Dnm1 is the Saccharomyces cerevisiae dynamin-related GTPase (DRP1 ortholog) that divides mitochondria. A soluble cytosolic pool is recruited to the cytoplasmic face of the mitochondrial outer membrane by the tail-anchored receptor Fis1 and the adaptors Mdv1 and Caf4, at sites often marked by ER tubules. There Dnm1 self-assembles, through its GTPase, middle and GTPase effector (GED) domains, into helical spirals whose diameter matches constricted mitochondria; GTP hydrolysis drives a conformational change that constricts the underlying membrane. Loss of Dnm1 produces net-like, interconnected mitochondria and suppresses fragmentation of fusion-defective fzo1 mutants, showing that Dnm1 fission opposes Fzo1/Mgm1 fusion. Dnm1 also contributes, together with Vps1, to peroxisome division, and to selective autophagy of organelles including nucleophagy, and associates with Num1 cortical anchoring sites that influence mitochondrial inheritance. An early study also reported that dnm1 mutants are slow to deliver internalized pheromone receptor to the vacuole, a post-internalization endocytic defect whose mechanism has not been resolved.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000001 mitochondrion inheritance | IGI PMID:17336903 Yeast mitochondrial division and distribution require the co... | KEEP AS NON CORE | Summary: Mitochondrion inheritance (IGI with NUM1): num1 dnm1 double mutants show defective mitochondrial transmission between mother and bud. Reason: Genetic interaction supports a contribution of Dnm1 (at Num1 cortical anchoring sites) to mitochondrial partitioning, but this is secondary to its core fission function. Supporting Evidence: PMID:17336903 we find that num1 dnm1 double mutants accumulate mitochondria in daughter buds and that mother cells are frequently devoid of all mitochondria PMID:23341591 Although the functional significance of Dnm1 at Num1 clusters is not clear, its dependence on Caf4 suggests that Dnm1 activity at Num1-tethering sites is different from its activity at mitochondrial-division sites. |
| GO:0000266 mitochondrial fission | IBA GO_REF:0000033 | ACCEPT | Summary: Mitochondrial fission. Dnm1 is the dynamin-related GTPase that assembles into helical spirals on the mitochondrial outer membrane and constricts it to divide mitochondria; dnm1 mutants have net-like, fission-defective mitochondria. Reason: Core process, supported by mutant phenotypes (IMP, IGI with FZO1), in vitro assembly/constriction (TAS/IDA), the PANTHER IBA and ARBA. Dnm1 performs the constriction step itself. Supporting Evidence: PMID:10559943 Genetic studies indicate that the activities of the GTPases Dnm1 and Fzo1 are antagonistic: dnm1 mutations block the mitochondrial fission and fragmentation normally observed in the fzo1 mutant strain. PMID:16272155 The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. PMID:21170049 Both dynamin and now Dnm1 have been shown to actively constrict the underlying lipid bilayer upon GTP hydrolysis PMID:16186251 suggest a model in which the Fis1–Mdv1 complex triggers division by promoting the self-assembly of Dnm1 spirals on the mitochondrial outer membrane |
| GO:0000266 mitochondrial fission | IDA PMID:23530241 Interchangeable adaptors regulate mitochondrial dynamin asse... | ACCEPT | Summary: Mitochondrial fission. Dnm1 is the dynamin-related GTPase that assembles into helical spirals on the mitochondrial outer membrane and constricts it to divide mitochondria; dnm1 mutants have net-like, fission-defective mitochondria. Reason: Core process, supported by mutant phenotypes (IMP, IGI with FZO1), in vitro assembly/constriction (TAS/IDA), the PANTHER IBA and ARBA. Dnm1 performs the constriction step itself. Supporting Evidence: PMID:10559943 Genetic studies indicate that the activities of the GTPases Dnm1 and Fzo1 are antagonistic: dnm1 mutations block the mitochondrial fission and fragmentation normally observed in the fzo1 mutant strain. PMID:16272155 The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. PMID:21170049 Both dynamin and now Dnm1 have been shown to actively constrict the underlying lipid bilayer upon GTP hydrolysis PMID:16186251 suggest a model in which the Fis1–Mdv1 complex triggers division by promoting the self-assembly of Dnm1 spirals on the mitochondrial outer membrane |
