id: Q8WQC9
gene_symbol: drp-1
aliases:
- T12E12.4
- Dynamin-related protein 1
product_type: PROTEIN
status: DRAFT
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
description: DRP-1 is a dynamin-related GTPase that mediates mitochondrial outer membrane
  fission in C. elegans. It is recruited from the cytosol to the mitochondrial outer
  membrane at sites of constriction, where it oligomerizes and uses GTP hydrolysis
  to drive membrane scission. DRP-1 is essential for normal mitochondrial division
  and morphology; loss of function causes enlarged, interconnected mitochondria with
  matrix retracted into blebs connected by outer membrane tubules (PMID:10619028).
  DRP-1 also plays roles in apoptosis downstream of caspase CED-3, where it promotes
  mitochondrial fragmentation and elimination in dying cells (PMID:18722182, PMID:15716954).
  DRP-1 is cleaved by CED-3, and this cleavage is required for its pro-apoptotic but
  not its fission function (PMID:18722182). The protein coordinates with autophagy/mitophagy
  during stress responses and influences lifespan in the context of insulin/IGF-1
  signaling. By similarity to mammalian DRP1, it likely also mediates peroxisome fission.
existing_annotations:
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: DRP-1 is a dynamin-related GTPase with conserved GTPase domains. The
      protein contains a Dynamin-type G domain (aa 24-304) with G1-G5 motifs characteristic
      of GTPases. Mutations in conserved GTPase domain residues (K40A, V43F, T61A)
      cause disrupted mitochondrial morphology (PMID:10619028), indicating GTPase
      activity is essential for function. Cross-species biochemical studies confirm
      Drp1 GTPase activity is assembly-stimulated and required for membrane scission.
    action: ACCEPT
    reason: Core molecular function supported by domain architecture and mutational
      analysis. The K40A mutation in the GTPase domain causes 80% of cells to have
      irregular mitochondria (PMID:10619028). IBA annotation is appropriate given
      strong phylogenetic conservation of this function in the dynamin superfamily.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: Mutant DRP-1 causes the mitochondrial matrix to retract into
        large blebs that are both surrounded and connected by tubules of outer membrane.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: DRP-1 localizes to the cytosol and is recruited to mitochondria at fission
      sites. UniProt annotation confirms cytosol localization with experimental evidence
      (PMID:21949250).
    action: ACCEPT
    reason: Consistent with cytosolic localization before recruitment to mitochondrial
      membrane. DRP-1 exists in cytosolic pools and is recruited to mitochondria upon
      fission signals, which is a general feature of dynamin-related proteins.
    supported_by:
    - reference_id: PMID:21949250
      supporting_text: the EGL-1-CED-9 complex promotes mitochondrial fission by recruiting
        DRP-1 to mitochondria
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: DRP-1 associates with membranes, specifically the mitochondrial outer
      membrane where it mediates fission. The term 'membrane' is very general.
    action: ACCEPT
    reason: DRP-1 does associate with membranes (mitochondrial outer membrane specifically).
      While more specific terms exist, this IBA annotation captures a broad but accurate
      property of the protein. The more specific annotation to mitochondrial outer
      membrane is also present.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: DRP-1 fused to GFP is observed in spots on mitochondria where
        scission eventually occurs.
- term:
    id: GO:0000266
    label: mitochondrial fission
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Mitochondrial fission is the core biological process function of DRP-1.
      Multiple experimental studies demonstrate DRP-1 is required for mitochondrial
      outer membrane scission (PMID:10619028, PMID:19327994, PMID:18827010).
    action: ACCEPT
    reason: This is the primary, defining function of DRP-1. Loss of DRP-1 function
      causes inhibition of mitochondrial outer membrane scission, while overexpression
      causes excessive fragmentation (PMID:10619028). This function is well-conserved
      across eukaryotes in the dynamin-related protein family.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: wild-type DRP-1 contributes to the final stages of mitochondrial
        division by controlling scission of the mitochondrial outer membrane.
