WDR35 (IFT121) is a subunit of the intraflagellar transport complex A (IFT-A), built from two N-terminal WD40 beta-propellers followed by a TPR-rich alpha-solenoid, an architecture related to COPI/clathrin vesicle coat proteins. Within IFT-A it belongs to the peripheral subcomplex (IFT43-IFT121-IFT139), where the IFT43-IFT121 dimer connects to the IFT122 core subunit. IFT-A mediates retrograde intraflagellar transport along the axoneme and, with the TULP3 adaptor, the entry of membrane proteins (GPCRs, Smoothened, EVC/EVC2) into the primary cilium; WDR35 is required for ciliary import of many membrane cargoes and for efficient delivery of membrane to the nascent cilium. WDR35 localizes to cilia (axoneme, tip), the basal body and centrosome. Fibroblasts lacking WDR35 fail to form or form short, bulbous cilia, and mouse Wdr35 mutants die at midgestation with Hedgehog-pathway defects. Biallelic WDR35 variants cause short-rib thoracic dysplasia with polydactyly (SRTD7) and cranioectodermal dysplasia (CED2).
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:27932497 Intraflagellar transport-A complex mediates ciliary entry an... | REMOVE | Summary: Interaction of WDR35 with IFT43 (and IFT122) within the IFT-A peripheral subcomplex. Reason: Generic protein binding derived from an interaction with another IFT-A subunit or partner. The interaction itself is real and well documented, but 'protein binding' conveys no functional information; the informative content (stable membership of the IFT-A complex) is already captured by the part_of intraciliary transport particle A annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0005515 protein binding | IPI PMID:29220510 Ciliopathy-associated mutations of IFT122 impair ciliary pro... | REMOVE | Summary: Interaction of WDR35 with IFT43 (and IFT122) within the IFT-A peripheral subcomplex. Reason: Generic protein binding derived from an interaction with another IFT-A subunit or partner. The interaction itself is real and well documented, but 'protein binding' conveys no functional information; the informative content (stable membership of the IFT-A complex) is already captured by the part_of intraciliary transport particle A annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Interaction of WDR35 with IFT43 (and IFT122) within the IFT-A peripheral subcomplex. Reason: Generic protein binding derived from an interaction with another IFT-A subunit or partner. The interaction itself is real and well documented, but 'protein binding' conveys no functional information; the informative content (stable membership of the IFT-A complex) is already captured by the part_of intraciliary transport particle A annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Interaction of WDR35 with IFT43 (and IFT122) within the IFT-A peripheral subcomplex. Reason: Generic protein binding derived from an interaction with another IFT-A subunit or partner. The interaction itself is real and well documented, but 'protein binding' conveys no functional information; the informative content (stable membership of the IFT-A complex) is already captured by the part_of intraciliary transport particle A annotations. Removal does not mean the interaction is false. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0005813 centrosome | IEA GO_REF:0000120 | ACCEPT | Summary: Centrosome localization (inferred from mouse Wdr35). Reason: Endogenous WDR35 localizes to centrosomes as well as cilia in mouse embryos; the centrosome/basal body is where IFT-A assembles before ciliary entry. Electronic annotation consistent with experimental and phylogenetic evidence. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. |
| GO:0005813 centrosome | ISS GO_REF:0000024 | ACCEPT | Summary: Centrosome localization (inferred from mouse Wdr35). Reason: Endogenous WDR35 localizes to centrosomes as well as cilia in mouse embryos; the centrosome/basal body is where IFT-A assembles before ciliary entry. Electronic annotation consistent with experimental and phylogenetic evidence. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. |