| GO:0000266 mitochondrial fission | IEA GO_REF:0000117 | ACCEPT | Summary: Mitochondrial fission. Dnm1 is the dynamin-related GTPase that assembles into helical spirals on the mitochondrial outer membrane and constricts it to divide mitochondria; dnm1 mutants have net-like, fission-defective mitochondria. Reason: Core process, supported by mutant phenotypes (IMP, IGI with FZO1), in vitro assembly/constriction (TAS/IDA), the PANTHER IBA and ARBA. Dnm1 performs the constriction step itself. Supporting Evidence: PMID:10559943 Genetic studies indicate that the activities of the GTPases Dnm1 and Fzo1 are antagonistic: dnm1 mutations block the mitochondrial fission and fragmentation normally observed in the fzo1 mutant strain. PMID:16272155 The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. PMID:21170049 Both dynamin and now Dnm1 have been shown to actively constrict the underlying lipid bilayer upon GTP hydrolysis PMID:16186251 suggest a model in which the Fis1–Mdv1 complex triggers division by promoting the self-assembly of Dnm1 spirals on the mitochondrial outer membrane |
| GO:0000266 mitochondrial fission | IGI PMID:10559943 The dynamin-related GTPase Dnm1 regulates mitochondrial fiss... | ACCEPT | Summary: Mitochondrial fission. Dnm1 is the dynamin-related GTPase that assembles into helical spirals on the mitochondrial outer membrane and constricts it to divide mitochondria; dnm1 mutants have net-like, fission-defective mitochondria. Reason: Core process, supported by mutant phenotypes (IMP, IGI with FZO1), in vitro assembly/constriction (TAS/IDA), the PANTHER IBA and ARBA. Dnm1 performs the constriction step itself. Supporting Evidence: PMID:10559943 Genetic studies indicate that the activities of the GTPases Dnm1 and Fzo1 are antagonistic: dnm1 mutations block the mitochondrial fission and fragmentation normally observed in the fzo1 mutant strain. PMID:16272155 The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. PMID:21170049 Both dynamin and now Dnm1 have been shown to actively constrict the underlying lipid bilayer upon GTP hydrolysis PMID:16186251 suggest a model in which the Fis1–Mdv1 complex triggers division by promoting the self-assembly of Dnm1 spirals on the mitochondrial outer membrane |
| GO:0000266 mitochondrial fission | IMP PMID:10559943 The dynamin-related GTPase Dnm1 regulates mitochondrial fiss... | ACCEPT | Summary: Mitochondrial fission. Dnm1 is the dynamin-related GTPase that assembles into helical spirals on the mitochondrial outer membrane and constricts it to divide mitochondria; dnm1 mutants have net-like, fission-defective mitochondria. Reason: Core process, supported by mutant phenotypes (IMP, IGI with FZO1), in vitro assembly/constriction (TAS/IDA), the PANTHER IBA and ARBA. Dnm1 performs the constriction step itself. Supporting Evidence: PMID:10559943 Genetic studies indicate that the activities of the GTPases Dnm1 and Fzo1 are antagonistic: dnm1 mutations block the mitochondrial fission and fragmentation normally observed in the fzo1 mutant strain. PMID:16272155 The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. PMID:21170049 Both dynamin and now Dnm1 have been shown to actively constrict the underlying lipid bilayer upon GTP hydrolysis PMID:16186251 suggest a model in which the Fis1–Mdv1 complex triggers division by promoting the self-assembly of Dnm1 spirals on the mitochondrial outer membrane |
| GO:0000266 mitochondrial fission | TAS PMID:21170049 Conformational changes in Dnm1 support a contractile mechani... | ACCEPT | Summary: Mitochondrial fission. Dnm1 is the dynamin-related GTPase that assembles into helical spirals on the mitochondrial outer membrane and constricts it to divide mitochondria; dnm1 mutants have net-like, fission-defective mitochondria. Reason: Core process, supported by mutant phenotypes (IMP, IGI with FZO1), in vitro assembly/constriction (TAS/IDA), the PANTHER IBA and ARBA. Dnm1 performs the constriction step itself. Supporting Evidence: PMID:10559943 Genetic studies indicate that the activities of the GTPases Dnm1 and Fzo1 are antagonistic: dnm1 mutations block the mitochondrial fission and fragmentation normally observed in the fzo1 mutant strain. PMID:16272155 The dynamin-related GTPase, Dnm1, self-assembles into punctate structures that are targeted to the outer mitochondrial membrane where they mediate mitochondrial division. PMID:21170049 Both dynamin and now Dnm1 have been shown to actively constrict the underlying lipid bilayer upon GTP hydrolysis PMID:16186251 suggest a model in which the Fis1–Mdv1 complex triggers division by promoting the self-assembly of Dnm1 spirals on the mitochondrial outer membrane |
