Affinage

TBC1D15

TBC1 domain family member 15 · UniProt Q8TC07

Length
691 aa
Mass
79.5 kDa
Annotated
2026-06-10
27 papers in source corpus 18 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/7 claims corpus-supported (86%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

TBC1D15 is a Rab7-selective GTPase-activating protein (GAP) that couples late-endosomal/lysosomal Rab7-GTP regulation to mitochondrial dynamics, membrane-contact-site biology, and autophagic flux (PMID:20363736). Its GAP activity is selective for Rab7 over Rab4, Rab5, and Rab11, lowers cellular Rab7-GTP, fragments lysosomes, and confers resistance to growth-factor-withdrawal death (PMID:20363736); crystal structures of the GAP domain confirm a conserved TBC fold whose catalytic arginine and glutamine residues are essential for activity (PMID:28168758). TBC1D15 is recruited to the mitochondrial outer membrane through a direct, reconstituted complex with FIS1, and loss of either protein produces a hyperfused mitochondrial network independently of DRP1 (PMID:23077178, PMID:37777154). At mitochondria it functions through two interaction surfaces — its FIS1-binding domain and its Rab7-GAP domain — to govern mitochondria-lysosome contacts (PMID:33042281), and through its C-terminal domain (574-624) it recruits DRP1 to these contacts to drive asymmetrical mitochondrial fission (PMID:35680100). By controlling Rab7 activity TBC1D15 sets a brake on autophagic flux: its depletion or downregulation (via the IFN-β-induced miR-1 axis) raises autophagy (PMID:31958036), and following lysosomal membrane damage ATG8 recruits TBC1D15 to scaffold the autophagic lysosomal reformation machinery (dynamin-2, kinesin-5B, clathrin) for membrane regeneration (PMID:37024685). The same Rab7-GAP activity routes cargo through the late-endosomal system, controlling GLUT4 surface availability and glucose uptake (PMID:30316925) and, with Annexin A6, late-endosomal cholesterol handling (PMID:31664461). Beyond GTPase regulation, TBC1D15 destabilizes the Numb-p53 complex via its N-terminal domain to promote stem-cell self-renewal (PMID:23468968), stabilizes NOTCH1 by blocking CDK8/CDK19 phosphodegron phosphorylation (PMID:38409448), and links mitochondria to lipid droplets through a PLIN5 interaction that enhances fatty-acid β-oxidation (PMID:40334909).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 2010 High

    Established the core biochemical identity of TBC1D15 as a substrate-selective Rab7 GAP with a defined cellular consequence, answering what GTPase it regulates.

    Evidence RILP effector pulldown of Rab7-GTP, lysosomal morphology imaging, cell survival assays in cells

    PMID:20363736

    Open questions at the time
    • Did not resolve how TBC1D15 is localized to its site of action
    • Substrate range beyond Rab4/5/7/11 not exhaustively tested
  2. 2012 High

    Resolved how TBC1D15 reaches mitochondria, showing FIS1 is a direct recruitment factor and that the pair restrains mitochondrial fusion independently of Drp1.

    Evidence In vitro binding with bacterially expressed proteins, reciprocal Co-IP, localization microscopy, and siRNA morphology readout

    PMID:23077178

    Open questions at the time
    • How FIS1 binding relates to Rab7-GAP activity unresolved
    • Did not define the mitochondrial fission machinery linkage
  3. 2013 Medium

    Extended TBC1D15 function beyond GTPase regulation into transcription/stemness control by identifying a Numb-p53-destabilizing activity.

    Evidence Affinity purification/MS, Co-IP, domain mapping, self-renewal and pluripotency assays

    PMID:23468968

    Open questions at the time
    • Mechanism of p53 disengagement from Numb not structurally defined
    • Relationship to GAP activity unclear
  4. 2013 Medium

    Placed TBC1D15 upstream of Rab7 in a developmental context, using Drosophila epistasis to confirm directionality of the GAP-Rab7 relationship in vivo.