- term:
    id: GO:0048312
    label: intracellular distribution of mitochondria
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: DRP-1 mutants show abnormal mitochondrial distribution. The fission function
      of DRP-1 contributes to proper mitochondrial inheritance and distribution. UniProt
      notes disruption phenotype includes disorganized gonads with abnormal mitochondrial
      distribution (PMID:10619028).
    action: ACCEPT
    reason: The annotation is appropriate as mitochondrial fission is necessary for
      proper distribution of mitochondria during cell division and within cells. Loss
      of drp-1 causes disorganized gonads with abnormal mitochondrial distribution.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: mitochondria are disrupted by mutations in a C. elegans dynamin-related
        protein (DRP-1).
- term:
    id: GO:0016559
    label: peroxisome fission
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Peroxisome fission function is inferred by similarity to mammalian DRP1/DNM1L
      which is well-documented to mediate peroxisome fission. UniProt annotates this
      function with ISS evidence (ECO:0000250|UniProtKB:O00429).
    action: ACCEPT
    reason: Mammalian DRP1 is established to mediate both mitochondrial and peroxisomal
      fission using the same membrane scission mechanism. The IBA annotation is phylogenetically
      sound given the conservation of this dual function in the Drp1 family. No direct
      experimental evidence in C. elegans, but strong inference from ortholog function.
    supported_by:
    - reference_id: file:worm/drp-1/drp-1-deep-research-falcon.md
      supporting_text: DRP-1 catalyzes mitochondrial (and peroxisomal, by inference)
        fission by binding the outer mitochondrial membrane (OMM), oligomerizing,
        and coupling GTP hydrolysis to membrane constriction and scission
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: DRP-1 localizes to mitochondria at fission sites. DRP-1::GFP is observed
      in spots on mitochondria where scission occurs (PMID:10619028).
    action: ACCEPT
    reason: Well-supported by experimental evidence. DRP-1 is recruited to mitochondria
      to execute its fission function.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: DRP-1 fused to GFP is observed in spots on mitochondria where
        scission eventually occurs.
- term:
    id: GO:0005874
    label: microtubule
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: This annotation appears to be inherited from classical dynamin family
      members that associate with microtubules for endocytic vesicle transport. While
      dynamin superfamily members can associate with microtubules, there is no direct
      evidence for DRP-1 microtubule localization in C. elegans.
    action: MARK_AS_OVER_ANNOTATED
    reason: This annotation likely derives from phylogenetic inference across the
      broader dynamin family, but DRP-1/Drp1 subfamily proteins function at mitochondria
      and peroxisomes, not at the plasma membrane or in endocytic trafficking where
      microtubule association is relevant. No C. elegans-specific evidence supports
      this localization for drp-1.
- term:
    id: GO:0008017
    label: microtubule binding
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  review:
    summary: Similar to the microtubule localization annotation, this molecular function
      annotation appears to derive from classical dynamins rather than the DRP1 subfamily.
      There is no evidence that DRP-1 binds microtubules in C. elegans.
    action: MARK_AS_OVER_ANNOTATED
    reason: The DRP-1/Drp1 subfamily is functionally distinct from classical dynamins
      that operate in endocytosis and require microtubule binding. DRP-1's function
      at mitochondria and peroxisomes does not require microtubule binding. This annotation
      represents over-inference from the broader dynamin family.
- term:
    id: GO:0000166
    label: nucleotide binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: DRP-1 binds GTP as part of its GTPase activity. The protein has conserved
      G1-G5 motifs for nucleotide binding in its dynamin-type G domain.
    action: ACCEPT
    reason: This is a parent term of the more specific GTP binding annotation. While
      somewhat redundant given the GTP binding annotation, it is not incorrect. The
      IEA annotation from UniProt keyword mapping is appropriate.
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  review:
    summary: GTPase activity is the core catalytic function. This IEA annotation from
      InterPro domain mapping is consistent with the IBA annotation.
    action: ACCEPT
    reason: Duplicates the IBA annotation but via a different evidence pathway (InterPro
      domain mapping). Both are valid and consistent.
- term:
    id: GO:0005525
    label: GTP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  review:
    summary: GTP binding is required for DRP-1 GTPase activity and membrane fission
      function. The G1-G5 motifs in the dynamin-type G domain mediate GTP binding.
    action: ACCEPT
    reason: Well-supported by domain architecture. GTP binding is an intrinsic property
      of the conserved dynamin GTPase domain.
