id: G5ECZ4
gene_symbol: dyf-2
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
description: >-
  DYF-2 is the Caenorhabditis elegans ortholog of human WDR19 (IFT144 in
  Chlamydomonas), a core subunit of the intraflagellar transport complex A
  (IFT-A). It is a large (1364 aa) WD40 β-propeller plus tetratricopeptide-repeat
  (TPR) solenoid scaffold protein with no catalytic domain, expressed selectively
  in ciliated sensory neurons and localizing along the axoneme of the non-motile
  sensory cilium. As part of IFT-A, DYF-2 is required for retrograde
  (tip-to-base) intraflagellar transport and for the assembly and structural
  integrity of the IFT particle as a whole. Its conserved WD40 domain is the key
  factor that reassembles the IFT-B subcomplex into the IFT-A–dynein machinery for
  retrograde transport at the ciliary tip, and it couples the BBSome to moving IFT
  particles (WDR19 interacts directly with BBS1). Loss of DYF-2 produces severely
  truncated cilia with disrupted IFT and mislocalized IFT-A and IFT-B components; a
  hypomorphic WD40-domain allele selectively abolishes retrograde IFT and causes
  IFT-B accumulation at the ciliary tip. Because sensory cilia are the sites of
  chemo- and osmosensation in the worm, dyf-2 mutants are dye-filling defective and
  show impaired chemotaxis and osmotic avoidance. WDR19 mutations cause human
  ciliopathies (e.g. cranioectodermal dysplasia/Sensenbrenner and nephronophthisis),
  underscoring a conserved role in cilium biogenesis.
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: []
  - 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:16957054
    title: Caenorhabditis elegans DYF-2, an orthologue of human WDR19, is a component
      of the intraflagellar transport machinery in sensory cilia.
    findings: []
    reference_review:
      relevance: HIGH
      correctness: VERIFIED
      review_notes: >-
        Founding paper that identified dyf-2 as the WDR19 ortholog and an IFT
        component in C. elegans sensory cilia (transgenic rescue + allele
        sequencing). Cached record is abstract-only (full_text_available: false),
        so experimental IDA/IMP annotations from this paper rest on the full text
        the WormBase curator read; the abstract independently confirms the
        IFT-machinery-integrity role and cilia/chemosensation phenotypes.
  - id: PMID:22922713
    title: The BBSome controls IFT assembly and turnaround in cilia.
    findings: []
    reference_review:
      relevance: HIGH
      correctness: VERIFIED
      review_notes: >-
        Full text available and read. Establishes DYF-2 = WDR19/IFT144 as an IFT
        structural protein whose WD40 domain is required for IFT turnaround and
        retrograde IFT, and for BBSome docking onto IFT particles (WDR19–BBS1
        interaction). Directly supports the retrograde-transport and
        cilium-assembly IMP annotations.
  - id: PMID:28479320
    title: Dynein-Driven Retrograde Intraflagellar Transport Is Triphasic in C. elegans
      Sensory Cilia.
    findings: []
    reference_review:
      relevance: HIGH
      correctness: VERIFIED
      review_notes: >-
        Affinity purification / mass spectrometry defined the worm IFT-A complex
        (che-11, daf-10, dyf-2, ift-139, ift-43, ifta-1); basis for the
        ComplexPortal (CPX-1289) NAS annotations placing DYF-2 in IFT-A and in the
        retrograde-transport process. Cached record is abstract-only.
existing_annotations:
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: is_active_in
    review:
      summary: >-
        DYF-2/WDR19 is an IFT-A subunit that acts within the cilium; ciliary
        localization is directly demonstrated in the worm and conserved (the mouse
        ortholog WDR19 also localizes to cilia).
      action: ACCEPT
      reason: >-
        Core localization. Phylogenetic inference agrees with direct experimental
        evidence in C. elegans (see the IDA non-motile cilium annotation) and with
        conservation of WDR19 ciliary localization.