    Evidence Drosophila loss-of-function and RNAi with constitutively active/dominant-negative Rab7 epistasis at the NMJ

    PMID:23812537

    Open questions at the time
    • Mammalian synaptic relevance not tested
    • Effectors downstream of Rab7 not identified
  5. 2013 Medium

    Linked TBC1D15 to RhoA-dependent membrane and cytokinetic dynamics, broadening its role in cell division.

    Evidence siRNA knockdown, RhoA activation assay, blebbing quantification, RhoA inhibitor, cytokinesis imaging

    PMID:24337944

    Open questions at the time
    • Direct molecular link between TBC1D15 and RhoA regulation not established
    • Whether this requires Rab7-GAP activity unknown
  6. 2017 High

    Provided the structural and catalytic basis of GAP activity, defining the essential active-site residues.

    Evidence X-ray crystallography of shark and pig GAP domains, in vitro GAP assays, active-site mutagenesis

    PMID:28168758

    Open questions at the time
    • No structure of full-length protein or substrate complex
    • Determinants of Arl4D vs Rab7 selectivity not defined
  7. 2017 Medium

    Distinguished TBC1D15's role in innate immunity from its fission function, showing a Drp1-independent requirement for STING competency.

    Evidence siRNA knockdown, STING reporter assays, genetic epistasis with Drp1 and NLRP3

    PMID:28729291

    Open questions at the time
    • Molecular mechanism connecting TBC1D15 to STING not defined
    • Whether Rab7-GAP activity is involved unknown
  8. 2018 Medium

    Connected Rab7-GAP activity to physiological cargo handling, showing TBC1D15 controls GLUT4 routing and glucose uptake.

    Evidence CRISPR/Cas9 knockout, glucose uptake assay, GLUT4 western blot, Rab7/Lamp1 co-localization

    PMID:30316925

    Open questions at the time
    • Whether GLUT4 effect is direct or systemic not resolved
    • In vivo metabolic relevance untested
  9. 2019 Medium

    Embedded TBC1D15 in a regulatory axis controlling late-endosomal cholesterol transfer via Annexin A6 and membrane contact sites.

    Evidence Co-IP, late-endosome localization microscopy, cholesterol assays, EM of contact sites, depletion in NPC1 mutant cells

    PMID:31664461

    Open questions at the time
    • Whether AnxA6 directly modulates TBC1D15 catalysis unknown
    • Stoichiometry of the AnxA6-TBC1D15 complex undefined
  10. 2020 Medium

    Defined two distinct interaction surfaces (FIS1-binding and GAP) as jointly required for tuning mitochondria-lysosome contact duration in cardiac injury.

    Evidence Domain-specific mutant rescue, TEM of contacts, live-cell imaging, mitophagy flux, adenoviral cardiac overexpression in mice

    PMID:33042281

    Open questions at the time
    • How the two domains are coordinated mechanistically unresolved
    • Single disease model
  11. 2020 Medium

    Identified a conserved miR-1-TBC1D15-Rab7 regulatory pathway by which IFN-β raises autophagic flux.

    Evidence miRNA overexpression, knockdown, Rab7 activity measurement, autophagy flux assays, C. elegans validation

    PMID:31958036

    Open questions at the time
    • Direct miR-1 targeting of TBC1D15 transcript not fully mapped
    • Physiological IFN-β contexts limited
  12. 2022 Medium

    Pinpointed the C-terminal 574-624 region as the DRP1-recruiting module that enables asymmetrical mitochondrial fission at contact sites.

    Evidence Co-IP, time-lapse confocal microscopy, Δ574-624 deletion, cardiac KO/KI mice, adenoviral rescue

    PMID:35680100

    Open questions at the time
    • Structural basis of TBC1D15-DRP1 binding not solved
    • How fission asymmetry is spatially determined unclear
  13. 2023 High

    Revealed a scaffolding role downstream of lysosomal damage, where ATG8 recruits TBC1D15 to assemble the autophagic lysosomal reformation machinery for membrane regeneration.