| GO:0000423 mitophagy | IGI PMID:41638207 The mitochondrial intermembrane space nuclease Nuc1 (endonuc... | KEEP AS NON CORE | Summary: Mitophagy (IGI with NUC1). The cached record is abstract-only and does not mention Dnm1; Dnm1-mediated fission is known to facilitate, but not to be strictly required for, mitophagy in yeast. Reason: Plausible secondary role in which Dnm1 divides mitochondria so that fragments can be engulfed; deferred to the curator who read the full text, but non-core. |
| GO:0003924 GTPase activity | IBA GO_REF:0000033 | ACCEPT | Summary: GTPase activity. Recombinant Dnm1 binds and hydrolyses GTP; assembly stimulates hydrolysis, and GTP hydrolysis drives constriction of Dnm1-lipid tubes. Reason: Core molecular function, directly demonstrated (IDA in several papers), consistent with the conserved dynamin-type G domain (IEA, IBA). Supporting Evidence: PMID:11553714 we show that bacterially expressed Dnm1p can bind and hydrolyze GTP in vitro PMID:16186251 Steady-state kinetics of Dnm1 GTPase activity under assembly conditions. PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. |
| GO:0003924 GTPase activity | IDA PMID:11553714 The GTPase effector domain sequence of the Dnm1p GTPase regu... | ACCEPT | Summary: GTPase activity. Recombinant Dnm1 binds and hydrolyses GTP; assembly stimulates hydrolysis, and GTP hydrolysis drives constriction of Dnm1-lipid tubes. Reason: Core molecular function, directly demonstrated (IDA in several papers), consistent with the conserved dynamin-type G domain (IEA, IBA). Supporting Evidence: PMID:11553714 we show that bacterially expressed Dnm1p can bind and hydrolyze GTP in vitro PMID:16186251 Steady-state kinetics of Dnm1 GTPase activity under assembly conditions. PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. |
| GO:0003924 GTPase activity | IDA PMID:16186251 Dnm1 forms spirals that are structurally tailored to fit mit... | ACCEPT | Summary: GTPase activity. Recombinant Dnm1 binds and hydrolyses GTP; assembly stimulates hydrolysis, and GTP hydrolysis drives constriction of Dnm1-lipid tubes. Reason: Core molecular function, directly demonstrated (IDA in several papers), consistent with the conserved dynamin-type G domain (IEA, IBA). Supporting Evidence: PMID:11553714 we show that bacterially expressed Dnm1p can bind and hydrolyze GTP in vitro PMID:16186251 Steady-state kinetics of Dnm1 GTPase activity under assembly conditions. PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. |
| GO:0003924 GTPase activity | IDA PMID:21170049 Conformational changes in Dnm1 support a contractile mechani... | ACCEPT | Summary: GTPase activity. Recombinant Dnm1 binds and hydrolyses GTP; assembly stimulates hydrolysis, and GTP hydrolysis drives constriction of Dnm1-lipid tubes. Reason: Core molecular function, directly demonstrated (IDA in several papers), consistent with the conserved dynamin-type G domain (IEA, IBA). Supporting Evidence: PMID:11553714 we show that bacterially expressed Dnm1p can bind and hydrolyze GTP in vitro PMID:16186251 Steady-state kinetics of Dnm1 GTPase activity under assembly conditions. PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. |
| GO:0003924 GTPase activity | IEA GO_REF:0000120 | ACCEPT | Summary: GTPase activity. Recombinant Dnm1 binds and hydrolyses GTP; assembly stimulates hydrolysis, and GTP hydrolysis drives constriction of Dnm1-lipid tubes. Reason: Core molecular function, directly demonstrated (IDA in several papers), consistent with the conserved dynamin-type G domain (IEA, IBA). Supporting Evidence: PMID:11553714 we show that bacterially expressed Dnm1p can bind and hydrolyze GTP in vitro PMID:16186251 Steady-state kinetics of Dnm1 GTPase activity under assembly conditions. PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. |
| GO:0003924 GTPase activity | IMP PMID:16272155 Mdv1 interacts with assembled dnm1 to promote mitochondrial ... | ACCEPT | Summary: GTPase activity. Recombinant Dnm1 binds and hydrolyses GTP; assembly stimulates hydrolysis, and GTP hydrolysis drives constriction of Dnm1-lipid tubes. Reason: Core molecular function, directly demonstrated (IDA in several papers), consistent with the conserved dynamin-type G domain (IEA, IBA). Supporting Evidence: PMID:11553714 we show that bacterially expressed Dnm1p can bind and hydrolyze GTP in vitro PMID:16186251 Steady-state kinetics of Dnm1 GTPase activity under assembly conditions. PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. |