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: the mouse orthologue of DYF-2, WDR19, also localizes to cilia
  - term:
      id: GO:0035721
      label: intraciliary retrograde transport
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: involved_in
    review:
      summary: >-
        As a core IFT-A subunit, DYF-2 is required for retrograde (tip-to-base)
        intraflagellar transport, the defining function of the IFT-A complex.
      action: ACCEPT
      reason: >-
        Represents the core biological process of the gene. Phylogenetic inference
        is corroborated by direct experimental evidence that a dyf-2 WD40 allele
        selectively abolishes retrograde IFT.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: in dyf-2(jhu616), IFT-B component OSM-6 showed characteristic
            anterograde IFT movement, but lost almost all retrograde IFT movements
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: involved_in
    review:
      summary: >-
        Retrograde IFT by IFT-A is required to build and maintain the ciliary
        axoneme; loss of DYF-2 gives severely truncated cilia.
      action: ACCEPT
      reason: >-
        Well-supported by phylogeny and by the null-allele phenotype (truncated
        cilia, disrupted IFT). A core process, though downstream of the direct IFT
        transport activity.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: the latter show severely truncated cilia and completely
            disrupted IFT transport
  - term:
      id: GO:0030991
      label: intraciliary transport particle A
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    qualifier: part_of
    review:
      summary: >-
        DYF-2 is a core subunit of the IFT-A complex, established by orthology to
        WDR19/IFT144 and by direct mass-spec identification in the worm IFT-A
        complex.
      action: ACCEPT
      reason: >-
        Core complex membership. Phylogenetic inference agrees with the
        experimental (NAS/mass-spec) IFT-A assignment.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: In Chlamydomonas, IFT144 (the homolog of DYF-2) is an
            IFT-A component
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: IEA
    original_reference_id: GO_REF:0000120
    qualifier: located_in
    review:
      summary: >-
        Electronic (SubCell/ARBA) assertion of ciliary localization, redundant with
        the experimental IDA and IBA cilium annotations.
      action: ACCEPT
      reason: >-
        Correct location; consistent with direct experimental evidence, albeit
        redundant with the higher-evidence cilium annotations.
  - term:
      id: GO:0008104
      label: intracellular protein localization
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    qualifier: involved_in
    review:
      summary: >-
        Generic ARBA electronic term. DYF-2's actual role is transporting/localizing
        IFT and cargo proteins within the cilium; a cilium-specific term is more
        accurate and informative.
      action: MODIFY
      reason: >-
        "intracellular protein localization" is uninformatively broad. The
        experimental basis (loss of DYF-2 mislocalizes ciliary IFT-A/IFT-B
        proteins) and DYF-2's IFT-A function are better captured by
        "protein localization to cilium".
      proposed_replacement_terms:
        - id: GO:0061512
          label: protein localization to cilium
  - term:
      id: GO:0030990
      label: intraciliary transport particle
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    qualifier: part_of
    review:
      summary: >-
        ARBA electronic assertion of membership in the (generic) intraflagellar
        transport particle. This is the parent of the specific, experimentally
        supported IFT-A membership.
      action: KEEP_AS_NON_CORE
      reason: >-
        Not wrong, but subsumed by and less informative than the IFT particle A
        (GO:0030991) annotation, which is the correct specific complex. Retained as
        a correct but non-core generalization.
  - term:
      id: GO:0035721
      label: intraciliary retrograde transport
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    qualifier: involved_in
    review:
      summary: >-
        InterPro2GO electronic annotation of the IFT-A retrograde-transport role,
        redundant with the IBA/NAS/IMP annotations to the same term.
      action: ACCEPT
      reason: >-
        Correct core process; consistent with, though redundant with, the
        experimental and phylogenetic annotations to this term.
  - term:
      id: GO:0044782
      label: cilium organization
    evidence_type: IEA
    original_reference_id: GO_REF:0000117
    qualifier: involved_in
    review:
      summary: >-
        ARBA electronic annotation to the parent term of cilium assembly.
      action: KEEP_AS_NON_CORE
      reason: >-
        Correct but general; the more specific "cilium assembly" / "non-motile
        cilium assembly" annotations capture the role more precisely.