    Evidence Proximity-labeling proteomics, Co-IP, high-resolution microscopy, depletion of TBC1D15 and ALR components, lysosomal damage model

    PMID:37024685

    Open questions at the time
    • Whether GAP catalysis is required for ALR scaffolding unresolved
    • Interaction interfaces with ATG8 and ALR components not mapped
  14. 2023 Medium

    Mapped a FIS1 SKY insert as the determinant of TBC1D15 and DRP1 mitochondrial docking, linking FIS1 intramolecular regulation to fission machinery recruitment.

    Evidence Site-directed mutagenesis, Co-IP, YFP-TBC1D15 localization microscopy, morphology analysis in HCT116 cells

    PMID:37777154

    Open questions at the time
    • Structural mechanism of SKY-mediated regulation undefined
    • How SKY state is physiologically controlled unknown
  15. 2023 Medium

    Identified a non-GAP nuclear/DNA-damage role, with a 594-624 segment binding DNA-PKcs to promote its cytosolic retention.

    Evidence LC-MS/MS, Co-IP, Δ594-624 deletion, cardiac KO/KI mice, DNA damage assays

    PMID:38045047

    Open questions at the time
    • Overlap of the DNA-PKcs and DRP1 binding regions not reconciled
    • Mechanism of cytosolic retention undefined
  16. 2024 Medium

    Connected TBC1D15 to NOTCH1 stability and NUMB handling, blocking CDK8/CDK19 phosphodegron phosphorylation to prevent FBW7-mediated degradation.

    Evidence ChIP-seq, Co-IP, phosphorylation assays, hepatocyte triple-KO and PDX mouse models

    PMID:38409448

    Open questions at the time
    • How TBC1D15 physically shields the phosphodegron unknown
    • Relationship to mitochondrial functions unclear
  17. 2025 Medium

    Defined a PLIN5-dependent mechanism by which TBC1D15 promotes mitochondria-lipid droplet contacts and fatty-acid β-oxidation.

    Evidence Co-IP, domain mapping (10-180 aa), contact-site immunofluorescence, TEM, PKA inhibitor, hepatocyte overexpression mouse model

    PMID:40334909

    Open questions at the time
    • Whether this is GAP-independent not formally tested
    • Trigger for TBC1D15 mitochondrial translocation upon alcohol exposure undefined
  18. 2026 Medium

    Expanded TBC1D15's substrate range, showing it is also a GAP for the Arf-family GTPase Arl4D acting through its TBC domain.

    Evidence Co-IP, in vitro GAP assay, localization microscopy, knockdown with Arl4D activity readout

    PMID:41709823

    Open questions at the time
    • Determinants of dual Rab7/Arl4D selectivity unresolved
    • Physiological balance between the two substrates unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • It remains unresolved how TBC1D15's GAP catalysis, its FIS1/DRP1 scaffolding at mitochondria, and its GAP-independent protein-stability roles (Numb-p53, NOTCH1, DNA-PKcs) are integrated within a single protein and which functions are coupled versus separable.
  • No full-length structure showing how distinct functional modules coexist
  • Whether GAP activity is required for scaffolding/protein-stability roles untested
  • Tissue- and stimulus-specific selection among functions undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0060090 molecular adaptor activity 4 GO:0098772 molecular function regulator activity 3 GO:0140096 catalytic activity, acting on a protein 3
Localization
GO:0005739 mitochondrion 4 GO:0005764 lysosome 3 GO:0005768 endosome 2 GO:0005829 cytosol 2
Pathway
R-HSA-1852241 Organelle biogenesis and maintenance 3 R-HSA-5653656 Vesicle-mediated transport 2 R-HSA-9612973 Autophagy 2
Partners
ARL4DATG8DRP1FIS1NOTCH1NUMBPLIN5RAB7

