19098100
2009 PINK1 forms a multiprotein complex with Miro (Miro-1/Miro-2) and Milton at the outer mitochondrial membrane. Overexpression of Miro and Milton increases the mitochondrial PINK1 pool, and Miro/Milton expression suppresses altered mitochondrial morphology induced by loss of PINK1, placing Miro in the PINK1 pathway for mitochondrial trafficking. Affinity purification/mass spectrometry screen, Co-immunoprecipitation, subcellular fractionation, genetic epistasis (Miro/Milton rescue of pink1 loss-of-function morphology) Biochemistry High 19152501
2011 PINK1 phosphorylates Miro (including Miro-2/RHOT2), which activates Parkin-dependent proteasomal degradation of Miro, thereby detaching kinesin from the mitochondrial surface and arresting mitochondrial movement. This PINK1→Miro phosphorylation→Parkin-mediated Miro degradation axis quarantines damaged mitochondria prior to mitophagy. In vitro kinase assay (PINK1 phosphorylation of Miro), proteasome inhibitor rescue, Parkin-dependent ubiquitination assays, live-cell imaging of mitochondrial motility in neurons Cell High 22078885
2013 Miro proteins (including Miro-2/RHOT2) on the outer mitochondrial membrane are substrates of PARKIN-dependent ubiquitylation upon mitochondrial depolarization, as determined by quantitative diGly ubiquitin-remnant proteomics. Quantitative diGly capture proteomics upon mitochondrial depolarization in cells expressing PARKIN Nature High 23503661
2018 Miro1 and Miro2 are direct mitochondrial receptors for myosin XIX (Myo19), an actin-based motor. Miro1 binds directly to a C-terminal fragment of the Myo19 tail, recruits Myo19 in vivo, and Myo19 protein stability depends on its association with Miro1/2. The interaction is regulated by the nucleotide state of the N-terminal Rho-like GTPase domain of Miro1/2. Downregulation of Miro1/2 or overexpression of TRAK1/2 reduces Myo19 levels. This establishes Miro1/2 as coordinators of both microtubule- and actin-based mitochondrial movement. Proximity labeling (BioID), direct binding assays (pulldown with purified fragments), in vivo co-localization/recruitment, protein stability assays upon Miro knockdown Journal of cell science High 30111583
2018 Inhibition of NOS3 in glial cells prevents axonal mitochondrial fission and restores mitochondrial motility in ischemic white matter by preserving Miro-2 protein levels, linking NO-mediated oxidative stress to Miro-2 degradation as a mechanism of mitochondrial dysfunction. Pharmacological NOS3 inhibition and NOS3 genetic deletion in mouse optic nerve; electrophysiology, 3D electron microscopy, measurement of Miro-2 protein levels The Journal of neuroscience Medium 29891729
2019 Miro2 expression levels regulate inter-mitochondrial communication (nanotunneling and kissing) along microtubules in adult cardiomyocytes. Adenovirus-mediated Miro2 overexpression increases nanotunnel formation, while Parkin-mediated ubiquitination leads to Miro2 degradation during cardiac hypertrophy, impairing inter-mitochondrial communication and cardiac function. Mitochondria-targeted photoactivatable GFP for content transfer assay, adenoviral Miro2 overexpression, Miro2 transgenic mice, transverse aortic constriction model, proteasome inhibition, Parkin overexpression Circulation research High 31455181
2019 Miro2 supplies a platform for Parkin translocation to damaged mitochondria during mitophagy. Upon mitochondrial depolarization (CCCP treatment), Miro2 undergoes demultimerization from tetramer to monomer and changes localization. This realignment requires PINK1-mediated phosphorylation at Ser325/Ser430 and Ca2+ binding to the EF2 domain, and is essential for subsequent Parkin recruitment. Miro2 ablation in mice causes delayed reticulocyte maturation, lactic acidosis, and cardiac disorders. Native PAGE and biochemical fractionation for oligomeric state; CCCP-induced mitophagy assay; phosphorylation-site mutagenesis; EF-hand Ca2+-binding mutants; Miro2 knockout mouse phenotyping; patient mutation analysis Science bulletin High 36659543
2020 Miro1 and Miro2 localize to peroxisomes (in addition to mitochondria) and negatively regulate Drp1-dependent peroxisomal fission to maintain peroxisomal size and morphology. Peroxisomal localization of Miro is regulated by its first GTPase domain and mediated by interaction of its transmembrane domain with the peroxisomal membrane protein chaperone Pex19. Fluorescence microscopy for Miro localization to peroxisomes, Miro knockdown with peroxisomal morphology readout, GTPase domain mutants, co-immunoprecipitation of Miro transmembrane domain with Pex19 EMBO reports High 31894645
