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CHE-13 (Chemotaxis abnormal protein 13; gene locus F59C6.7) is the C. elegans ortholog of vertebrate Intraflagellar Transport protein 57 (IFT57), also known as HIPPI (Huntingtin-Interacting Protein 1 Protein Interactor) in mammals (taschner2016intraflagellartransportproteins pages 1-2). The protein belongs to the IFT57 family and is a structural/adaptor component of the intraflagellar transport (IFT) machinery rather than an enzyme or classical transporter. Its key structural features include an N-terminal calponin homology (CH) domain (IPR019530/PF10498) and a C-terminal coiled-coil region, both of which mediate critical protein-protein interactions within the IFT-B complex (taschner2016intraflagellartransportproteins pages 3-4, taschner2016intraflagellartransportproteins pages 1-2).
The following table summarizes the key properties and annotations for CHE-13/IFT57:
| Property | Description |
|---|---|
| Gene name | che-13; also described as Chemotaxis abnormal protein 13 in C. elegans literature and UniProt; corresponds to the IFT57 family member in worm (efimenko2006caenorhabditiselegansdyf2an pages 1-2, taschner2016intraflagellartransportproteins pages 1-2) |
| Protein name | Intraflagellar transport protein CHE-13 / IFT57; a non-enzymatic structural/adaptor component of the intraflagellar transport machinery rather than a catalyst or transporter with a discrete small-molecule substrate (efimenko2006caenorhabditiselegansdyf2an pages 1-2, taschner2016intraflagellartransportproteins pages 3-4) |
| Organism | Caenorhabditis elegans (worm), the specific target organism verified from UniProt and supported by the cited cilia literature (efimenko2006caenorhabditiselegansdyf2an pages 1-2, kaplan1993adualmechanosensory pages 3-4) |
| UniProt accession | Q93833 (user-supplied UniProt record for C. elegans CHE-13) |
| Protein family | IFT57 family; conserved component of the IFT-B machinery required for cilia/flagella assembly and transport, with CHE-13 representing the worm ortholog (taschner2016intraflagellartransportproteins pages 1-2, houde2006hippiisessential pages 6-8) |
| Key domain | Contains an N-terminal calponin-homology (CH) domain and a C-terminal coiled-coil region; the CH domain mediates interaction with IFT172, whereas the coiled-coil region supports association with IFT38 (taschner2016intraflagellartransportproteins pages 3-4, taschner2016intraflagellartransportproteins pages 5-5, taschner2016intraflagellartransportproteins pages 1-2) |
| Subcellular localization | Localizes to the ciliary base/basal body region in C. elegans sensory neurons and functions within sensory cilia; CHE-13 has also been observed as an IFT-B component entering residual cilia in mutant backgrounds (cevik2013activetransportand pages 3-5, efimenko2006caenorhabditiselegansdyf2an pages 6-8) |
| IFT complex membership (IFT-B2) | CHE-13/IFT57 is a member of the IFT-B2 (peripheral) subcomplex of IFT-B, together with IFT172, IFT80, IFT54, IFT38, and IFT20; this subcomplex can assemble stably apart from the IFT-B1 core (taschner2016intraflagellartransportproteins pages 5-5, taschner2016intraflagellartransportproteins pages 1-2, taschner2016theintraflagellartransport pages 6-8) |
| Direct protein interactions | IFT172: bound by the IFT57 CH domain; IFT38: forms a stable heterodimer/coiled-coil pair with IFT57; IFT88/IFT52: part of the bridging interface linking IFT-B2 to IFT-B1 via IFT57/38 and IFT88/52N; IFT20: interacts with IFT57 within IFT-B and has been pulled down with it; KIF3B/kinesin-2: vertebrate studies implicate IFT57 and IFT20 in association with KIF3B; dynein-2/WDR34 and related dynein-2 subunits: IFT57 contributes to dynein-2–IFT-B interactions important for effective IFT (taschner2016intraflagellartransportproteins pages 5-5, taschner2016intraflagellartransportproteins pages 8-9, taschner2016intraflagellartransportproteins pages 5-7, follit2006theintraflagellartransport pages 4-6, bhogaraju2013intraflagellartransportcomplex pages 5-6, hiyamizu2023multipleinteractionsof pages 1-2) |