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: located_in
    review:
      summary: >-
        ComplexPortal (CPX-1289) NAS assertion of ciliary localization for the
        IFT-A complex, based on the mass-spec study of worm retrograde IFT.
      action: ACCEPT
      reason: >-
        Correct core localization, consistent with experimental IDA evidence.
  - term:
      id: GO:0030991
      label: intraciliary transport particle A
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: part_of
    review:
      summary: >-
        ComplexPortal NAS annotation placing DYF-2 in the IFT-A complex, based on
        affinity purification / mass spectrometry of the worm IFT-A complex.
      action: ACCEPT
      reason: >-
        Core complex membership, experimentally grounded (mass-spec identification
        of DYF-2 in IFT-A).
  - term:
      id: GO:0035721
      label: intraciliary retrograde transport
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: involved_in
    review:
      summary: >-
        ComplexPortal NAS annotation of the IFT-A retrograde-transport role.
      action: ACCEPT
      reason: >-
        Core process, consistent with the experimental and phylogenetic evidence.
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: NAS
    original_reference_id: PMID:28479320
    qualifier: involved_in
    review:
      summary: >-
        ComplexPortal NAS annotation of the cilium-assembly role of IFT-A.
      action: ACCEPT
      reason: >-
        Correct; downstream outcome of the IFT-A transport function. Consistent
        with the null-allele phenotype.
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: IMP
    original_reference_id: PMID:22922713
    qualifier: acts_upstream_of_or_within
    review:
      summary: >-
        Mutant analysis: dyf-2(m160) null shows severely truncated cilia,
        demonstrating a requirement for DYF-2 in ciliary assembly/maintenance.
      action: ACCEPT
      reason: >-
        Directly supported by the mutant phenotype; a core process (downstream of
        the direct retrograde-IFT activity).
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: the latter show severely truncated cilia and completely
            disrupted IFT transport
  - term:
      id: GO:0035721
      label: intraciliary retrograde transport
    evidence_type: IMP
    original_reference_id: PMID:22922713
    qualifier: acts_upstream_of_or_within
    review:
      summary: >-
        The hypomorphic dyf-2(jhu616) WD40-domain allele selectively abolishes
        retrograde IFT while leaving anterograde IFT intact, directly implicating
        DYF-2 in retrograde intraflagellar transport.
      action: ACCEPT
      reason: >-
        Strong, direct experimental evidence for the core molecular process of the
        gene.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: our observations reveal a role for the WD40 domain of
            DYF-2 as the key factor in reassembling IFT-B subcomplex into
            IFT-A-dynein retrograde machinery
  - term:
      id: GO:0006935
      label: chemotaxis
    evidence_type: IMP
    original_reference_id: PMID:16957054
    qualifier: involved_in
    review:
      summary: >-
        dyf-2 mutants have defective sensory cilia and are impaired in chemotaxis
        to volatile odorants. This is a whole-organism sensory phenotype downstream
        of the ciliary/IFT defect, not a direct molecular function of DYF-2.
      action: KEEP_AS_NON_CORE
      reason: >-
        Valid IMP phenotype but a pleiotropic downstream consequence of ciliary
        dysfunction shared by essentially all cilium/IFT genes; not part of the core
        molecular/cellular function of DYF-2.
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: leads to defects in cilia structure and chemosensation
            in the nematode
  - term:
      id: GO:0007635
      label: chemosensory behavior
    evidence_type: IMP
    original_reference_id: PMID:16957054
    qualifier: involved_in
    review:
      summary: >-
        Chemosensory-behavior defect in dyf-2 mutants, a downstream consequence of
        defective sensory cilia.
      action: KEEP_AS_NON_CORE
      reason: >-
        Legitimate mutant phenotype but downstream of the ciliary/IFT defect; not a
        core function.
