| Domain/Region | Interacting Partner | Interaction Type | Functional Consequence | Evidence Source |
|---|---|---|---|---|
| N-terminal calponin homology (CH) domain of IFT38/DYF-3 | IFT80 | Direct protein-protein interaction; CH domain of IFT38 binds IFT80 | Anchors IFT38 within the IFT-B2/peripheral IFT-B subcomplex; supports IFT-B2 architecture rather than tubulin binding by IFT38 itself (pqac-00000007, pqac-00000009, pqac-00000011) | Taschner et al. 2016 (pqac-00000007, pqac-00000009, pqac-00000011) |
| C-terminal coiled-coil region of IFT38/DYF-3 | IFT57 | Stable heterodimer/coiled-coil association | Forms the IFT57/38 module, a core architectural unit of IFT-B2 that links to additional IFT-B2 components and helps organize complex assembly (pqac-00000008, pqac-00000010, pqac-00000011) | Taschner et al. 2016 (pqac-00000008, pqac-00000010, pqac-00000011) |
| IFT57/38 heterodimer (with IFT38 as one subunit) | IFT172, IFT80, IFT54/20 | Higher-order subcomplex assembly within IFT-B2 | Builds the stable six-subunit IFT-B2 complex (IFT172/80/57/54/38/20), which is required for ciliogenesis and ciliary transport complex integrity (pqac-00000002, pqac-00000007, pqac-00000008, pqac-00000012) | Taschner et al. 2016 (pqac-00000002, pqac-00000007, pqac-00000008, pqac-00000012) |
| IFT57/38 module containing IFT38/DYF-3 | IFT88 and N-terminus of IFT52 (IFT52N) | Bridging interaction between IFT-B2 and IFT-B1 | Connects peripheral IFT-B2 to core IFT-B1, enabling holocomplex formation and anterograde IFT train assembly (pqac-00000004, pqac-00000010, pqac-00000012) | Taschner et al. 2016; Tasaki et al. 2025 (pqac-00000004, pqac-00000010, pqac-00000012) |
| IFT38/DYF-3 as an IFT-B2 subunit at basal body/mother centriole | IFT54, IFT52, IFT88-dependent assembly machinery | Subcomplex recruitment/localization dependency | Recruitment of IFT38 to the mother centriole/basal body depends on IFT54 and IFT-B1b components, indicating a role in pre-ciliary IFT-B assembly before ciliogenesis (pqac-00000003, pqac-00000004) | Tasaki et al. 2025 (pqac-00000003, pqac-00000004) |
| IFT38/CLUAP1 | VCP/UBXD3 | UBXD3 binds IFT38/CLUAP1 and directs VCP/UBXD3 motility with IFT | Implicated in assembly/remodeling of IFT trains at the ciliary base and tip; loss of VCP/UBXD3 disrupts bidirectional IFT and train integrity (pqac-00000040) | Tran & Lechtreck 2016 conference report summarizing primary data (pqac-00000040) |
| CLUAP1/IFT38 interactome (non-IFT-associated fraction) | Ephrin-B1 | Proteomic interaction | Suggests a role outside canonical IFT in cytoskeletal arrangement and cell architecture (pqac-00000035, pqac-00000037) | Beyer et al. 2018 (pqac-00000035, pqac-00000037) |
| CLUAP1/IFT38 interactome (non-IFT-associated fraction) | TRIP6 | Proteomic interaction | Links CLUAP1 to actin remodeling and cell migration-related pathways; consistent with actin phenotype in CLUAP1-knockout cells (pqac-00000035, pqac-00000036, pqac-00000037) | Beyer et al. 2018 (pqac-00000035, pqac-00000036, pqac-00000037) |
| CLUAP1/IFT38 interactome (non-IFT-associated fraction) | PDGFA, CCDC6, CEP55, BBS7 | Proteomic interaction network | Expands CLUAP1 functional landscape to ciliogenesis-associated signaling, BBSome-linked pathways, and possible cancer/cell-cycle related processes (pqac-00000013, pqac-00000035, pqac-00000038) | Beyer et al. 2018 (pqac-00000013, pqac-00000035, pqac-00000038) |
| Worm DYF-3 protein in sensory cilia (orthologous structural role inferred from IFT38) | IFT-B complex in ciliated sensory neurons | Conserved orthologous complex membership | Explains why dyf-3 mutants show severe dye-filling defects and abnormal ciliary protein accumulation in amphid/phasmid neurons, consistent with defective IFT-B-mediated cilium assembly/function (pqac-00000001, pqac-00000006, pqac-00000020, pqac-00000023) | Sun et al. 2025; Efimenko et al. 2006 (pqac-00000001, pqac-00000006, pqac-00000020, pqac-00000023) |


*Table: This table summarizes the domain-level interactions and higher-order structural organization of IFT38/DYF-3 within the IFT-B complex, along with selected non-IFT partners. It is useful for linking worm DYF-3 function to conserved mechanistic data from vertebrate CLUAP1/IFT38 studies.*