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000117
  review:
    summary: Cytoplasmic localization is consistent with experimental evidence showing
      DRP-1 in cytosol before recruitment to mitochondria.
    action: ACCEPT
    reason: Consistent with experimental observations. DRP-1 exists in cytosolic pools.
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: Mitochondrial localization is well-supported by experimental evidence
      showing DRP-1::GFP at mitochondrial fission sites (PMID:10619028).
    action: ACCEPT
    reason: Consistent with experimental evidence for DRP-1 localization to mitochondria.
- term:
    id: GO:0005741
    label: mitochondrial outer membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: DRP-1 functions at the mitochondrial outer membrane where it mediates
      membrane scission. The protein is recruited to the OMM at constriction sites.
    action: ACCEPT
    reason: Well-supported by experimental evidence. DRP-1 controls scission of the
      mitochondrial outer membrane specifically (PMID:10619028).
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: wild-type DRP-1 contributes to the final stages of mitochondrial
        division by controlling scission of the mitochondrial outer membrane.
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  review:
    summary: DRP-1 resides in the cytosol and is recruited to mitochondria upon fission
      signals. UniProt subcellular location annotation supports cytosol localization.
    action: ACCEPT
    reason: Consistent with experimental evidence that DRP-1 exists in cytosolic pools
      before recruitment to mitochondria (PMID:21949250).
- term:
    id: GO:0006915
    label: apoptotic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: DRP-1 has a role in apoptosis, promoting mitochondrial fragmentation
      and elimination during cell death. However, drp-1 is not required for apoptosis
      activation but acts downstream of caspase CED-3 in cell death execution (PMID:18722182).
    action: KEEP_AS_NON_CORE
    reason: The apoptotic role is real but secondary to the core mitochondrial fission
      function. DRP-1 acts downstream of CED-3 to promote mitochondrial elimination
      in dying cells, but is not essential for apoptosis activation. The annotation
      is appropriate but represents a context-dependent function rather than core
      function.
    supported_by:
    - reference_id: PMID:18722182
      supporting_text: drp-1 and fis-2 function independent of one another and the
        Bcl-2 homolog CED-9 and downstream of the CED-3 caspase to promote elimination
        of mitochondria in dying cells
- term:
    id: GO:0008289
    label: lipid binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: Dynamin-related proteins bind membrane lipids as part of their membrane
      remodeling function. The annotation is based on UniProt lipid-binding keyword.
    action: ACCEPT
    reason: Membrane binding is required for DRP-1 function. GTPase activity is increased
      by binding to phospholipid membranes (UniProt activity regulation note). Cross-species
      studies show Drp1 binds membranes via adaptors and lipid interactions.
- term:
    id: GO:0016787
    label: hydrolase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000043
  review:
    summary: DRP-1 is a GTPase that hydrolyzes GTP to GDP + Pi. Hydrolase activity
      is a parent term of GTPase activity.
    action: ACCEPT
    reason: True but very general. GTPase activity is a more informative child term
      that is also annotated. This parent term is not wrong.
- term:
    id: GO:0000266
    label: mitochondrial fission
  evidence_type: IMP
  original_reference_id: PMID:19327994
  review:
    summary: This study examined drp-1 mutants and found mitochondrial fission is
      defective. The study specifically looked at mitochondrial morphology in drp-1
      mutants in the context of analyzing Bcl-2 protein function.
    action: ACCEPT
    reason: Direct experimental evidence. The study confirms drp-1 mutants have defective
      mitochondrial fission while fusion still occurs, resulting in abnormal mitochondrial
      connectivity.
    supported_by:
    - reference_id: PMID:19327994
      supporting_text: in a drp-1 mutant, in which mitochondrial fusion occurs but
        mitochondrial fission is defective
- term:
    id: GO:0000266
    label: mitochondrial fission
  evidence_type: IGI
  original_reference_id: PMID:18827010
  review:
    summary: This study showed genetic interaction between drp-1 and ced-9 in regulating
      mitochondrial morphology. Increased DRP-1 expression suppresses the interconnected
      mitochondria phenotype caused by CED-9 overexpression.