| Biological function | CHE-13 is a structural/adaptor component of anterograde intraflagellar transport needed for sensory cilium assembly and maintenance. Its main role is to help organize the IFT-B train architecture, connect IFT-B2 to IFT-B1, and support transport of ciliary cargoes rather than directly binding tubulin as the main cargo receptor. In C. elegans, complex B defects including CHE-13 loss cause severe shortening of cilia and impaired forward IFT (efimenko2006caenorhabditiselegansdyf2an pages 1-2, taschner2016intraflagellartransportproteins pages 3-4, taschner2016intraflagellartransportproteins pages 8-9) |
| Mutant phenotype in C. elegans | che-13 mutants show severe ultrastructural defects in ciliated sensory endings, markedly impaired sensory cilium formation/length, and chemotaxis abnormalities; they also show reduced nose-touch avoidance, consistent with dysfunction of ciliated sensory neurons such as ASH/FLP/OLQ-linked pathways (kaplan1993adualmechanosensory pages 3-4, efimenko2006caenorhabditiselegansdyf2an pages 1-2) |
| Mammalian ortholog | The mammalian ortholog is IFT57/HIPPI. In mouse, loss of Hippi/IFT57 eliminates nodal monocilia, disrupts left-right patterning, and impairs Sonic hedgehog signaling in the neural tube, showing strong evolutionary conservation of ciliary function (houde2006hippiisessential pages 6-8, houde2006hippiisessential pages 5-6, houde2006hippiisessential pages 2-3) |
| Disease associations in humans | Human IFT57 is associated in current datasets with Bardet-Biedl syndrome, orofaciodigital syndrome / OFD18, and hypothyroidism signals in Open Targets; more broadly, its conserved ciliary role supports classification as a ciliopathy-related gene. A 2025 study also reported defective IFT57 as a novel cause of Bardet-Biedl syndrome, though that primary paper was not directly retrievable here (OpenTargets Search: -IFT57) |
Table: This table summarizes the identity, localization, molecular interactions, and biological roles of C. elegans CHE-13/IFT57, along with conserved mammalian and disease-relevant information. It is useful as a compact reference for the gene’s functional annotation.
CHE-13 is not an enzyme, transporter, or signaling receptor. Rather, it functions as a structural scaffolding and adaptor protein within the IFT-B complex, which is essential for the bidirectional transport of cargo molecules along the axonemal microtubules of cilia. The IFT-B complex is subdivided into two stable subcomplexes: the IFT-B1 (core) and IFT-B2 (peripheral) subcomplexes. CHE-13/IFT57 is a member of the IFT-B2 subcomplex, together with IFT172, IFT80, IFT54, IFT38, and IFT20 (taschner2016intraflagellartransportproteins pages 1-2, taschner2016intraflagellartransportproteins pages 5-5). This IFT-B2 subcomplex can assemble independently of the IFT-B1 core, forming a stable six-subunit complex (taschner2016intraflagellartransportproteins pages 1-2).
Biochemical and structural studies, primarily using recombinant Chlamydomonas reinhardtii proteins, have defined the molecular interactions through which IFT57 organizes the IFT-B2 complex architecture. The calponin homology (CH) domain of IFT57 directly mediates the interaction with IFT172, forming a strong association that helps stabilize IFT172 positioning within the complex (taschner2016intraflagellartransportproteins pages 3-4, taschner2016intraflagellartransportproteins pages 5-5, corbo2024newevidenceon pages 33-39). Notably, among the three CH domain-containing proteins in IFT-B2 (IFT57, IFT54, and IFT38), only IFT54 binds αβ-tubulin as cargo; the CH domains of IFT57 and IFT38 instead mediate protein-protein interactions—IFT57's CH domain with IFT172, and IFT38's CH domain with IFT80 (taschner2016intraflagellartransportproteins pages 1-2).
