IFT52

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005515 protein binding	IPI PMID:26980730 Overall Architecture of the Intraflagellar Transport (IFT)-B...	REMOVE	Summary: Protein binding (IPI) from PMID:26980730. The partner is another IFT-B subunit identified in the visible immunoprecipitation (VIP) mapping of IFT-B architecture; this is captured more informatively by the IFT-B complex (GO:0030992) annotation. Reason: Generic 'protein binding' conveys no functional information. Removal does not dispute the reported interaction; the informative content (membership of the IFT complex, or a specific interaction partner) is better represented by complex membership or a specific binding term. Supporting Evidence: PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively.
GO:0005515 protein binding	IPI PMID:26980730 Overall Architecture of the Intraflagellar Transport (IFT)-B...	REMOVE	Summary: Protein binding (IPI) from PMID:26980730. The partner is another IFT-B subunit identified in the visible immunoprecipitation (VIP) mapping of IFT-B architecture; this is captured more informatively by the IFT-B complex (GO:0030992) annotation. Reason: Generic 'protein binding' conveys no functional information. Removal does not dispute the reported interaction; the informative content (membership of the IFT complex, or a specific interaction partner) is better represented by complex membership or a specific binding term. Supporting Evidence: PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively.
GO:0005515 protein binding	IPI PMID:31637240 SANS (USH1G) Molecularly Links the Human Usher Syndrome Prot...	REMOVE	Summary: Protein binding (IPI) from PMID:31637240. Reason: Generic 'protein binding' conveys no functional information. Removal does not dispute the reported interaction; the informative content (membership of the IFT complex, or a specific interaction partner) is better represented by complex membership or a specific binding term.
GO:0005515 protein binding	ISS GO_REF:0000024	REMOVE	Summary: Protein binding (ISS) from GO_REF:0000024. Reason: Generic 'protein binding' conveys no functional information. Removal does not dispute the reported interaction; the informative content (membership of the IFT complex, or a specific interaction partner) is better represented by complex membership or a specific binding term.
GO:0005813 centrosome	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Located in centrosome (IEA, GO_REF:0000107). Reason: The ciliary basal body is a modified mother centriole, so pericentriolar/centrosomal signal for IFT52 largely reflects its pool at the ciliary base; the more specific 'ciliary basal body' location is annotated separately. Retained as a correct but non-core location.
GO:0005814 centriole	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Located in centriole (IBA, GO_REF:0000033). Reason: The ciliary basal body is a modified mother centriole, so pericentriolar/centrosomal signal for IFT52 largely reflects its pool at the ciliary base; the more specific 'ciliary basal body' location is annotated separately. Retained as a correct but non-core location.
GO:0005814 centriole	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Located in centriole (IEA, GO_REF:0000107). Reason: The ciliary basal body is a modified mother centriole, so pericentriolar/centrosomal signal for IFT52 largely reflects its pool at the ciliary base; the more specific 'ciliary basal body' location is annotated separately. Retained as a correct but non-core location.
GO:0005929 cilium	IBA GO_REF:0000033	ACCEPT	Summary: Located in cilium (IBA, GO_REF:0000033). IFT particles containing IFT52 move bidirectionally along the ciliary axoneme. Reason: IFT52 is an intrinsic component of the IFT machinery that operates inside cilia; cilium is a correct (if general) location. More specific locations (ciliary base/basal body, axoneme, ciliary tip) are also annotated. Supporting Evidence: PMID:24140113 Intraflagellar transport (IFT) depends on two evolutionarily conserved modules, subcomplexes A (IFT-A) and B (IFT-B), to drive ciliary assembly and maintenance.
GO:0005929 cilium	IEA GO_REF:0000120	ACCEPT	Summary: Located in cilium (IEA, GO_REF:0000120). IFT particles containing IFT52 move bidirectionally along the ciliary axoneme. Reason: IFT52 is an intrinsic component of the IFT machinery that operates inside cilia; cilium is a correct (if general) location. More specific locations (ciliary base/basal body, axoneme, ciliary tip) are also annotated. Supporting Evidence: PMID:24140113 Intraflagellar transport (IFT) depends on two evolutionarily conserved modules, subcomplexes A (IFT-A) and B (IFT-B), to drive ciliary assembly and maintenance.