    action: ACCEPT
    reason: Valid genetic interaction evidence. The study demonstrates DRP-1 functions
      in opposition to CED-9 in controlling mitochondrial morphology, with DRP-1 promoting
      fission.
    supported_by:
    - reference_id: PMID:18827010
      supporting_text: This mitochondrial phenotype is partially suppressed by increased
        expression of the dynamin-related GTPase DRP-1
- term:
    id: GO:0000266
    label: mitochondrial fission
  evidence_type: IMP
  original_reference_id: PMID:18827010
  review:
    summary: The study examines drp-1 function in mitochondrial dynamics and shows
      it promotes fission. DRP-1 overexpression causes fragmented mitochondria.
    action: ACCEPT
    reason: Direct mutant phenotype evidence supporting DRP-1 role in mitochondrial
      fission.
    supported_by:
    - reference_id: PMID:18827010
      supporting_text: This mitochondrial phenotype is partially suppressed by increased
        expression of the dynamin-related GTPase DRP-1
- term:
    id: GO:0009792
    label: embryo development ending in birth or egg hatching
  evidence_type: IMP
  original_reference_id: PMID:10619028
  review:
    summary: RNAi knockdown of drp-1 causes embryonic lethality. This represents a
      broad developmental phenotype resulting from the essential mitochondrial fission
      function.
    action: KEEP_AS_NON_CORE
    reason: The embryonic lethality phenotype is real but represents a pleiotropic
      consequence of disrupted mitochondrial dynamics rather than a specific developmental
      function. DRP-1's role is in mitochondrial fission; the developmental phenotype
      is downstream of this core function.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: mitochondria are disrupted by mutations in a C. elegans dynamin-related
        protein (DRP-1).
- term:
    id: GO:0006915
    label: apoptotic process
  evidence_type: IGI
  original_reference_id: PMID:18722182
  review:
    summary: This study demonstrated genetic interaction between drp-1 and ced-3 (caspase)
      in apoptosis. DRP-1 functions downstream of CED-3 to promote cell death execution
      through mitochondrial elimination.
    action: KEEP_AS_NON_CORE
    reason: The apoptotic role is real but represents a secondary function. DRP-1
      is not required for apoptosis activation but acts downstream of caspase to facilitate
      mitochondrial elimination in dying cells. The annotation is correct but this
      is not the core function.
    supported_by:
    - reference_id: PMID:18722182
      supporting_text: drp-1 and fis-2 function independent of one another and the
        Bcl-2 homolog CED-9 and downstream of the CED-3 caspase to promote elimination
        of mitochondria in dying cells
- term:
    id: GO:0000266
    label: mitochondrial fission
  evidence_type: IMP
  original_reference_id: PMID:10619028
  review:
    summary: This is the foundational paper establishing DRP-1 function in mitochondrial
      fission. Mutant DRP-1 causes mitochondrial matrix to retract into blebs connected
      by outer membrane tubules, indicating outer membrane scission is inhibited.
      Overexpression causes excessive fragmentation.
    action: ACCEPT
    reason: Primary experimental evidence establishing DRP-1 as a mitochondrial fission
      factor. This is the core function of the protein.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: Mutant DRP-1 causes the mitochondrial matrix to retract into
        large blebs that are both surrounded and connected by tubules of outer membrane.
        This indicates that scission of the mitochondrial outer membrane is inhibited
- term:
    id: GO:0005525
    label: GTP binding
  evidence_type: ISS
  original_reference_id: PMID:10619028
  review:
    summary: GTP binding is inferred by sequence similarity to mammalian DRP1 (UniProtKB:O00429).
      The conserved dynamin-type G domain with G1-G5 motifs supports this function.
    action: ACCEPT
    reason: Valid sequence similarity-based inference. The conserved domain architecture
      strongly supports GTP binding function.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: C. elegans dynamin-related protein (DRP-1)
- term:
    id: GO:0005739
    label: mitochondrion
  evidence_type: IDA
  original_reference_id: PMID:10619028
  review:
    summary: Direct experimental evidence showing DRP-1::GFP localization to mitochondria
      at fission sites.
    action: ACCEPT
    reason: Strong experimental evidence. GFP-tagged DRP-1 was observed at sites of
      mitochondrial scission.
    supported_by:
    - reference_id: PMID:10619028
      supporting_text: DRP-1 fused to GFP is observed in spots on mitochondria where
        scission eventually occurs.