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2012 Fis1 acts as a mitochondrial recruitment factor for TBC1D15: Fis1 and TBC1D15 form a direct and stable complex (demonstrated with bacterially expressed proteins), and coexpression with Fis1 relocalized TBC1D15 from cytoplasm to mitochondria. Knockdown of TBC1D15 induced highly developed mitochondrial network structures (hyperfusion) similar to Fis1 knockdown, independently of Drp1. Co-immunoprecipitation, in vitro binding with bacterially expressed proteins, subcellular localization by fluorescence microscopy, siRNA knockdown with mitochondrial morphology readout Journal of cell science High 23077178
2010 TBC1D15 functions as a selective Rab7 GTPase-activating protein (GAP) in cells, reducing Rab7-GTP levels (measured by effector pulldown with RILP), fragmenting lysosomes, and conferring resistance to growth factor withdrawal-induced cell death. TBC1D15 GAP activity was selective for Rab7 and did not affect Rab4-, Rab5-, or Rab11-dependent processes. Effector pulldown assay (RILP binding to Rab7-GTP), lysosomal morphology imaging, cell survival assay, transferrin internalization/recycling assay The Journal of biological chemistry High 20363736
2017 Crystal structures of TBC1D15 GAP domain (shark and pig orthologs) resolved to 2.8 Å and 2.5 Å revealed structural conservation within the TBC1D15 family and showed variations compared to yeast Gyp1p and TBC1D1. Active-site mutagenesis demonstrated that the catalytic arginine and glutamine residues are essential for GAP activity; substitution to alanine or lysine abolished activity. X-ray crystallography, in vitro GAP activity assay, active-site mutagenesis Protein science High 28168758
2013 TBC1D15 was identified as a Numb-associated protein by large-scale affinity purification and tandem mass spectrometry. The amino-terminal domain of TBC1D15 disengages p53 from the Numb-p53 complex, triggering p53 proteolysis and promoting stem cell self-renewal and pluripotency. TBC1D15 protein levels are reduced by autophagy-mediated degradation upon nutrient deprivation. Affinity purification and tandem mass spectrometry, co-immunoprecipitation, domain mapping, cell self-renewal and pluripotency assays, autophagy inhibitor experiments PloS one Medium 23468968
2013 Depletion of TBC1D15 by siRNA induced RhoA activation and membrane blebbing, which was abolished by a RhoA signaling inhibitor. TBC1D15 is also required for proper accumulation of RhoA at the equatorial cortex during cytokinesis, establishing a role for TBC1D15 in regulating RhoA activity during membrane dynamics and cell division. siRNA knockdown, RhoA activation assay, membrane bleb quantification, RhoA inhibitor treatment, fluorescence microscopy of cytokinesis Molecular and cellular biochemistry Medium 24337944
2013 The Drosophila TBC1D15 ortholog Tbc1d15-17 is required for normal presynaptic growth and postsynaptic organization at the NMJ. Loss-of-function or presynaptic knockdown increased synaptic bouton number and NMJ length. Genetic epistasis showed that presynaptic overexpression of constitutively active Rab7 phenocopied tbc1d15-17 mutants (overgrowth), while dominant-negative Rab7 had the opposite effect, placing Tbc1d15-17 upstream of Rab7 in synaptic development. Drosophila genetics (loss-of-function mutant, tissue-specific RNAi), epistasis with constitutively active and dominant-negative Rab7, NMJ morphology analysis Molecules and cells Medium 23812537