The C-terminal coiled-coil region of IFT57 mediates interaction with the coiled-coil region of IFT38, forming a stable heterodimer (taschner2016intraflagellartransportproteins pages 3-4, taschner2016intraflagellartransportproteins pages 5-5). This IFT57/IFT38 pair is critical for the overall architecture and integrity of the IFT-B2 subcomplex.
A key structural role of CHE-13/IFT57 is its participation in bridging the IFT-B2 peripheral subcomplex to the IFT-B1 core. The IFT57/38 complex on the IFT-B2 side directly contacts the preformed IFT88/IFT52N subcomplex on the IFT-B1 side, forming a salt-stable interaction that links the two major subcomplexes into the IFT-B holocomplex (taschner2016theintraflagellartransport pages 6-8, taschner2016intraflagellartransportproteins pages 8-9, taschner2016intraflagellartransportproteins pages 5-7). GST pull-down experiments demonstrated that both IFT88 and IFT52N are required for this bridging interaction, and that the IFT-B2 complex is efficiently pulled down by IFT88/IFT52N when IFT57/38 are present (taschner2016intraflagellartransportproteins pages 8-9). Mutations altering IFT52 conformation at this interface are associated with ciliopathy in humans, underscoring the functional significance of this bridging architecture (liu2025structuremakesa pages 2-3).
IFT57 participates in coupling the IFT-B complex to both anterograde and retrograde molecular motors. Co-immunoprecipitation experiments in vertebrate cells and yeast two-hybrid analyses have implicated IFT57 and IFT20 in binding to KIF3B, the motor subunit of the heterotrimeric kinesin-2 complex that powers anterograde IFT (bhogaraju2013intraflagellartransportcomplex pages 5-6, follit2006theintraflagellartransport pages 4-6). IFT20 strongly interacts with both IFT57 and KIF3B, suggesting that the IFT20-IFT57 module may serve as an interface for anterograde motor coupling (bhogaraju2013intraflagellartransportcomplex pages 5-6).
On the retrograde side, a systematic interaction screen identified that IFT57 also contributes to interactions with dynein-2 subunits, including WDR34, which interacts with IFT57 via its C-terminal WD40 repeat domain (hiyamizu2023multipleinteractionsof pages 1-2). These multiple interactions between IFT-B and dynein-2 are required for effective bidirectional intraflagellar transport.
The complete set of known IFT57 protein interactions is summarized below:
| Interaction Partner | Complex/Context | Domain Involved in IFT57 | Evidence Type | Functional Significance | Reference |
|---|---|---|---|---|---|
| IFT172 | IFT-B2 subcomplex | CH domain | Crystal structure / pulldown | Stabilizes and positions IFT172 within IFT-B2 architecture (taschner2016intraflagellartransportproteins pages 5-5, taschner2016intraflagellartransportproteins pages 3-4, taschner2016intraflagellartransportproteins pages 1-2) | Taschner 2016 |
| IFT38 | IFT-B2 subcomplex | Coiled-coil domain | Copurification | Forms a stable IFT57–IFT38 heterodimer that supports IFT-B2 assembly (taschner2016intraflagellartransportproteins pages 5-5, taschner2016intraflagellartransportproteins pages 3-4, taschner2016intraflagellartransportproteins pages 1-2) | Taschner 2016 |
| IFT88/IFT52N | IFT-B1/B2 bridge | IFT57/38 complex | GST pulldown | Bridges IFT-B2 to the IFT-B1 core to form the IFT-B holocomplex (taschner2016theintraflagellartransport pages 6-8, taschner2016intraflagellartransportproteins pages 8-9, taschner2016intraflagellartransportproteins pages 5-7) | Taschner 2016 |
| IFT20 | IFT-B2 subcomplex | Not specified | GST pulldown | Supports shared IFT-B subcomplex organization and likely contributes to kinesin-2 coupling through the IFT20–IFT57 module (bhogaraju2013intraflagellartransportcomplex pages 5-6, follit2006theintraflagellartransport pages 4-6) | Follit 2006 |