- term:
    id: GO:0008637
    label: apoptotic mitochondrial changes
  evidence_type: IMP
  original_reference_id: PMID:15716954
  review:
    summary: This study showed DRP-1 is required for mitochondrial fragmentation during
      EGL-1-induced cell death. DRP-1 overexpression is sufficient to induce mitochondrial
      fragmentation and cell death.
    action: ACCEPT
    reason: Well-supported by experimental evidence. DRP-1 mediates mitochondrial
      fragmentation during apoptosis, which represents apoptotic mitochondrial changes.
    supported_by:
    - reference_id: PMID:15716954
      supporting_text: DRP-1/dynamin-related protein, a key component of the mitochondrial
        fission machinery, is required and sufficient to induce mitochondrial fragmentation
        and programmed cell death during C. elegans development.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings:
  - statement: IBA annotations based on PANTHER phylogenetic trees with characterized
      orthologs
- id: GO_REF:0000043
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping
  findings: []
- id: GO_REF:0000117
  title: Electronic Gene Ontology annotations created by ARBA machine learning models
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:10619028
  title: C. elegans dynamin-related protein DRP-1 controls severing of the mitochondrial
    outer membrane.
  findings:
  - statement: Established DRP-1 as the mitochondrial fission factor in C. elegans
    supporting_text: wild-type DRP-1 contributes to the final stages of mitochondrial
      division by controlling scission of the mitochondrial outer membrane.
  - statement: Mutant DRP-1 inhibits outer membrane scission while inner membrane
      scission still occurs
    supporting_text: Mutant DRP-1 causes the mitochondrial matrix to retract into
      large blebs that are both surrounded and connected by tubules of outer membrane.
  - statement: DRP-1::GFP localizes to sites of mitochondrial scission
    supporting_text: DRP-1 fused to GFP is observed in spots on mitochondria where
      scission eventually occurs.
  - statement: Overexpression causes excessive mitochondrial fragmentation
    supporting_text: Overexpressed wild-type DRP-1 causes mitochondria to become excessively
      fragmented
- id: PMID:15716954
  title: DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death
    in C. elegans.
  findings:
  - statement: DRP-1 is required and sufficient to induce mitochondrial fragmentation
      during apoptosis
    supporting_text: DRP-1/dynamin-related protein, a key component of the mitochondrial
      fission machinery, is required and sufficient to induce mitochondrial fragmentation
      and programmed cell death during C. elegans development.
  - statement: Mitochondrial fragmentation is induced by EGL-1 and blocked by ced-9
      mutations
    supporting_text: Mitochondrial fragmentation is induced by the BH3-only protein
      EGL-1 and can be blocked by mutations in the bcl-2-like gene ced-9
  - statement: Mitochondrial fragmentation is independent of CED-4 and CED-3
    supporting_text: Mitochondrial fragmentation is independent of CED-4/Apaf-1 and
      CED-3/caspase
- id: PMID:18722182
  title: Caenorhabditis elegans drp-1 and fis-2 regulate distinct cell-death execution
    pathways downstream of ced-3 and independent of ced-9.
  findings:
  - statement: drp-1 is not required for apoptosis activation but acts downstream
      of CED-3
    supporting_text: profusion genes fzo-1 and eat-3 or the profission gene drp-1
      are not required for apoptosis activation in C. elegans.
  - statement: DRP-1 promotes mitochondrial elimination in dying cells
    supporting_text: drp-1 and fis-2 function independent of one another and the Bcl-2
      homolog CED-9 and downstream of the CED-3 caspase to promote elimination of
      mitochondria in dying cells
  - statement: CED-3 cleaves DRP-1; this cleavage is required for pro-apoptotic but
      not fission function
    supporting_text: CED-3 can cleave DRP-1, which appears to be important for DRP-1's
      proapoptotic function, but not its mitochondria fission function.