| GO:0005525 GTP binding | IEA GO_REF:0000002 | ACCEPT | Summary: GTP binding from InterPro dynamin G-domain signatures. Reason: Correct; Dnm1 binds GTP, which is required for its catalytic cycle. Supporting Evidence: PMID:11553714 we show that bacterially expressed Dnm1p can bind and hydrolyze GTP in vitro |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: Cytoplasm. A pool of Dnm1 is soluble in the cytoplasm and is recruited to the outer face of the mitochondrial outer membrane. Reason: Correct; Dnm1 is a peripheral protein on the cytoplasmic side of the outer membrane and also cytosolic. Supporting Evidence: file:yeast/DNM1/DNM1-uniprot.txt Note=Cytoplasm, localizes to the cytoplasmic outer membrane of mitochondria. |
| GO:0005737 cytoplasm | IDA PMID:23530241 Interchangeable adaptors regulate mitochondrial dynamin asse... | ACCEPT | Summary: Cytoplasm. A pool of Dnm1 is soluble in the cytoplasm and is recruited to the outer face of the mitochondrial outer membrane. Reason: Correct; Dnm1 is a peripheral protein on the cytoplasmic side of the outer membrane and also cytosolic. Supporting Evidence: file:yeast/DNM1/DNM1-uniprot.txt Note=Cytoplasm, localizes to the cytoplasmic outer membrane of mitochondria. |
| GO:0005739 mitochondrion | HDA PMID:16823961 Toward the complete yeast mitochondrial proteome: multidimen... | ACCEPT | Summary: Mitochondrion, from proteomics (HDA), GFP localization and immunofluorescence (IDA) and the PANTHER IBA. Reason: Correct though less specific than outer membrane. Supporting Evidence: PMID:11038182 Dnm1p in mdv1 cells is localized to punctate structures on mitochondrial membranes with characteristics similar to Dnm1p-containing structures in wild-type cells file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0005739 mitochondrion | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | ACCEPT | Summary: Mitochondrion, from proteomics (HDA), GFP localization and immunofluorescence (IDA) and the PANTHER IBA. Reason: Correct though less specific than outer membrane. Supporting Evidence: PMID:11038182 Dnm1p in mdv1 cells is localized to punctate structures on mitochondrial membranes with characteristics similar to Dnm1p-containing structures in wild-type cells file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0005739 mitochondrion | IBA GO_REF:0000033 | ACCEPT | Summary: Mitochondrion, from proteomics (HDA), GFP localization and immunofluorescence (IDA) and the PANTHER IBA. Reason: Correct though less specific than outer membrane. Supporting Evidence: PMID:11038182 Dnm1p in mdv1 cells is localized to punctate structures on mitochondrial membranes with characteristics similar to Dnm1p-containing structures in wild-type cells file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0005739 mitochondrion | IDA PMID:10559943 The dynamin-related GTPase Dnm1 regulates mitochondrial fiss... | ACCEPT | Summary: Mitochondrion, from proteomics (HDA), GFP localization and immunofluorescence (IDA) and the PANTHER IBA. Reason: Correct though less specific than outer membrane. Supporting Evidence: PMID:11038182 Dnm1p in mdv1 cells is localized to punctate structures on mitochondrial membranes with characteristics similar to Dnm1p-containing structures in wild-type cells file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0005739 mitochondrion | IDA PMID:23530241 Interchangeable adaptors regulate mitochondrial dynamin asse... | ACCEPT | Summary: Mitochondrion, from proteomics (HDA), GFP localization and immunofluorescence (IDA) and the PANTHER IBA. Reason: Correct though less specific than outer membrane. Supporting Evidence: PMID:11038182 Dnm1p in mdv1 cells is localized to punctate structures on mitochondrial membranes with characteristics similar to Dnm1p-containing structures in wild-type cells file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0005741 mitochondrial outer membrane | IDA PMID:11038182 Mdv1p is a WD repeat protein that interacts with the dynamin... | ACCEPT | Summary: Mitochondrial outer membrane. Dnm1 assembles in punctate complexes on the cytoplasmic face of the outer membrane at division sites. Reason: Core location of action. Supporting Evidence: PMID:11553714 Dnm1p-containing complexes assemble on the cytoplasmic surface of the outer mitochondrial membrane at sites where mitochondrial tubules divide PMID:11038182 Dnm1p in mdv1 cells is localized to punctate structures on mitochondrial membranes with characteristics similar to Dnm1p-containing structures in wild-type cells file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0005741 