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: leads to defects in cilia structure and chemosensation
            in the nematode
  - term:
      id: GO:0008104
      label: intracellular protein localization
    evidence_type: IMP
    original_reference_id: PMID:16957054
    qualifier: involved_in
    review:
      summary: >-
        Loss of DYF-2 alters the assembly and motility of IFT components and
        mislocalizes ciliary IFT-A/IFT-B proteins. The generic "intracellular
        protein localization" term understates that this is protein localization
        within the cilium.
      action: MODIFY
      reason: >-
        The experimental readout is mislocalization of ciliary IFT proteins;
        "protein localization to cilium" is the accurate, informative term. Same
        replacement proposed for the redundant ARBA IEA annotation.
      proposed_replacement_terms:
        - id: GO:0061512
          label: protein localization to cilium
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: Loss of DYF-2 function selectively affects the assembly
            and motility of different IFT components
  - term:
      id: GO:0030992
      label: intraciliary transport particle B
    evidence_type: IDA
    original_reference_id: PMID:16957054
    qualifier: part_of
    review:
      summary: >-
        The 2006 founding paper concluded that DYF-2 "can associate with IFT
        particle complex B" (based on DYF-2 co-migration behavior in a BBS mutant
        with partially disrupted IFT particles), while also noting that dyf-2
        mutations interfere with IFT-A components. Subsequent work firmly places
        WDR19/IFT144/DYF-2 as a core IFT-A subunit (direct mass-spec identification
        in the worm IFT-A complex; Chlamydomonas IFT144 = IFT-A).
      action: MARK_AS_OVER_ANNOTATED
      reason: >-
        DYF-2's stable complex membership is IFT-A, not IFT-B. The IFT-B
        "association" reflects DYF-2 acting at the IFT-A/IFT-B interface (its WD40
        domain reassembles IFT-B into the IFT-A–dynein retrograde machinery at the
        tip), a functional interplay rather than IFT-B core membership. The
        experimental observation is genuine but its complex-membership
        interpretation has been superseded; flagged as over-annotation rather than
        removed, in deference to the original experimental call.
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: we conclude that DYF-2 can associate with IFT particle
            complex B
        - reference_id: PMID:22922713
          supporting_text: In Chlamydomonas, IFT144 (the homolog of DYF-2) is an
            IFT-A component
  - term:
      id: GO:0042048
      label: olfactory behavior
    evidence_type: IMP
    original_reference_id: PMID:16957054
    qualifier: involved_in
    review:
      summary: >-
        dyf-2 mutants are impaired in responses to volatile (olfactory) odorants
        such as pyrazine and iso-amyl alcohol, a downstream consequence of the
        sensory-cilia defect.
      action: KEEP_AS_NON_CORE
      reason: >-
        Valid mutant phenotype (odorant response requires functional AWA/AWC
        sensory cilia) but a pleiotropic downstream consequence of the ciliary/IFT
        defect, not a core function of DYF-2.
  - term:
      id: GO:0042073
      label: intraciliary transport
    evidence_type: IDA
    original_reference_id: PMID:16957054
    qualifier: involved_in
    review:
      summary: >-
        DYF-2 is a component of the intraflagellar transport machinery that moves
        along the sensory-cilium axoneme; direct experimental evidence in the worm.
      action: ACCEPT
      reason: >-
        Core process. This general IFT term is the parent of the more specific
        retrograde-IFT annotation; both are appropriate for a bidirectionally
        transported IFT-A subunit.
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: component of the intraflagellar transport machinery in
            sensory cilia
  - term:
      id: GO:0097730
      label: non-motile cilium
    evidence_type: IDA
    original_reference_id: PMID:16957054
    qualifier: located_in
    review:
      summary: >-
        DYF-2 localizes to the non-motile sensory cilia of C. elegans neurons
        (direct experimental evidence).
      action: ACCEPT
      reason: >-
        Core localization, accurately specific to the worm's non-motile sensory
        cilia.