2020 Miro2 is a direct target of miR-351-5p in hippocampal neural progenitor cells. Downregulation of Miro2 by siRNA or miR-351-5p causes excessive mitochondrial fragmentation, decreased mitochondrial membrane potential, increased ROS, induction of PINK1/Parkin-mediated mitophagy, and cell death. Ectopic Miro2 expression rescues these effects, and inhibition of mitochondrial fission (Mdivi-1) blocks miR-351-5p-induced cell death. siRNA knockdown, adenoviral Miro2 overexpression, miR-351-5p transfection, mitochondrial morphology imaging, membrane potential assay, ROS measurement, mitophagy markers, Mdivi-1 pharmacological rescue Molecular therapy. Nucleic acids Medium 33575111
2022 MIRO2 interacts with GCN1 in prostate cancer cells and is required for efficient GCN1-mediated GCN2 kinase signaling and induction of ATF4. A MIRO2 patient mutation (159L) increases GCN1 binding. MIRO2 depletion impairs cell growth, colony formation, and tumor growth. MIRO2 and activated GCN2 are enriched in hypoxic tumor areas, defining a MIRO2-GCN1-GCN2-ATF4 mitochondrial stress-signaling pathway. Network/interactome analysis, Co-immunoprecipitation, siRNA knockdown, MIRO2 mutation functional analysis, xenograft mouse model, GCN2 kinase activity assays, ATF4 induction assays Molecular cancer research Medium 34992146
2022 NMR backbone chemical shift assignments of the N-terminal GTPase (nGTPase) domain of human Miro2 (residues 1–180) bound to GTP were determined, confirming that the secondary structure closely resembles that of Miro1 nGTPase-GTP with only minor variations attributable to crystal packing in the Miro1 structure. Solution NMR spectroscopy (backbone resonance assignment of 22 kDa construct) Biomolecular NMR assignments Medium 36050579
2024 Miro2 is sulfhydrated by H2S (produced by CBS) at Cys185 and Cys504. This post-translational modification preserves mitochondrial dynamics and is required for cytotrophoblast invasion and migration. Knockdown of Miro2 or double mutation of Miro2-C185S/C504S fragments mitochondria and inhibits cell invasion and migration, and these effects cannot be rescued by H2S, placing CBS/H2S upstream of Miro2 sulfhydration. H2S donor treatment, CBS knockdown, site-directed mutagenesis (C185S/C504S), sulfhydration detection assay, mitochondrial morphology imaging, invasion/migration assays Cell death & disease Medium 39461943
2024 MIRO2 promotes cancer cell invasion and metastasis through its binding partner unconventional myosin 9B (MYO9B). MIRO2 depletion reduces tumor invasion in vitro and metastatic burden in vivo. Mechanistically, MIRO2/MYO9B cooperation suppresses active RhoA; dual ablation of MIRO2 and RhoA fully rescues invasion, establishing MIRO2→MYO9B→RhoA suppression as the relevant pathway. Co-immunoprecipitation (MIRO2-MYO9B interaction), siRNA knockdown of MIRO2 and MYO9B, RhoA activity assay, genetic epistasis (dual MIRO2/RhoA knockout), in vitro invasion assay, mouse metastasis models (prostate and breast cancer) Cell reports High 39723893
2025 MIRO2 is required for mitochondrial transfer from cancer cells to fibroblasts, which induces cancer-associated fibroblast (CAF) differentiation. MIRO2 depletion in cancer cells suppresses mitochondrial transfer, CAF marker expression, protumorigenic secretome release, and tumor growth in xenograft models. MIRO2 is overexpressed at the leading edge of epithelial skin cancers. Co-culture mitochondrial transfer assay, xenograft tumor models, MIRO2 siRNA/CRISPR depletion, metabolic profiling of recipient fibroblasts, CAF marker analysis Nature cancer High 40877413
2025 Miro2 (but not Miro1) is specifically required for mitochondrial motility in pancreatic alpha cells, and its knockdown impairs glucose-induced inhibition of glucagon secretion without affecting insulin secretion or mitochondrial motility in beta cells. Under low glucose, mitochondria localize further from the nucleus and correlate with increased sub-plasma membrane ATP/ADP, revealing a Miro2-dependent mechanism coupling mitochondrial positioning to glucagon secretion. siRNA knockdown of Miro1 and Miro2 in mouse islets, live-cell mitochondrial motility imaging, glucagon/insulin secretion assays, subcellular ATP/ADP sensor measurements The Journal of biological chemistry Medium 41308986
2026 Proximity labeling (TurboID) in hippocampal neural stem cells identified 66 Miro2-specific interactors, with CISD1 as a top hit. Knockdown of either Miro2 or CISD1 impairs mitochondrial trafficking and stem cell differentiation with increased cytotoxicity; both proteins show increased expression and interaction during differentiation. Rescue experiments partially reverse cell death. TurboID proximity labeling, affinity-MS interactomics, siRNA knockdown of Miro2 and CISD1, mitochondrial motility assays, differentiation assays Communications biology Medium 41663665

Source papers

Stage 0 corpus · 48 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2011 PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility. Cell 951 22078885
2013 Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization. Nature 870 23503661
2020 A reference map of the human binary protein interactome. Nature 849 32296183
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2003 Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature genetics 754 14702039