2019 Annexin A6 (AnxA6) promotes Rab7 inactivation via TBC1D15 (Rab7-GAP). AnxA6 overexpression induces late endosomal cholesterol accumulation dependent on TBC1D15-mediated Rab7 inactivation. AnxA6 depletion in NPC1 mutant cells leads to Rab7 activation, peripheral redistribution of late endosomes, and StARD3-dependent cholesterol transfer to the ER via membrane contact sites. Co-immunoprecipitation, fluorescence microscopy of late endosome localization, cholesterol accumulation assays, electron microscopy of membrane contact sites, genetic depletion experiments Cellular and molecular life sciences Medium 31664461
2020 TBC1D15 loosens abnormal mitochondria-lysosome contacts after myocardial infarction through both its Fis1-binding domain and its Rab7 GAP domain. Interference with either domain reversed TBC1D15-dependent beneficial effects on lysosomal function and mitophagy flux, establishing that both interaction surfaces are required for TBC1D15's role in mitochondria-lysosome contact regulation. Domain-specific mutant overexpression (Fis1-binding and GAP-domain mutants), transmission electron microscopy of mitochondria-lysosome contacts, live-cell time-lapse imaging, mitophagy flux assay (fluorescence and western blot), adenoviral cardiac overexpression in mice Theranostics Medium 33042281
2022 TBC1D15 directly interacts with Drp1 through its C-terminal domain (residues 574-624), recruiting Drp1 to mitochondria-lysosome contact sites to promote asymmetrical mitochondrial fission. TBC1D15 mutants lacking this domain (Δ574-624) failed to support asymmetrical fission and mitochondrial function, and could not rescue cardiac phenotypes in TBC1D15 knockout mice after I/R injury. Co-immunoprecipitation, time-lapse confocal microscopy, domain-deletion mutant analysis, cardiac-specific knockout/knockin mouse models, adenoviral rescue with wild-type vs. mutant TBC1D15 Metabolism: clinical and experimental Medium 35680100
2023 Following lysosomal membrane damage, LIMP2 acts as a lysophagy receptor to recruit ATG8, which in turn recruits TBC1D15 to damaged lysosomes. TBC1D15 interacts with ATG8 proteins and provides a scaffold to assemble the autophagic lysosomal reformation (ALR) machinery including dynamin-2, kinesin-5B, and clathrin, enabling lysosomal tubulation and scission for membrane regeneration. Proximity-labeling proteomics, co-immunoprecipitation, high-resolution microscopy, genetic depletion of TBC1D15 and ALR components, lysosomal damage model (oxalate nephropathy cell culture) Nature cell biology High 37024685
2017 TBC1D15 knockdown rescued nigericin-induced suppression of the STING innate immune pathway, while knockdown of Drp1 (also rescuing mitochondrial fission) did not restore STING activity. This establishes a specific, Drp1-independent role for TBC1D15 in maintaining STING pathway competency during mitochondrial fragmentation induced by inflammasome-activating signals. siRNA knockdown, STING pathway reporter assays (IFN-β, ISG56), mitochondrial morphology imaging, genetic epistasis between TBC1D15, Drp1, and NLRP3 FASEB journal Medium 28729291
2023 TBC1D15 interacts with DNA-PKcs at its segment 594-624. TBC1D15 promotes cytosolic retention of DNA-PKcs, contributing to DNA damage signaling; a TBC1D15 deletion mutant lacking residues 594-624 failed to elicit cytosolic DNA-PKcs accumulation or exacerbate DOX-induced DNA damage and cardiomyocyte apoptosis. Liquid chromatography-tandem mass spectrometry, co-immunoprecipitation, domain-deletion mutant analysis, cardiac-specific knockout/knockin mouse models, DNA damage assays Acta pharmaceutica Sinica. B Medium 38045047
