| Property | Details |
|---|---|
| Verified identity | **C. elegans dyf-11** corresponds to UniProt Q17595 and is the nematode ortholog of mammalian **TRAF3IP1/IFT54**; literature also identifies DYF-11 as an IFT-associated ciliary protein in sensory neurons (pqac-00000003, pqac-00000023) |
| Gene names / orthologs across species | **C. elegans:** dyf-11; **human/vertebrates:** TRAF3IP1, also called **IFT54**; older literature also refers to mammalian family members as **MIP-T3**. Reviews and primary studies consistently place these proteins in the conserved IFT-B2/peripheral IFT-B subcomplex (pqac-00000000, pqac-00000001, pqac-00000024, pqac-00000031) |
| Protein family / complex membership | DYF-11/TRAF3IP1/IFT54 belongs to the conserved **IFT54/TRAF3IP1 family** and is a component of the **IFT-B2 (peripheral IFT-B) subcomplex** together with IFT20, IFT38, IFT57, IFT80, and IFT172 (pqac-00000001, pqac-00000024, pqac-00000025, pqac-00000031) |
| Key domains | IFT54 contains an **N-terminal calponin homology (CH) domain** and a **C-terminal coiled-coil region**. The CH domain is the major tubulin-binding module within IFT-B2, while the coiled-coil region mediates stable association with IFT20 (pqac-00000004, pqac-00000005, pqac-00000009, pqac-00000030) |
| Key biochemical interactions | Forms a stable **IFT54–IFT20 heterodimer**; the IFT54/20 unit associates with **IFT57/38** and interfaces with **IFT80** within IFT-B2. IFT-B2 is linked to IFT-B1 mainly through the **IFT57/38–IFT88/52N** connection (pqac-00000004, pqac-00000006, pqac-00000024, pqac-00000026, pqac-00000028) |
| Motor interactions | IFT54 interacts with both major IFT motors: reviews state it binds **kinesin-2** and **dynein-2**, and 2023 work showed extensive functional interaction with dynein-2, especially via **WDR60**, supporting retrograde transport coupling (pqac-00000010, pqac-00000012, pqac-00000013) |
| Cargo-related interactions | The CH domain binds **αβ-tubulin** directly through a basic surface patch; the measured affinity for soluble tubulin is in the **low micromolar range (~3 ± 1 μM)**, supporting a role in tubulin delivery during ciliogenesis (pqac-00000004, pqac-00000005, pqac-00000006, pqac-00000008) |
| Subcellular localization | In vertebrate cells, IFT54 localizes to the **ciliary transition zone/transition fibers**, co-localizes with **Cep164**, and is also detected near **proximal centrioles** with **γ-tubulin**; in **C. elegans**, the DYF-11 homolog **translocates within sensory cilia via IFT** (pqac-00000000, pqac-00000009, pqac-00000020, pqac-00000023) |
| Expression / cell-type context in worm | Available worm evidence places DYF-11 in **ciliated sensory neurons**, where it functions in sensory cilia formation and transport-dependent signaling homeostasis (pqac-00000003, pqac-00000023) |
| Primary molecular function | DYF-11/IFT54 is best understood as a **structural and cargo-binding adapter in IFT-B2** that helps couple the IFT particle to tubulin cargo and to anterograde/retrograde motors, thereby supporting **ciliogenesis, cilium maintenance, and bidirectional intraflagellar transport** (pqac-00000001, pqac-00000004, pqac-00000012, pqac-00000024) |
| Broader biological role | Required for **sensory cilium formation/function** in nematodes and for conserved ciliary assembly in other systems; defects impair entry/localization of IFT54 at the ciliary compartment and perturb effective IFT (pqac-00000000, pqac-00000003, pqac-00000020) |
| Extraciliary function | Beyond cilia, TRAF3IP1/IFT54 acts as a **negative regulator of cytoplasmic microtubule stability** through **MAP4**, influencing epithelial organization, polarity, and tissue morphogenesis (pqac-00000014, pqac-00000015, pqac-00000016, pqac-00000017, pqac-00000018) |
| Worm mutant phenotypes | **dyf-11 mutants** show severe **dye-filling defects** in amphid and phasmid neurons (reported as essentially **0% dye fill** in a recent re-analysis), consistent with strong defects in sensory cilia biogenesis/function; mutants also misaccumulate **GFP::DLK-1** in ciliary regions (pqac-00000003) |
| Human disease relevance of ortholog | Mutations in human **TRAF3IP1/IFT54** cause ciliopathy phenotypes including **nephronophthisis**, **retinal degeneration/Senior-Løken syndrome**, and sometimes **Bardet-Biedl-like features**; disease mechanisms likely combine ciliary transport defects with abnormal microtubule stabilization (pqac-00000014, pqac-00000015, pqac-00000016, pqac-00000018) |
| Recent developments | Recent studies emphasize that IFT54 is not just a static IFT-B subunit: **2023** work clarified its multiple contacts with **dynein-2** needed for effective IFT, and newer structural/assembly studies place IFT54 as important for proper **IFT-B2 assembly and recruitment** during ciliogenesis (pqac-00000001, pqac-00000010, pqac-00000025) |


*Table: This table summarizes the verified identity, conserved orthology, domain architecture, interactions, localization, functions, and phenotypes of C. elegans DYF-11 and its mammalian ortholog TRAF3IP1/IFT54. It is useful as a compact reference for the gene’s core ciliary role and its broader relevance to ciliopathy biology.*