mitochondrial outer membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Mitochondrial outer membrane. Dnm1 assembles in punctate complexes on the cytoplasmic face of the outer membrane at division sites. Reason: Core location of action. Supporting Evidence: PMID:11553714 Dnm1p-containing complexes assemble on the cytoplasmic surface of the outer mitochondrial membrane at sites where mitochondrial tubules divide PMID:11038182 Dnm1p in mdv1 cells is localized to punctate structures on mitochondrial membranes with characteristics similar to Dnm1p-containing structures in wild-type cells file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0005777 peroxisome | IBA GO_REF:0000033 | ACCEPT | Summary: Peroxisome. Dnm1-GFP shows dual localization on mitochondria and peroxisomes. Reason: Experimentally supported and consistent with Dnm1 role in peroxisome fission. Supporting Evidence: PMID:16968746 Fluorescence microscopy of cells producing Dnm1-GFP or GFP-Fis1p demonstrated that both proteins had a dual localization on mitochondria and peroxisomes. |
| GO:0005777 peroxisome | IDA PMID:16968746 Dynamin-related proteins Vps1p and Dnm1p control peroxisome ... | ACCEPT | Summary: Peroxisome. Dnm1-GFP shows dual localization on mitochondria and peroxisomes. Reason: Experimentally supported and consistent with Dnm1 role in peroxisome fission. Supporting Evidence: PMID:16968746 Fluorescence microscopy of cells producing Dnm1-GFP or GFP-Fis1p demonstrated that both proteins had a dual localization on mitochondria and peroxisomes. |
| GO:0005777 peroxisome | IEA GO_REF:0000117 | ACCEPT | Summary: Peroxisome. Dnm1-GFP shows dual localization on mitochondria and peroxisomes. Reason: Experimentally supported and consistent with Dnm1 role in peroxisome fission. Supporting Evidence: PMID:16968746 Fluorescence microscopy of cells producing Dnm1-GFP or GFP-Fis1p demonstrated that both proteins had a dual localization on mitochondria and peroxisomes. |
| GO:0005829 cytosol | IDA PMID:16272155 Mdv1 interacts with assembled dnm1 to promote mitochondrial ... | ACCEPT | Summary: Cytosol. A soluble Dnm1 pool exists in the cytosol prior to recruitment by Fis1/Mdv1/Caf4. Reason: Correct; cytosol-to-membrane recruitment is central to Dnm1 regulation. Supporting Evidence: file:yeast/DNM1/DNM1-uniprot.txt Note=Cytoplasm, localizes to the cytoplasmic outer membrane of mitochondria. |
| GO:0005829 cytosol | IEA GO_REF:0000117 | ACCEPT | Summary: Cytosol. A soluble Dnm1 pool exists in the cytosol prior to recruitment by Fis1/Mdv1/Caf4. Reason: Correct; cytosol-to-membrane recruitment is central to Dnm1 regulation. Supporting Evidence: file:yeast/DNM1/DNM1-uniprot.txt Note=Cytoplasm, localizes to the cytoplasmic outer membrane of mitochondria. |
| GO:0005874 microtubule | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Microtubule (IBA from a dynamin-superfamily node). Reason: Microtubule association was originally described for classical dynamin; there is no evidence that yeast Dnm1 acts on or with microtubules, and Dnm1 lacks the PH and proline-rich domains of classical dynamin. The UniProt phrase "microtubule-associated force-producing protein" is legacy family boilerplate. Over-propagation from distant family members. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE GRANULARITY MISMATCH Sources checked: PANTHER:PTN000170013 SUPPORTS SOURCE BUT NOT TARGET Dynamin-superfamily node seeded by classical dynamin/plant DRP microtubule data; the Drp1/Dnm1 mitochondrial-fission subclade has no microtubule evidence. Supporting Evidence: PMID:16186251 suggest a model in which the Fis1–Mdv1 complex triggers division by promoting the self-assembly of Dnm1 spirals on the mitochondrial outer membrane |
| GO:0007005 mitochondrion organization | IMP PMID:9786946 The dynamin-related GTPase, Dnm1p, controls mitochondrial mo... | MODIFY | Summary: Mitochondrion organization (IMP): dnm1 null cells have collapsed, elongated mitochondrial networks. Reason: Correct but generic; the underlying defect is loss of mitochondrial fission. Proposed replacements: mitochondrial fission Supporting Evidence: PMID:9786946 At later time points, mitochondrial morphology collapses further in these cells to produce the elongated mitochondrial structures characteristic of dnm1 null cells PMID:10559943 Genetic studies indicate that the activities of the GTPases Dnm1 and Fzo1 are antagonistic: dnm1 mutations block the mitochondrial fission and fragmentation normally observed in the fzo1 mutant strain. |