2018 TBC1D15 knockout (CRISPR/Cas9) caused reduced glucose uptake, decreased total GLUT4 levels, and increased co-localization of GLUT4 with Rab7-positive late endosomes/lysosomes, demonstrating that TBC1D15-mediated Rab7-GAP activity controls GLUT4 routing through the late endosomal pathway to regulate glucose transporter surface availability. CRISPR/Cas9 knockout, 2-NBDG glucose uptake assay, GLUT4 western blot, immunofluorescence co-localization with Rab7/Lamp1 Gene Medium 30316925
2020 IFN-β induces expression of Mir1 microRNA, which reduces TBC1D15 levels, thereby decreasing Rab7 activity and stimulating macroautophagy. This MIR1-TBC1D15-RAB7 pathway is conserved from humans to C. elegans and represents a mechanism by which IFN-β regulates autophagic flux. miRNA overexpression, TBC1D15 knockdown, Rab7 activity measurement, autophagy flux assays, C. elegans genetic validation Autophagy Medium 31958036
2023 A conserved SKY insert (S45, K46, Y47) in FIS1's first TPR repeat is required for proper TBC1D15 recruitment to mitochondria. Deletion of SKY impaired mitochondrial recruitment of both TBC1D15 and DRP1, while the SKY-to-AAA substitution enhanced TBC1D15-driven DRP1 recruitment, indicating intramolecular regulation of FIS1 activity governs TBC1D15 and DRP1 docking. Site-directed mutagenesis, co-immunoprecipitation, fluorescence microscopy of YFP-TBC1D15 localization, mitochondrial morphology analysis in HCT116 cells The Journal of biological chemistry Medium 37777154
2024 TBC1D15 stabilizes NOTCH1 by blocking CDK8- and CDK19-mediated phosphorylation of the NOTCH1 PEST phosphodegron, thereby preventing FBW7 E3 ligase recruitment to Thr-2512 of NOTCH1. TBC1D15 interacts with full-length NUMB and NUMB isoform 5 and relocalizes NUMB5 to mitochondria. The NOTCH1-TBC1D15-FIS1 interaction recruits mitochondria to the perinuclear region. Chromatin immunoprecipitation sequencing (ChIP-seq), co-immunoprecipitation, phosphorylation assays, hepatocyte-specific triple knockout mouse model, PDX mouse model Experimental & molecular medicine Medium 38409448
2025 TBC1D15 translocates to mitochondrial membranes in hepatocytes upon alcohol exposure and recruits PLIN5 through its N-terminal 10-180 aa domain. This interaction promotes mitochondria-lipid droplet contacts and facilitates PKA-induced nuclear translocation of PLIN5, upregulating PPARα, PGC1α and CPT1α to enhance fatty acid β-oxidation. Co-immunoprecipitation, domain mapping, immunofluorescence of mitochondria-LD contacts, transmission electron microscopy, PKA inhibitor experiments, hepatocyte-specific TBC1D15 overexpression mouse model Metabolism: clinical and experimental Medium 40334909
2026 TBC1D15 functions as a GAP for Arl4D (an Arf-family GTPase) in addition to Rab7: TBC1D15 interacts with Arl4D through its TBC domain and promotes GTP hydrolysis of Arl4D. TBC1D15 knockdown increases Arl4D activity and decreases Arl4D mitochondrial translocation under serum starvation, establishing TBC1D15 as a regulator of Arl4D-dependent mitochondrial homeostasis. Co-immunoprecipitation, in vitro GAP activity assay, subcellular fractionation/localization by fluorescence microscopy, TBC1D15 knockdown with Arl4D activity readout Journal of cell science Medium 41709823
2024 In vivo knockdown of murine Tbc1d15 activates autophagy, reduces α-synuclein-mediated neurotoxicity, and improves motor performance in a Parkinson's disease mouse model, corroborating that TBC1D15 inhibits autophagic flux through Rab7 regulation and that its reduction is neuroprotective. In vivo Tbc1d15 knockdown (lentiviral/AAV), autophagy flux assays, α-synuclein aggregation quantification, motor performance behavioral assays bioRxivpreprint Low