| KIF3B (kinesin-2) | Motor-IFT interaction | Not specified | Co-IP / Y2H | Implicates IFT57 in anterograde motor coupling of IFT particles (bhogaraju2013intraflagellartransportcomplex pages 5-6) | Bhogaraju 2013 |
| Dynein-2 (WDR34) | Motor-IFT interaction | Not specified | Interaction screen | Supports retrograde motor coupling and effective bidirectional IFT coordination (hiyamizu2023multipleinteractionsof pages 1-2) | Hiyamizu 2023 |
| IFT80 | IFT-B2 subcomplex | Via IFT172 association | Copurification | Contributes to higher-order IFT-B2 architecture together with the IFT57–IFT172 module (taschner2016intraflagellartransportproteins pages 5-5, taschner2016intraflagellartransportproteins pages 3-4) | Taschner 2016 |
| SANS/USH1G | Ciliary USH network | N-terminal region | Y2H / co-localization | Links the Usher syndrome protein network to IFT-B proteins including IFT57 (OpenTargets Search: -IFT57) | Sorusch 2019 |
Table: This table summarizes experimentally supported protein-protein interactions involving C. elegans CHE-13/IFT57 and conserved orthologous IFT57 complexes. It is useful for linking domain-level interactions to IFT-B assembly, motor coupling, and ciliary disease-related networks.
In C. elegans sensory neurons, CHE-13/IFT57 localizes prominently to the ciliary base/basal body region. Fluorescence microscopy studies using CHE-13::mCherry or CHE-13::YFP fusion constructs have demonstrated that CHE-13 concentrates at the basal body, with a gap of approximately 1 μm between CHE-13 signal and the proximal ciliary membrane marker ARL-13, corresponding to the transition zone (cevik2013activetransportand pages 3-5). CHE-13 has been used as a basal body marker in localization studies of other ciliary proteins.
As a component of IFT-B, CHE-13 also undergoes bidirectional motility along the ciliary axoneme as part of IFT trains. In dyf-2 mutant backgrounds (which disrupt the IFT-A component), CHE-13::YFP can still enter and accumulate in residual cilia, distinguishing it from some other IFT-B proteins (such as OSM-5) that are more dependent on DYF-2 for ciliary entry (efimenko2006caenorhabditiselegansdyf2an pages 6-8). This observation positions CHE-13 in a hierarchy of IFT particle assembly, with some degree of independence from IFT-A components for ciliary localization.
CHE-13 is essential for the formation and maintenance of sensory cilia in C. elegans. Loss-of-function mutations in che-13 result in drastically reduced cilia length and severe ultrastructural defects affecting all ciliated sensory endings (efimenko2006caenorhabditiselegansdyf2an pages 1-2, kaplan1993adualmechanosensory pages 3-4). These phenotypes are characteristic of IFT complex B deficiency, reflecting a requirement for CHE-13 in anterograde IFT—the kinesin-powered movement of IFT particles and associated cargoes from the ciliary base toward the tip (efimenko2006caenorhabditiselegansdyf2an pages 1-2).
che-13 mutants exhibit profound chemotaxis defects, which is the basis for the gene's name. They display severely impaired responses to chemical attractants and repellents, consistent with the disruption of sensory receptor-bearing ciliated endings in amphid and phasmid neurons. che-13 mutants are among the most severely affected chemotaxis-defective mutants in C. elegans, because the ultrastructural defects extend to all ciliated sensory endings, unlike mutants affecting only specific subsets of cilia (kaplan1993adualmechanosensory pages 3-4).
Beyond chemotaxis, che-13 mutants show significantly reduced nose-touch avoidance—a mechanosensory behavior mediated by ciliated neurons including ASH, FLP, and OLQ. The severity of touch sensitivity defects correlates with the extent of ciliary ultrastructural defects; che-13 mutants have more severe structural damage and correspondingly greater behavioral impairment than mutants such as osm-6 (kaplan1993adualmechanosensory pages 3-4).