| GO:0007031 peroxisome organization | IGI PMID:16968746 Dynamin-related proteins Vps1p and Dnm1p control peroxisome ... | MODIFY | Summary: Peroxisome organization (IMP, IGI with VPS1): deletion of DNM1 reduces peroxisome number in oleate-grown cells, synergistically with vps1. Reason: The phenotype reflects a role in peroxisome division; peroxisome fission is the more specific term. Proposed replacements: peroxisome fission Supporting Evidence: PMID:16968746 Here we show that deletion of DNM1 also results in reduction of peroxisome numbers. PMID:18445678 Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. |
| GO:0007031 peroxisome organization | IMP PMID:16968746 Dynamin-related proteins Vps1p and Dnm1p control peroxisome ... | MODIFY | Summary: Peroxisome organization (IMP, IGI with VPS1): deletion of DNM1 reduces peroxisome number in oleate-grown cells, synergistically with vps1. Reason: The phenotype reflects a role in peroxisome division; peroxisome fission is the more specific term. Proposed replacements: peroxisome fission Supporting Evidence: PMID:16968746 Here we show that deletion of DNM1 also results in reduction of peroxisome numbers. PMID:18445678 Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. |
| GO:0008017 microtubule binding | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: Microtubule binding (IBA from a dynamin-superfamily node with a Drosophila shibire donor). Reason: No evidence that Dnm1 or other Drp1-subfamily members bind microtubules; the activity is a property attributed to classical dynamins and does not reflect Dnm1 function on mitochondrial membranes. Propagation Review Root cause: PROPAGATION BAD Failure modes: FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN000170013 SUPPORTS SOURCE BUT NOT TARGET Node seeded by Drosophila shibire (classical dynamin); microtubule binding is not supported for the Drp1/Dnm1 subclade. |
| GO:0015886 heme transport | IMP PMID:32265272 Mitochondrial-nuclear heme trafficking in budding yeast is r... | MARK AS OVER ANNOTATED | Summary: Heme transport (IMP): dnm1 deletion increases mitochondrial-to-nuclear heme trafficking. Reason: The paper itself describes Dnm1 as an indirect modulator acting through fission/ERMES; Dnm1 does not transport heme. Indirect phenotype. Supporting Evidence: PMID:32265272 In addition, we identified GTPases that directly (Gem1) and indirectly (Dnm1 and Mgm1) regulate ERMES as being modulators of nuclear heme transport. |
| GO:0016020 membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Membrane (IBA). Reason: Correct but uninformative; mitochondrial outer membrane captures the location. Supporting Evidence: file:yeast/DNM1/DNM1-uniprot.txt SUBCELLULAR LOCATION: Mitochondrion outer membrane |
| GO:0016050 vesicle organization | IDA PMID:21170049 Conformational changes in Dnm1 support a contractile mechani... | MODIFY | Summary: Vesicle organization (IDA) from cryo-EM of Dnm1 assembling on and constricting liposome-derived lipid tubes. Reason: Dnm1 tubulates and constricts liposomes in vitro, which is a membrane remodeling activity rather than organization of cellular vesicles; membrane bending better describes the observation. Proposed replacements: membrane bending Supporting Evidence: PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. |
| GO:0016236 macroautophagy | IMP PMID:19793921 A genomic screen for yeast mutants defective in selective mi... | MARK AS OVER ANNOTATED | Summary: Macroautophagy (IMP) from a genome-wide mitophagy screen (abstract only cached). Reason: Dnm1 is not a general macroautophagy factor; its contribution is to selective degradation of organelles (mitophagy, pexophagy, nucleophagy) by dividing them. The general term over-states the role. |
| GO:0016559 peroxisome fission | IBA GO_REF:0000033 | ACCEPT | Summary: Peroxisome fission: Dnm1 with Fis1, Mdv1 and Caf4 divides peroxisomes (redundantly with Vps1). Reason: Supported genetically and by the PANTHER IBA and ARBA. Supporting Evidence: PMID:18445678 Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. PMID:16968746 Here we show that deletion of DNM1 also results in reduction of peroxisome numbers. |
| GO:0016559 peroxisome fission | IEA GO_REF:0000117 | ACCEPT | Summary: Peroxisome fission: Dnm1 with Fis1, Mdv1 and Caf4 divides peroxisomes (redundantly with Vps1). Reason: Supported genetically and by the PANTHER IBA and ARBA. Supporting Evidence: PMID:18445678 Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. PMID:16968746 Here we show that deletion of DNM1 also results in reduction of peroxisome numbers. |