| GO:0005929 cilium | NAS PMID:27806291 Role for the IFT-A Complex in Selective Transport to the Pri... | ACCEPT | Summary: WDR35 localizes to cilia. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005929 cilium | TAS Reactome:R-HSA-5610725 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005929 cilium | TAS Reactome:R-HSA-5610726 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005929 cilium | TAS Reactome:R-HSA-5617829 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005929 cilium | TAS Reactome:R-HSA-5624949 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005929 cilium | TAS Reactome:R-HSA-5625416 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005929 cilium | TAS Reactome:R-HSA-5625424 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005929 cilium | TAS Reactome:R-HSA-5625426 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: WDR35 is a ciliary IFT-A subunit; endogenous protein localizes to cilia. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0005930 axoneme | IBA GO_REF:0000033 | ACCEPT | Summary: Axoneme localization. Reason: IFT trains carrying IFT-A move along axonemal microtubules; WDR35 is detected along the ciliary axoneme. Phylogenetically supported (IBA). Supporting Evidence: file:human/WDR35/WDR35-uniprot.txt Cytoplasm, cytoskeleton, cilium axoneme PMID:36775821 Intraflagellar transport (IFT) complexes, IFT-A and IFT-B, form bidirectional trains that move along the axonemal microtubules and are essential for assembling and maintaining cilia. |
| GO:0005930 axoneme | IEA GO_REF:0000120 | ACCEPT | Summary: Axoneme localization. Reason: IFT trains carrying IFT-A move along axonemal microtubules; WDR35 is detected along the ciliary axoneme. Phylogenetically supported (IBA). Supporting Evidence: file:human/WDR35/WDR35-uniprot.txt Cytoplasm, cytoskeleton, cilium axoneme PMID:36775821 Intraflagellar transport (IFT) complexes, IFT-A and IFT-B, form bidirectional trains that move along the axonemal microtubules and are essential for assembling and maintaining cilia. |
| GO:0005930 axoneme | ISS GO_REF:0000024 | ACCEPT | Summary: Axoneme localization. Reason: IFT trains carrying IFT-A move along axonemal microtubules; WDR35 is detected along the ciliary axoneme. Phylogenetically supported (IBA). Supporting Evidence: file:human/WDR35/WDR35-uniprot.txt Cytoplasm, cytoskeleton, cilium axoneme PMID:36775821 Intraflagellar transport (IFT) complexes, IFT-A and IFT-B, form bidirectional trains that move along the axonemal microtubules and are essential for assembling and maintaining cilia. |
| GO:0030991 intraciliary transport particle A | IBA GO_REF:0000033 | ACCEPT | Summary: WDR35/IFT121 is a subunit of the IFT-A complex. Reason: Membership of the IFT-A peripheral subcomplex is shown biochemically, structurally (human IFT-A cryo-EM) and by phylogeny. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located PMID:36775821 Here we report cryo-EM structures of human IFT-A complexes in the presence and absence of TULP3 at overall resolutions of 3.0-3.9 Γ
. file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0030991 intraciliary transport particle A | IDA PMID:20889716 TULP3 bridges the IFT-A complex and membrane phosphoinositid... | ACCEPT | Summary: WDR35/IFT121 is a subunit of the IFT-A complex. Reason: Membership of the IFT-A peripheral subcomplex is shown biochemically, structurally (human IFT-A cryo-EM) and by phylogeny. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located PMID:36775821 Here we report cryo-EM structures of human IFT-A complexes in the presence and absence of TULP3 at overall resolutions of 3.0-3.9 Γ
. file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0030991 intraciliary transport particle A | IDA PMID:27932497 Intraflagellar transport-A complex mediates ciliary entry an... | ACCEPT | Summary: WDR35/IFT121 is a subunit of the IFT-A complex. Reason: Membership of the IFT-A peripheral subcomplex is shown biochemically, structurally (human IFT-A cryo-EM) and by phylogeny. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located PMID:36775821 Here we report cryo-EM structures of human IFT-A complexes in the presence and absence of TULP3 at overall resolutions of 3.0-3.9 Γ
. file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0030991 intraciliary transport particle A | IDA PMID:36775821 Human IFT-A complex structures provide molecular insights in... | ACCEPT | Summary: WDR35/IFT121 is a subunit of the IFT-A complex. Reason: Membership of the IFT-A peripheral subcomplex is shown biochemically, structurally (human IFT-A cryo-EM) and by phylogeny. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located PMID:36775821 Here we report cryo-EM structures of human IFT-A complexes in the presence and absence of TULP3 at overall resolutions of 3.0-3.9 Γ
. file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0030991 intraciliary transport particle A | IEA GO_REF:0000107 | ACCEPT | Summary: WDR35/IFT121 is a subunit of the IFT-A complex. Reason: Membership of the IFT-A peripheral subcomplex is shown biochemically, structurally (human IFT-A cryo-EM) and by phylogeny. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located PMID:36775821 Here we report cryo-EM structures of human IFT-A complexes in the presence and absence of TULP3 at overall resolutions of 3.0-3.9 Γ