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: component of the intraflagellar transport machinery in
            sensory cilia
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IMP
    original_reference_id: PMID:16957054
    qualifier: involved_in
    review:
      summary: >-
        DYF-2 is required to build the non-motile sensory cilium; loss of function
        gives defects in cilium structure.
      action: ACCEPT
      reason: >-
        Correct and accurately specific for the worm's non-motile sensory cilia; a
        core process (downstream of the direct retrograde-IFT activity).
      supported_by:
        - reference_id: PMID:16957054
          supporting_text: leads to defects in cilia structure and chemosensation
            in the nematode
core_functions:
  - description: >-
      Structural constituent of the intraflagellar transport complex A (IFT-A) that
      drives retrograde (tip-to-base) intraflagellar transport along the sensory
      cilium. As the WDR19/IFT144 ortholog, DYF-2 has no catalytic activity; it acts
      as a WD40/TPR scaffold within IFT-A, and its WD40 domain reassembles the IFT-B
      subcomplex into the IFT-A–dynein machinery for retrograde transport at the
      ciliary tip.
    molecular_function:
      id: GO:0005198
      label: structural molecule activity
    directly_involved_in:
      - id: GO:0035721
        label: intraciliary retrograde transport
      - id: GO:0042073
        label: intraciliary transport
    locations:
      - id: GO:0097730
        label: non-motile cilium
    in_complex:
      id: GO:0030991
      label: intraciliary transport particle A
    supported_by:
      - reference_id: PMID:22922713
        supporting_text: the major role of DYF-2 as an IFT structural protein
      - reference_id: PMID:22922713
        supporting_text: our observations reveal a role for the WD40 domain of
          DYF-2 as the key factor in reassembling IFT-B subcomplex into
          IFT-A-dynein retrograde machinery
  - description: >-
      Required for assembly and structural integrity of the sensory cilium: IFT-A
      function via DYF-2 is needed to build and maintain the non-motile ciliary
      axoneme and to keep IFT-A/IFT-B components correctly localized. DYF-2 also
      couples the BBSome to moving IFT particles (WDR19 binds BBS1), integrating
      cargo adaptor function with the IFT cycle.
    directly_involved_in:
      - id: GO:0060271
        label: cilium assembly
      - id: GO:1905515
        label: non-motile cilium assembly
    locations:
      - id: GO:0097730
        label: non-motile cilium
    supported_by:
      - reference_id: PMID:16957054
        supporting_text: DYF-2, that plays a critical role in maintaining the
          structural and functional integrity of the IFT machinery
      - reference_id: PMID:22922713
        supporting_text: the WD40 domain of DYF-2 protein is critical for the
          association between the BBSome and IFT particles
knowledge_gaps:
  - gap_statement: >-
      DYF-2 has no assigned molecular function and no term to express one. Its role
      is to be a structural constituent of the IFT-A particle, but GO has no
      "structural constituent of the intraflagellar transport particle" molecular
      function term, so the gene reads as MF-dark despite a well-understood cellular
      and process-level role.
    boundary: >-
      It is firmly established that DYF-2 = WDR19/IFT144 is a WD40+TPR scaffolding
      subunit of IFT-A with no catalytic domain, required for retrograde IFT and
      cilium assembly. What is missing is a molecular-function representation: the
      worm GOA record carries only cellular-component and biological-process terms
      and no molecular_function annotation at all.
    gap_kind:
      - ONTOLOGY
      - CURATION
    dark_aspect: MF_DARK
    status: OPEN
    significance: >-
      This is the canonical "structural subunit" ontology gap: a mechanistically
      well-understood protein that cannot be annotated with an informative MF term,
      contributing to apparent molecular-function darkness across the IFT/ciliopathy
      gene set.
    resolution: >-
      Develop/adopt a molecular-function term for a structural constituent of the
      IFT particle (analogous to "structural constituent of ribosome"), then
      annotate DYF-2 (and other IFT-A/IFT-B core subunits) to it.