| GO:0016559 peroxisome fission | IGI PMID:18445678 Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and... | ACCEPT | Summary: Peroxisome fission: Dnm1 with Fis1, Mdv1 and Caf4 divides peroxisomes (redundantly with Vps1). Reason: Supported genetically and by the PANTHER IBA and ARBA. Supporting Evidence: PMID:18445678 Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p. PMID:16968746 Here we show that deletion of DNM1 also results in reduction of peroxisome numbers. |
| GO:0030001 metal ion transport | IEA GO_REF:0000117 | REMOVE | Summary: Metal ion transport (ARBA). Reason: No evidence that Dnm1 transports metal ions; an ARBA rule artefact with no biological basis for this GTPase. |
| GO:0042802 identical protein binding | IDA PMID:16186251 Dnm1 forms spirals that are structurally tailored to fit mit... | KEEP AS NON CORE | Summary: Identical protein binding: Dnm1 self-interacts (two-hybrid, co-IP, large-scale interactome screens) and self-assembles into spirals. Reason: Correct; self-assembly underlies its mechanism but the more informative description is oligomerization coupled to GTPase activity. Supporting Evidence: PMID:11553714 Coimmunoprecipitation studies and yeast two-hybrid analysis suggest that Dnm1p oligomerizes in vivo. PMID:16186251 Dnm1 self-assembles into large spirals in the presence of GMP-PCP. |
| GO:0042802 identical protein binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Identical protein binding: Dnm1 self-interacts (two-hybrid, co-IP, large-scale interactome screens) and self-assembles into spirals. Reason: Correct; self-assembly underlies its mechanism but the more informative description is oligomerization coupled to GTPase activity. Supporting Evidence: PMID:11553714 Coimmunoprecipitation studies and yeast two-hybrid analysis suggest that Dnm1p oligomerizes in vivo. PMID:16186251 Dnm1 self-assembles into large spirals in the presence of GMP-PCP. |
| GO:0042802 identical protein binding | IPI PMID:18467557 An in vivo map of the yeast protein interactome. | KEEP AS NON CORE | Summary: Identical protein binding: Dnm1 self-interacts (two-hybrid, co-IP, large-scale interactome screens) and self-assembles into spirals. Reason: Correct; self-assembly underlies its mechanism but the more informative description is oligomerization coupled to GTPase activity. Supporting Evidence: PMID:11553714 Coimmunoprecipitation studies and yeast two-hybrid analysis suggest that Dnm1p oligomerizes in vivo. PMID:16186251 Dnm1 self-assembles into large spirals in the presence of GMP-PCP. |
| GO:0042802 identical protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | KEEP AS NON CORE | Summary: Identical protein binding: Dnm1 self-interacts (two-hybrid, co-IP, large-scale interactome screens) and self-assembles into spirals. Reason: Correct; self-assembly underlies its mechanism but the more informative description is oligomerization coupled to GTPase activity. Supporting Evidence: PMID:11553714 Coimmunoprecipitation studies and yeast two-hybrid analysis suggest that Dnm1p oligomerizes in vivo. PMID:16186251 Dnm1 self-assembles into large spirals in the presence of GMP-PCP. |
| GO:0042802 identical protein binding | IPI PMID:21170049 Conformational changes in Dnm1 support a contractile mechani... | KEEP AS NON CORE | Summary: Identical protein binding: Dnm1 self-interacts (two-hybrid, co-IP, large-scale interactome screens) and self-assembles into spirals. Reason: Correct; self-assembly underlies its mechanism but the more informative description is oligomerization coupled to GTPase activity. Supporting Evidence: PMID:11553714 Coimmunoprecipitation studies and yeast two-hybrid analysis suggest that Dnm1p oligomerizes in vivo. PMID:16186251 Dnm1 self-assembles into large spirals in the presence of GMP-PCP. |
| GO:0048311 mitochondrion distribution | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Mitochondrion distribution (ARBA). Reason: Consistent with Dnm1 effects on mitochondrial distribution via fission and Num1; secondary. Supporting Evidence: PMID:17336903 we find that num1 dnm1 double mutants accumulate mitochondria in daughter buds and that mother cells are frequently devoid of all mitochondria |