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2015 SLC38A9 is a component of the lysosomal amino acid sensing machinery that controls mTORC1. Nature 548 25561175
2008 Bidirectional Ca2+-dependent control of mitochondrial dynamics by the Miro GTPase. Proceedings of the National Academy of Sciences of the United States of America 456 19098100
2004 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome research 438 15489334
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2018 DNA Repair Network Analysis Reveals Shieldin as a Key Regulator of NHEJ and PARP Inhibitor Sensitivity. Cell 379 29656893
2006 The atypical Rho GTPases Miro-1 and Miro-2 have essential roles in mitochondrial trafficking. Biochemical and biophysical research communications 355 16630562
2021 A proximity-dependent biotinylation map of a human cell. Nature 339 34079125
2002 Atypical Rho GTPases have roles in mitochondrial homeostasis and apoptosis. The Journal of biological chemistry 323 12482879
2004 Rho GTPases have diverse effects on the organization of the actin filament system. The Biochemical journal 319 14521508
2004 Functional proteomics mapping of a human signaling pathway. Genome research 247 15231748
2021 Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context. Cell metabolism 239 34800366
2014 Glucose regulates mitochondrial motility via Milton modification by O-GlcNAc transferase. Cell 231 24995978
2009 Pink1 forms a multiprotein complex with Miro and Milton, linking Pink1 function to mitochondrial trafficking. Biochemistry 230 19152501
2016 Mitochondrial Protein Interaction Mapping Identifies Regulators of Respiratory Chain Function. Molecular cell 220 27499296
2012 Voltage-dependent anion channels (VDACs) recruit Parkin to defective mitochondria to promote mitochondrial autophagy. The Journal of biological chemistry 208 23060438
2018 An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations. Nature communications 201 29568061
2013 Interlaboratory reproducibility of large-scale human protein-complex analysis by standardized AP-MS. Nature methods 170 23455922
2019 A protein-interaction network of interferon-stimulated genes extends the innate immune system landscape. Nature immunology 159 30833792
2020 A High-Density Human Mitochondrial Proximity Interaction Network. Cell metabolism 148 32877691
2018 Identification of Miro1 and Miro2 as mitochondrial receptors for myosin XIX. Journal of cell science 86 30111583
2020 Miro2 tethers the ER to mitochondria to promote mitochondrial fusion in tobacco leaf epidermal cells. Communications biology 41 32246085
2020 Peroxisomal fission is modulated by the mitochondrial Rho-GTPases, Miro1 and Miro2. EMBO reports 39 31894645
2019 Miro2 Regulates Inter-Mitochondrial Communication in the Heart and Protects Against TAC-Induced Cardiac Dysfunction. Circulation research 36 31455181
2020 miR-351-5p/Miro2 axis contributes to hippocampal neural progenitor cell death via unbalanced mitochondrial fission. Molecular therapy. Nucleic acids 23 33575111
2022 MIRO2 Regulates Prostate Cancer Cell Growth via GCN1-Dependent Stress Signaling. Molecular cancer research : MCR 22 34992146
2018 NOS3 Inhibition Confers Post-Ischemic Protection to Young and Aging White Matter Integrity by Conserving Mitochondrial Dynamics and Miro-2 Levels. The Journal of neuroscience : the official journal of the Society for Neuroscience 18 29891729
2011 Arabidopsis thaliana MIRO1 and MIRO2 GTPases are unequally redundant in pollen tube growth and fusion of polar nuclei during female gametogenesis. PloS one 18 21494602
2025 MIRO2-mediated mitochondrial transfer from cancer cells induces cancer-associated fibroblast differentiation. Nature cancer 11 40877413
2012 Genetic Screening of the Mitochondrial Rho GTPases MIRO1 and MIRO2 in Parkinson's Disease. The open neurology journal 10 22496713
2019 Miro2 supplies a platform for Parkin translocation to damaged mitochondria. Science bulletin 9 36659543
2024 Miro2 sulfhydration by CBS/H2S promotes human trophoblast invasion and migration via regulating mitochondria dynamics. Cell death & disease 8 39461943
2020 The role of RHOT1 and RHOT2 genetic variation on Parkinson disease risk and onset. Neurobiology of aging 7 32948353
2024 MIRO2 promotes cancer invasion and metastasis via MYO9B suppression of RhoA activity. Cell reports 4 39723893
2004 Cloning and characterization of the mouse Arht2 gene which encodes a putative atypical GTPase. Cytogenetic and genome research 4 15218247
2026 Proximity labeling unveils potential roles of the Miro2-CISD1 network in mitochondrial dynamics and neuronal differentiation. Communications biology 0 41663665
2025 Mitochondrial movement in pancreatic alpha cells requires Miro2 and is regulated by glucose. The Journal of biological chemistry 0 41308986
2022 NMR resonance assignment of the N-terminal GTPase domain of human Miro2 Bound to GTP. Biomolecular NMR assignments 0 36050579