    provenance:
      - reference_id: PMID:22922713
        supporting_text: the major role of DYF-2 as an IFT structural protein
        reference_section_type: RESULTS
    proposed_terms:
      - proposed_name: structural constituent of intraflagellar transport particle
        proposed_definition: >-
          The action of a protein that contributes to the structural integrity of an
          intraflagellar transport (IFT) particle (IFT-A or IFT-B subcomplex), for
          example by acting as a WD40/TPR scaffold that holds core IFT subunits
          together and enables their bidirectional transport along the ciliary
          axoneme, without itself catalyzing a biochemical reaction.
        proposed_parent:
          id: GO:0005198
          label: structural molecule activity
  - gap_statement: >-
      The molecular interface by which the DYF-2/WDR19 WD40 domain docks the BBSome
      onto moving IFT particles, and the direct IFT-A subunit contacts of DYF-2 in
      the worm, are inferred (from point mutants, BiFC and cross-species proteomics),
      not resolved structurally. How the WD40 domain physically "reassembles" IFT-B
      into the IFT-A–dynein machinery at the ciliary tip is a model, not a solved
      mechanism.
    boundary: >-
      Genetics and imaging establish that the conserved WD40 residue (worm G361 /
      mouse WDR19 G341) is required for BBSome association and retrograde IFT, and
      that WDR19 interacts with BBS1; the worm IFT-A composition (che-11, daf-10,
      dyf-2, ift-139, ift-43, ifta-1) is known from mass spectrometry. The
      subunit-resolved architecture and the DYF-2–BBSome binding interface are not
      determined.
    gap_kind:
      - BIOLOGY
    dark_aspect: RESIDUAL_SUBGAP
    status: OPEN
    significance: >-
      The tip-reassembly/BBSome-docking step is the load-bearing, incompletely
      understood mechanism of IFT turnaround; resolving it would explain how
      retrograde transport is licensed and how ciliopathy-causing WDR19 mutations
      disrupt it.
    resolution: >-
      Cryo-EM of the worm IFT-A complex and of an IFT-A–BBSome assembly; structure-
      guided separation-of-function mutagenesis of the DYF-2 WD40 surface with
      retrograde-IFT and BBSome-docking readouts.
    provenance:
      - reference_id: PMID:22922713
        supporting_text: probably mediate the interaction between the BBSome and the
          IFT machinery
        reference_section_type: RESULTS
proposed_new_terms:
  - proposed_name: structural constituent of intraflagellar transport particle
    proposed_definition: >-
      The action of a protein that contributes to the structural integrity of an
      intraflagellar transport (IFT) particle (IFT-A or IFT-B subcomplex), for
      example by acting as a WD40/TPR scaffold that holds core IFT subunits together
      and enables their bidirectional transport along the ciliary axoneme, without
      itself catalyzing a biochemical reaction.
    proposed_parent:
      id: GO:0005198
      label: structural molecule activity
suggested_questions:
  - question: What is the subunit-resolved architecture of the C. elegans IFT-A
      complex, and which IFT-A subunits does DYF-2/WDR19 directly contact?
    experts:
      - Ou G
  - question: What is the structural basis of the DYF-2/WDR19 WD40-domain interface
      that docks the BBSome onto moving IFT particles?
    experts:
      - Hu J
suggested_experiments:
  - hypothesis: The DYF-2 WD40 domain provides a dedicated docking surface for the
      BBSome on IFT particles, separable from its role in IFT-A integrity.
    description: >-
      Generate structure-guided separation-of-function alleles across the DYF-2 WD40
      surface and score, in vivo, retrograde IFT (kymography of IFT-B markers),
      BBSome co-migration/docking (BiFC or dual-color imaging), and cilium length,
      to map the BBSome-docking interface independently of IFT-A assembly.
    experiment_type: structure-function mutagenesis
  - hypothesis: DYF-2 occupies a defined position within an IFT-A scaffold that can
      be resolved structurally.
    description: >-
      Reconstitute or affinity-purify the worm IFT-A complex and determine its
      architecture by cryo-EM, assigning DYF-2/WDR19 and its direct neighbors and
      testing whether ciliopathy-mimicking substitutions perturb specific interfaces.
    experiment_type: structural biology
tags:
  - caeel-ciliopathy