| GO:0048312 intracellular distribution of mitochondria | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Intracellular distribution of mitochondria (IBA; IGI with NUM1 and FZO1). Reason: Dnm1 at Num1 cortical tethering sites contributes to mitochondrial distribution, but this is secondary to fission. Supporting Evidence: PMID:23341591 Although the functional significance of Dnm1 at Num1 clusters is not clear, its dependence on Caf4 suggests that Dnm1 activity at Num1-tethering sites is different from its activity at mitochondrial-division sites. |
| GO:0048312 intracellular distribution of mitochondria | IGI PMID:23341591 Endoplasmic reticulum-associated mitochondria-cortex tether ... | KEEP AS NON CORE | Summary: Intracellular distribution of mitochondria (IBA; IGI with NUM1 and FZO1). Reason: Dnm1 at Num1 cortical tethering sites contributes to mitochondrial distribution, but this is secondary to fission. Supporting Evidence: PMID:23341591 Although the functional significance of Dnm1 at Num1 clusters is not clear, its dependence on Caf4 suggests that Dnm1 activity at Num1-tethering sites is different from its activity at mitochondrial-division sites. |
| GO:0051260 protein homooligomerization | IDA PMID:21170049 Conformational changes in Dnm1 support a contractile mechani... | KEEP AS NON CORE | Summary: Protein homooligomerization (IDA): Dnm1 assembles into helical filaments on lipid tubes. Reason: Directly shown; self-assembly is part of the fission mechanism but not a separate biological role. Supporting Evidence: PMID:21170049 Additionally, we show that Dnm1-lipid tubes constrict by ~50 nm upon addition of GTP. PMID:16186251 Dnm1 self-assembles into large spirals in the presence of GMP-PCP. |
| GO:0061024 membrane organization | IDA PMID:21170049 Conformational changes in Dnm1 support a contractile mechani... | KEEP AS NON CORE | Summary: Membrane organization (IDA) from Dnm1-driven constriction of lipid tubes. Reason: Correct but generic. Supporting Evidence: PMID:21170049 Both dynamin and now Dnm1 have been shown to actively constrict the underlying lipid bilayer upon GTP hydrolysis |
| GO:0090148 membrane fission | IMP PMID:39920277 A quantitative ultrastructural timeline of nuclear autophagy... | KEEP AS NON CORE | Summary: Membrane fission (IMP) in nucleophagy: Dnm1 is proposed to execute outer nuclear membrane fission releasing nucleus-derived vesicles. Reason: Supported by the cited study, which also shows dnm1 deletion stalls only a fraction of nucleophagy events; an extension of the same membrane-scission activity to a non-mitochondrial membrane. Supporting Evidence: PMID:39920277 the Dnm1-dependent nucleophagy pathway requires a second membrane fission reaction executed at the ONM |
| GO:0097753 membrane bending | IDA PMID:29202017 Molecular Motor Dnm1 Synergistically Induces Membrane Curvat... | KEEP AS NON CORE | Summary: Membrane bending (IDA): Dnm1 induces negative Gaussian curvature in membranes. Reason: Directly shown in vitro; a mechanistic step of fission. Supporting Evidence: PMID:29202017 Molecular Motor Dnm1 Synergistically Induces Membrane Curvature To Facilitate Mitochondrial Fission. |
| GO:1901858 regulation of mitochondrial DNA metabolic process | IGI PMID:41638207 The mitochondrial intermembrane space nuclease Nuc1 (endonuc... | UNDECIDED | Summary: Regulation of mitochondrial DNA metabolic process (IGI with NUC1). Reason: The cached record is abstract-only and does not mention Dnm1; the full text (not retrievable from PMC) presumably tests dnm1 in the nuc1 mtDNA escape assay. Any effect would be indirect via mitophagy, but this cannot be assessed here. |
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Download this section (compressed HTML)Q: Is Dnm1 constriction sufficient for complete scission of both mitochondrial membranes in vivo, or are additional factors (e.g. Vps1/dynamin-2 equivalents, inner-membrane constriction) required?
Q: What distinguishes Dnm1 activity at Num1 cortical anchors from its activity at division sites?
Experiment: Time-resolved cryo-ET of Dnm1 spirals on mitochondria in Fis1/Mdv1/Caf4 mutants to determine which adaptor controls spiral nucleation versus constriction.
Dynamin-related GTPase involved in mitochondrial organization; required for mitochondrial fission and inheritance; self assembles on mitochondrial tubules at incipient division sites; involved in endocytosis; regulates peroxisome fission with Vps1p; role in nuclear envelope remodeling during nucleophagy; mutants in human ortholog DNM1L, which mediates mitochondrial fission, peroxisomal division, autophagy, and mitophagy, are associated with slowly progressive infantile encephalopathy
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