Source papers

Stage 0 corpus · 27 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Fis1 acts as a mitochondrial recruitment factor for TBC1D15 that is involved in regulation of mitochondrial morphology. Journal of cell science 124 23077178
2020 TBC1D15/RAB7-regulated mitochondria-lysosome interaction confers cardioprotection against acute myocardial infarction-induced cardiac injury. Theranostics 107 33042281
2010 Differential effects of TBC1D15 and mammalian Vps39 on Rab7 activation state, lysosomal morphology, and growth factor dependence. The Journal of biological chemistry 102 20363736
2023 A lysosome membrane regeneration pathway depends on TBC1D15 and autophagic lysosomal reformation proteins. Nature cell biology 70 37024685
2019 Annexin A6 modulates TBC1D15/Rab7/StARD3 axis to control endosomal cholesterol export in NPC1 cells. Cellular and molecular life sciences : CMLS 60 31664461
2022 TBC1D15-Drp1 interaction-mediated mitochondrial homeostasis confers cardioprotection against myocardial ischemia/reperfusion injury. Metabolism: clinical and experimental 57 35680100
2017 Stimulator of IFN genes-mediated DNA-sensing pathway is suppressed by NLRP3 agonists and regulated by mitofusin 1 and TBC1D15, mitochondrial dynamics mediators. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 25 28729291
2013 The TBC1D15 oncoprotein controls stem cell self-renewal through destabilization of the Numb-p53 complex. PloS one 22 23468968
2023 TBC1D15 deficiency protects against doxorubicin cardiotoxicity via inhibiting DNA-PKcs cytosolic retention and DNA damage. Acta pharmaceutica Sinica. B 18 38045047
2020 IFNB/interferon-β regulates autophagy via a MIR1-TBC1D15-RAB7 pathway. Autophagy 16 31958036
2018 TBC1D15 affects glucose uptake by regulating GLUT4 translocation. Gene 13 30316925
2017 Crystal structure of TBC1D15 GTPase-activating protein (GAP) domain and its activity on Rab GTPases. Protein science : a publication of the Protein Society 12 28168758
2013 Silencing of TBC1D15 promotes RhoA activation and membrane blebbing. Molecular and cellular biochemistry 10 24337944
2025 TBC1D15 protects alcohol-induced liver injury in female mice through PLIN5-mediated mitochondrial and lipid droplet contacting. Metabolism: clinical and experimental 9 40334909
2024 TBC1D15-regulated mitochondria-lysosome membrane contact exerts neuroprotective effects by alleviating mitochondrial calcium overload in seizure. Scientific reports 8 39390030
2024 NOTCH localizes to mitochondria through the TBC1D15-FIS1 interaction and is stabilized via blockade of E3 ligase and CDK8 recruitment to reprogram tumor-initiating cells. Experimental & molecular medicine 7 38409448
2023 A conserved, noncanonical insert in FIS1 mediates TBC1D15 and DRP1 recruitment for mitochondrial fission. The Journal of biological chemistry 7 37777154
2013 Tbc1d15-17 regulates synaptic development at the Drosophila neuromuscular junction. Molecules and cells 7 23812537
2024 The role of TBC1D15 in sepsis-induced acute lung injury: Regulation of mitochondrial homeostasis and mitophagy. International journal of biological macromolecules 6 39740704
2015 A New Member of the TBC1D15 Family from Chiloscyllium plagiosum: Rab GTPase-Activating Protein Based on Rab7 as a Substrate. Marine drugs 6 25984991
2024 Biogenic selenium nanoparticles alleviate intestinal barrier injury in mice through TBC1D15/Fis1/Rab7 pathway. Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie 5 38749178
2023 Upregulation of mitochondrial PGK1 by ROS-TBC1D15 pathway promotes neuronal death after oxygen-glucose deprivation/reoxygenation injury. Brain research 3 38110073
2019 A fragment activity assay reveals the key residues of TBC1D15 GTPase-activating protein (GAP) in Chiloscyllium plagiosum. BMC molecular biology 2 30755162
2026 Case Report: Pediatric AML with TBC1D15::RAB21 fusion and FLT3-ITD/NPM1 co-mutation: diagnostic pitfalls in morphologic mimicry of acute promyelocytic leukemia. Frontiers in oncology 0 41607534
2026 TBC1D15 functions as an Arl4D GAP and promotes the mitochondrial translocation of Arl4D for organelle homeostasis. Journal of cell science 0 41709823
2025 TBC1D15 Expression Indicates the Toxicity of Gold Nanoparticles on Mitochondria in PC-12 Cells. ACS omega 0 40727815
2025 Songorine inhibits mitophagy in chronic heart failure via the TBC1D15/Fis1/Rab7A pathway. British journal of pharmacology 0 41360698

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