. file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0030991 intraciliary transport particle A | IPI PMID:27173435 An organelle-specific protein landscape identifies novel dis... | ACCEPT | Summary: WDR35/IFT121 is a subunit of the IFT-A complex. Reason: Membership of the IFT-A peripheral subcomplex is shown biochemically, structurally (human IFT-A cryo-EM) and by phylogeny. Supporting Evidence: PMID:27932497 the IFT-A complex is divided into a core subcomplex, composed of IFT122/IFT140/IFT144, which is associated with TULP3, and a peripheral subcomplex, composed of IFT43/IFT121/IFT139, where IFT139 is most distally located PMID:36775821 Here we report cryo-EM structures of human IFT-A complexes in the presence and absence of TULP3 at overall resolutions of 3.0-3.9 Γ
. file:human/WDR35/WDR35-uniprot.txt Interacts directy with IFT122, ITF43 and TTC21B |
| GO:0035720 intraciliary anterograde transport | IDA PMID:20889716 TULP3 bridges the IFT-A complex and membrane phosphoinositid... | ACCEPT | Summary: Intraciliary anterograde transport. Reason: IFT-A rides anterograde trains and WDR35 is essential for ciliary entry of many membrane proteins, i.e. for their anterograde import. The 40472089 full text discusses TULP3-dependent GPR45 entry with IFT-A as the TULP3 partner; deferring to the curator, the term is biologically correct. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:20889716 IFT-A is linked to retrograde ciliary transport, but, surprisingly, we find that the IFT-A complex has a second role directing ciliary entry of TULP3. PMID:27932497 the IFT-A complex mediates not only retrograde trafficking but also entry into cilia of GPCRs |
| GO:0035720 intraciliary anterograde transport | IDA PMID:40472089 GPR45 modulates GΞ±(s) at primary cilia of the paraventricula... | ACCEPT | Summary: Intraciliary anterograde transport. Reason: IFT-A rides anterograde trains and WDR35 is essential for ciliary entry of many membrane proteins, i.e. for their anterograde import. The 40472089 full text discusses TULP3-dependent GPR45 entry with IFT-A as the TULP3 partner; deferring to the curator, the term is biologically correct. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:20889716 IFT-A is linked to retrograde ciliary transport, but, surprisingly, we find that the IFT-A complex has a second role directing ciliary entry of TULP3. PMID:27932497 the IFT-A complex mediates not only retrograde trafficking but also entry into cilia of GPCRs |
| GO:0035721 intraciliary retrograde transport | IBA GO_REF:0000033 | ACCEPT | Summary: Intraciliary retrograde transport. Reason: IFT-A mediates retrograde IFT; WDR35-null cells show disrupted retrograde transport of IFT88 and IFT-A loss causes tip accumulation. Supported by IBA and experimental data. Supporting Evidence: PMID:27806291 Intraflagellar transport sub-complex A (IFT-A) is known to regulate retrograde IFT in the cilium. PMID:27932497 Intraflagellar transport (IFT)-A and -B complexes mediate retrograde and anterograde ciliary protein trafficking, respectively. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0035721 intraciliary retrograde transport | IMP PMID:20889716 TULP3 bridges the IFT-A complex and membrane phosphoinositid... | ACCEPT | Summary: Intraciliary retrograde transport. Reason: IFT-A mediates retrograde IFT; WDR35-null cells show disrupted retrograde transport of IFT88 and IFT-A loss causes tip accumulation. Supported by IBA and experimental data. Supporting Evidence: PMID:27806291 Intraflagellar transport sub-complex A (IFT-A) is known to regulate retrograde IFT in the cilium. PMID:27932497 Intraflagellar transport (IFT)-A and -B complexes mediate retrograde and anterograde ciliary protein trafficking, respectively. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0035721 intraciliary retrograde transport | NAS PMID:27806291 Role for the IFT-A Complex in Selective Transport to the Pri... | ACCEPT | Summary: Intraciliary retrograde transport. Reason: IFT-A mediates retrograde IFT; WDR35-null cells show disrupted retrograde transport of IFT88 and IFT-A loss causes tip accumulation. Supported by IBA and experimental data. Supporting Evidence: PMID:27806291 Intraflagellar transport sub-complex A (IFT-A) is known to regulate retrograde IFT in the cilium. PMID:27932497 Intraflagellar transport (IFT)-A and -B complexes mediate retrograde and anterograde ciliary protein trafficking, respectively. file:human/WDR35/WDR35-uniprot.txt As a component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in ciliogenesis and ciliary protein trafficking |
| GO:0036064 ciliary basal body | IEA GO_REF:0000107 | ACCEPT | Summary: Ciliary basal body localization (inferred from mouse). Reason: WDR35 localizes to centrosomes/basal bodies, where IFT trains assemble. Electronic annotation consistent with experimental and phylogenetic evidence. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. |