As with other IFT-B mutants, che-13 animals are expected to show dye-filling defects (Dyf phenotype), reflecting the inability of fluorescent dyes to access the environmentally exposed sensory cilia due to structural abnormalities. This phenotype is commonly used as a diagnostic marker for cilia defects in C. elegans (efimenko2006caenorhabditiselegansdyf2an pages 1-2).
Recent work has shown that disruption of sensory neuron cilia (as occurs in che-13 and other IFT mutants) elicits acute responses from associated glial cells (amphid sheath glia). These responses include increased extracellular matrix accumulation around cilia and changes in glial gene expression and secretory activity, representing a homeostatic mechanism by which glia monitor and respond to dendrite substructure integrity (varandas2025gliadetectand pages 1-2).
The mammalian ortholog of CHE-13, known as IFT57 or HIPPI, has been extensively characterized. In mouse, Hippi knockout results in the complete absence of motile monocilia on embryonic node cells, leading to loss of leftward nodal flow and severe left-right axis patterning defects, including randomized expression of normally asymmetric genes (Nodal, Lefty-2, Pitx2) (houde2006hippiisessential pages 6-8, houde2006hippiisessential pages 5-6). Hippi-null embryos also display neural tube closure defects, exencephaly, hypotelorism, and polydactyly, reflecting impaired Sonic hedgehog (Shh) signaling in the neural tube (houde2006hippiisessential pages 5-6). The mutant embryos are lethal before E10.5 (houde2006hippiisessential pages 2-3).
In adult ciliated cells, Hippi interacts with other IFT proteins including Ift88 and KIF3A, confirming its conserved role in ciliary protein complexes (houde2006hippiisessential pages 6-8).
A distinctive feature of mammalian IFT57/HIPPI is its dual cellular function. In addition to its ciliary role, HIPPI was independently identified as an adaptor protein that mediates pro-apoptotic signaling from polyglutamine-expanded huntingtin through the HIP1-HIPPI complex, activating caspase-8 to trigger cell death in Huntington's disease pathology (houde2006hippiisessential pages 1-2). The ciliary function operates primarily during development, while the apoptosis signaling function has been implicated in adult brain pathology under pathogenic stress conditions (houde2006hippiisessential pages 8-9). Some neuronal degenerative phenotypes in ciliopathy patients may involve IFT57's non-ciliary functions, complicating interpretation of disease mechanisms (gerdes2009thevertebrateprimary pages 8-9).
OpenTargets data indicate that human IFT57 is associated with several ciliopathy-related conditions, including Bardet-Biedl syndrome, orofaciodigital syndrome type 18 (OFD18), and hypothyroidism (OpenTargets Search: -IFT57). A 2025 study by Nitoiu et al. identified defective IFT57 as a novel cause of Bardet-Biedl syndrome in a human patient, further confirming the clinical relevance of this gene's ciliary function. These associations are consistent with the essential role of IFT57 in cilia assembly and function, as ciliopathies commonly arise from mutations in IFT components.
CHE-13 (IFT57) in C. elegans is a non-enzymatic structural adaptor protein of the IFT-B2 subcomplex that is essential for intraflagellar transport and sensory cilia biogenesis. Its primary molecular role is to organize the IFT-B train architecture through specific domain-mediated interactions: the N-terminal calponin homology domain binds IFT172, the C-terminal coiled-coil mediates heterodimerization with IFT38, and the IFT57/38 module bridges the IFT-B2 peripheral subcomplex to the IFT-B1 core via contacts with IFT88/IFT52. CHE-13 localizes to the basal body region and undergoes IFT-dependent motility within sensory cilia. Loss of CHE-13 causes severe cilia structural defects across all ciliated sensory neurons, resulting in chemotaxis abnormalities, touch avoidance deficits, and dye-filling failure. The protein's function is deeply conserved across evolution, with the mammalian ortholog IFT57/HIPPI being essential for node cilia assembly, left-right patterning, and Hedgehog signaling, and mutations in human IFT57 being linked to Bardet-Biedl syndrome and orofaciodigital syndrome.
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