- id: PMID:18827010
  title: CED-9 and mitochondrial homeostasis in C. elegans muscle.
  findings:
  - statement: CED-9 overexpression causes interconnected mitochondria
    supporting_text: increased CED-9 expression in these cells produces highly interconnected
      mitochondria.
  - statement: DRP-1 overexpression suppresses CED-9-induced mitochondrial connectivity
    supporting_text: This mitochondrial phenotype is partially suppressed by increased
      expression of the dynamin-related GTPase DRP-1
- id: PMID:19327994
  title: Bcl-2 proteins EGL-1 and CED-9 do not regulate mitochondrial fission or fusion
    in Caenorhabditis elegans.
  findings:
  - statement: drp-1 mutants have defective fission with normal fusion
    supporting_text: in a drp-1 mutant, in which mitochondrial fusion occurs but mitochondrial
      fission is defective
  - statement: EGL-1 and CED-9 do not regulate mitochondrial fission or fusion
    supporting_text: loss of egl-1 or ced-9, or overexpression of their gene products,
      had no apparent effect on mitochondrial connectivity or mitochondrial size.
- id: PMID:21463460
  title: The dynamin-related protein DRP-1 and the insulin signaling pathway cooperate
    to modulate Caenorhabditis elegans longevity.
  findings: []
- id: PMID:21949250
  title: A molecular switch that governs mitochondrial fusion and fission mediated
    by the BCL2-like protein CED-9 of Caenorhabditis elegans.
  findings:
  - statement: DRP-1 interacts with CED-9
    supporting_text: CED-9 also physically interacts with the mitochondrial fission
      protein DRP-1
  - statement: Interaction is enhanced by GTP rather than GDP
    supporting_text: this interaction can be enhanced when CED-9 is associated with
      the BH3-only protein EGL-1.
  - statement: DRP-1 is recruited to mitochondria by CED-9/EGL-1 complex
    supporting_text: the EGL-1-CED-9 complex promotes mitochondrial fission by recruiting
      DRP-1 to mitochondria
- id: PMID:33734301
  title: Autophagy facilitates mitochondrial rebuilding after acute heat stress via
    a DRP-1-dependent process.
  findings: []
- id: file:worm/drp-1/drp-1-deep-research-falcon.md
  title: Deep research summary for drp-1
  findings:
  - statement: DRP-1 is recruited from cytosol to OMM by adaptor proteins including
      FIS-1, FIS-2 and MFF-1/MFF-2
  - statement: Loss of drp-1 in dystrophin mutants reduces TUNEL-positive muscle cells
      from 5.28 to 2.07 per animal
  - statement: drp-1 disruption during development extends daf-2 (IIS) mutant longevity
core_functions:
- description: DRP-1 is a dynamin-related GTPase that controls mitochondrial outer
    membrane fission. It is recruited from the cytosol to the mitochondrial outer
    membrane at constriction sites, where it oligomerizes and uses GTP hydrolysis
    to drive membrane scission.
  molecular_function:
    id: GO:0003924
    label: GTPase activity
  directly_involved_in:
  - id: GO:0000266
    label: mitochondrial fission
  locations:
  - id: GO:0005741
    label: mitochondrial outer membrane
  - id: GO:0005829
    label: cytosol
  supported_by:
  - reference_id: PMID:10619028
    supporting_text: wild-type DRP-1 contributes to the final stages of mitochondrial
      division by controlling scission of the mitochondrial outer membrane.
proposed_new_terms: []
suggested_questions:
- question: Does C. elegans DRP-1 directly mediate peroxisome fission, or is this
    function performed by a different dynamin-related protein?
- question: What are the specific adaptor proteins that recruit DRP-1 to the mitochondrial
    outer membrane in C. elegans?
- question: How does post-translational modification (e.g., phosphorylation, sumoylation)
    regulate DRP-1 activity in worms?
suggested_experiments:
- description: Direct visualization of DRP-1 at peroxisomes to confirm peroxisome
    fission function
- description: Biochemical characterization of C. elegans DRP-1 GTPase activity and
    membrane binding properties
- description: Identification of the CED-3 cleavage products and their functional
    differences
tags:
- caeel-mitophagy