| GO:0036064 ciliary basal body | ISS GO_REF:0000024 | ACCEPT | Summary: Ciliary basal body localization (inferred from mouse). Reason: WDR35 localizes to centrosomes/basal bodies, where IFT trains assemble. Electronic annotation consistent with experimental and phylogenetic evidence. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. |
| GO:0042073 intraciliary transport | IMP PMID:29220510 Ciliopathy-associated mutations of IFT122 impair ciliary pro... | ACCEPT | Summary: Intraciliary transport (IMP). Reason: Loss of IFT-A subunits impairs ciliary protein trafficking. Supporting Evidence: PMID:29220510 knockout (KO) of the IFT122 gene in hTERT-RPE1 cells using the CRISPR/Cas9 system led to a severe ciliogenesis defect, whereas KO of other IFT-A genes had minor effects on ciliogenesis but impaired ciliary protein trafficking PMID:29220510 The intraflagellar transport (IFT) machinery containing the IFT-A and IFT-B complexes mediates ciliary protein trafficking. |
| GO:0060271 cilium assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Cilium assembly. Reason: Human and mouse fibroblasts lacking WDR35 fail to produce cilia; WDR35 regulates cilium assembly by controlling transport of distinct cargoes. Supported by IMP and IBA. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. PMID:27806291 We found that Wdr35 regulates cilium assembly by selectively regulating transport of distinct cargoes. |
| GO:0060271 cilium assembly | IEA GO_REF:0000120 | ACCEPT | Summary: Cilium assembly. Reason: Human and mouse fibroblasts lacking WDR35 fail to produce cilia; WDR35 regulates cilium assembly by controlling transport of distinct cargoes. Supported by IMP and IBA. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. PMID:27806291 We found that Wdr35 regulates cilium assembly by selectively regulating transport of distinct cargoes. |
| GO:0060271 cilium assembly | IMP PMID:21473986 Human and mouse mutations in WDR35 cause short-rib polydacty... | ACCEPT | Summary: Cilium assembly. Reason: Human and mouse fibroblasts lacking WDR35 fail to produce cilia; WDR35 regulates cilium assembly by controlling transport of distinct cargoes. Supported by IMP and IBA. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. PMID:27806291 We found that Wdr35 regulates cilium assembly by selectively regulating transport of distinct cargoes. |
| GO:0060271 cilium assembly | NAS PMID:27806291 Role for the IFT-A Complex in Selective Transport to the Pri... | ACCEPT | Summary: Cilium assembly. Reason: Human and mouse fibroblasts lacking WDR35 fail to produce cilia; WDR35 regulates cilium assembly by controlling transport of distinct cargoes. Supported by IMP and IBA. Supporting Evidence: PMID:21473986 We show that endogenous WDR35 localizes to cilia and centrosomes throughout the developing embryo and that human and mouse fibroblasts lacking the protein fail to produce cilia. PMID:27806291 We found that Wdr35 regulates cilium assembly by selectively regulating transport of distinct cargoes. |
| GO:0061512 protein localization to cilium | IMP PMID:29220510 Ciliopathy-associated mutations of IFT122 impair ciliary pro... | ACCEPT | Summary: protein localization to cilium. Reason: WDR35/IFT-A is essential for entry of many membrane proteins into the primary cilium, and IFT-A with TULP3 promotes ciliary trafficking of GPCRs. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:20889716 TULP3 and IFT-A, in turn, promote trafficking of a subset of G protein-coupled receptors (GPCRs), but not Smoothened, to cilia. PMID:36775821 TULP3, the cargo adapter, interacts with IFT-A through its N-terminal region, and interface mutations disrupt cargo transport. |
| GO:0097499 protein localization to non-motile cilium | IDA PMID:20889716 TULP3 bridges the IFT-A complex and membrane phosphoinositid... | ACCEPT | Summary: protein localization to non-motile cilium. Reason: WDR35/IFT-A is essential for entry of many membrane proteins into the primary cilium, and IFT-A with TULP3 promotes ciliary trafficking of GPCRs. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:20889716 TULP3 and IFT-A, in turn, promote trafficking of a subset of G protein-coupled receptors (GPCRs), but not Smoothened, to cilia. PMID:36775821 TULP3, the cargo adapter, interacts with IFT-A through its N-terminal region, and interface mutations disrupt cargo transport. |
| GO:0097499 protein localization to non-motile cilium | IDA PMID:36775821 Human IFT-A complex structures provide molecular insights in... | ACCEPT | Summary: protein localization to non-motile cilium. Reason: WDR35/IFT-A is essential for entry of many membrane proteins into the primary cilium, and IFT-A with TULP3 promotes ciliary trafficking of GPCRs. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:20889716 TULP3 and IFT-A, in turn, promote trafficking of a subset of G protein-coupled receptors (GPCRs), but not Smoothened, to cilia. PMID:36775821 TULP3, the cargo adapter, interacts with IFT-A through its N-terminal region, and interface mutations disrupt cargo transport. |
| GO:0097499 protein localization to non-motile cilium | IDA PMID:40472089 GPR45 modulates GΞ±(s) at primary cilia of the paraventricula... | ACCEPT | Summary: protein localization to non-motile cilium. Reason: WDR35/IFT-A is essential for entry of many membrane proteins into the primary cilium, and IFT-A with TULP3 promotes ciliary trafficking of GPCRs. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:20889716 TULP3 and IFT-A, in turn, promote trafficking of a subset of G protein-coupled receptors (GPCRs), but not Smoothened, to cilia. PMID:36775821 TULP3, the cargo adapter, interacts with IFT-A through its N-terminal region, and interface mutations disrupt cargo transport. |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5624952 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: IFT-A reaches the ciliary tip on IFT trains and accumulates there when retrograde transport is disrupted. Supporting Evidence: PMID:27932497 IFT139-KO cells showed the accumulation of IFT-A, IFT-B, and GPCRs, including Smoothened and GPR161, at the bulged ciliary tips |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5625416 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: IFT-A reaches the ciliary tip on IFT trains and accumulates there when retrograde transport is disrupted. Supporting Evidence: PMID:27932497 IFT139-KO cells showed the accumulation of IFT-A, IFT-B, and GPCRs, including Smoothened and GPR161, at the bulged ciliary tips |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5625421 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: IFT-A reaches the ciliary tip on IFT trains and accumulates there when retrograde transport is disrupted. Supporting Evidence: PMID:27932497 IFT139-KO cells showed the accumulation of IFT-A, IFT-B, and GPCRs, including Smoothened and GPR161, at the bulged ciliary tips |
| GO:0097542 ciliary tip | TAS Reactome:R-HSA-5625426 | ACCEPT | Summary: Reactome pathway-level traceable author statement placing the protein in the cilium as part of the intraflagellar transport / ciliary cargo trafficking reactions. Reason: IFT-A reaches the ciliary tip on IFT trains and accumulates there when retrograde transport is disrupted. Supporting Evidence: PMID:27932497 IFT139-KO cells showed the accumulation of IFT-A, IFT-B, and GPCRs, including Smoothened and GPR161, at the bulged ciliary tips |
| GO:0140597 protein carrier activity | IDA PMID:20889716 TULP3 bridges the IFT-A complex and membrane phosphoinositid... | ACCEPT | Summary: Contributes to protein carrier activity (IDA). Reason: IFT-A together with TULP3 carries membrane proteins into cilia; WDR35 interacts robustly with cargoes. The contributes_to qualifier correctly reflects a complex-level activity. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:36775821 TULP3, the cargo adapter, interacts with IFT-A through its N-terminal region, and interface mutations disrupt cargo transport. |
| GO:0140597 protein carrier activity | IDA PMID:36775821 Human IFT-A complex structures provide molecular insights in... | ACCEPT | Summary: Contributes to protein carrier activity (IDA). Reason: IFT-A together with TULP3 carries membrane proteins into cilia; WDR35 interacts robustly with cargoes. The contributes_to qualifier correctly reflects a complex-level activity. Supporting Evidence: PMID:27806291 Wdr35 is essential for entry of many membrane proteins into the cilium through robust interactions with cargoes and other IFT-A subunits PMID:36775821 TULP3, the cargo adapter, interacts with IFT-A through its N-terminal region, and interface mutations disrupt cargo transport. |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Does the COPI-like architecture of WDR35 reflect a direct membrane-coat function in delivering vesicles to the nascent ciliary membrane, independent of its role in IFT trains?
Suggested experts: Mill P, Dynlacht BD
Q: WDR35 lacks HPA subcellular data; can a validated antibody confirm its basal body versus axonemal distribution in human ciliated cells?
Experiment: Liposome flotation and cargo-peptide binding assays with purified WDR35/IFT43 heterodimer and disease variants, coupled with rescue of WDR35-KO RPE1 ciliary membrane delivery.
Hypothesis: WDR35 directly binds lipid membranes or vesicle cargo through its beta-propellers.
Type: biochemical reconstitution
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)