GO:0005929 cilium	NAS PMID:26980730 Overall Architecture of the Intraflagellar Transport (IFT)-B...	ACCEPT	Summary: Located in cilium (NAS, PMID:26980730). IFT particles containing IFT52 move bidirectionally along the ciliary axoneme. Reason: IFT52 is an intrinsic component of the IFT machinery that operates inside cilia; cilium is a correct (if general) location. More specific locations (ciliary base/basal body, axoneme, ciliary tip) are also annotated. Supporting Evidence: PMID:24140113 Intraflagellar transport (IFT) depends on two evolutionarily conserved modules, subcomplexes A (IFT-A) and B (IFT-B), to drive ciliary assembly and maintenance.
GO:0005929 cilium	TAS Reactome:R-HSA-5624949	ACCEPT	Summary: Located in cilium (TAS, Reactome:R-HSA-5624949). IFT particles containing IFT52 move bidirectionally along the ciliary axoneme. Reason: IFT52 is an intrinsic component of the IFT machinery that operates inside cilia; cilium is a correct (if general) location. More specific locations (ciliary base/basal body, axoneme, ciliary tip) are also annotated. Supporting Evidence: Reactome:R-HSA-5624949 Both the anterograde and retrograde trains are associated with the outer microtubule doublets and with the inner surface of the flagellar membrane
GO:0005929 cilium	TAS Reactome:R-HSA-5625416	ACCEPT	Summary: Located in cilium (TAS, Reactome:R-HSA-5625416). IFT particles containing IFT52 move bidirectionally along the ciliary axoneme. Reason: IFT52 is an intrinsic component of the IFT machinery that operates inside cilia; cilium is a correct (if general) location. More specific locations (ciliary base/basal body, axoneme, ciliary tip) are also annotated. Supporting Evidence: Reactome:R-HSA-5625416 Anterograde trains travel along the axoneme of the cilium at an estimated rate of 2 micrometers per second in an ATP- and kinesin-2-dependent fashion
GO:0005929 cilium	TAS Reactome:R-HSA-5625424	ACCEPT	Summary: Located in cilium (TAS, Reactome:R-HSA-5625424). IFT particles containing IFT52 move bidirectionally along the ciliary axoneme. Reason: IFT52 is an intrinsic component of the IFT machinery that operates inside cilia; cilium is a correct (if general) location. More specific locations (ciliary base/basal body, axoneme, ciliary tip) are also annotated. Supporting Evidence: Reactome:R-HSA-5625424 At the base of the cilium, retrograde trains are believed to disassemble and recycle for a subsequent round of IFT transport
GO:0005929 cilium	TAS Reactome:R-HSA-5625426	ACCEPT	Summary: Located in cilium (TAS, Reactome:R-HSA-5625426). IFT particles containing IFT52 move bidirectionally along the ciliary axoneme. Reason: IFT52 is an intrinsic component of the IFT machinery that operates inside cilia; cilium is a correct (if general) location. More specific locations (ciliary base/basal body, axoneme, ciliary tip) are also annotated. Supporting Evidence: Reactome:R-HSA-5625426 Retrograde trains are shorter than anterograde particles and travel along the cilliary axoneme at an estimated rate of 3 micrometers per second
GO:0030991 intraciliary transport particle A	IDA PMID:26980730 Overall Architecture of the Intraflagellar Transport (IFT)-B...	REMOVE	Summary: Part of intraciliary transport particle A (IFT-A), IDA from the Katoh et al. 2016 VIP study of IFT-B architecture. IFT52 is a core (IFT-B1) subunit of the IFT-B complex, not of IFT-A. Reason: IFT-A and IFT-B are biochemically distinct subcomplexes (IFT-A: IFT144/WDR19, IFT140, IFT122, IFT139/TTC21B, IFT121/WDR35, IFT43). The cited paper itself mapped IFT52 as a subunit of the IFT-B complex (and the same paper supports the GO:0030992 IFT-B annotation for IFT52); the IFT-A term is contradicted by decades of biochemistry and structural work, and the same IDA appears on every IFT-B subunit annotated from this paper, consistent with a batch term-selection error. IFT-B does associate with IFT-A within IFT trains, but train co-assembly is not complex membership. This is a genuinely contradicted claim, not a judgment based on an abstract foregrounding a different gene. Supporting Evidence: PMID:15955805 revealing a 500-kDa core that contains IFT88, IFT81, IFT74/72, IFT52, IFT46, and IFT27. PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively. PMID:15955805 IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits, respectively. PMID:27932497 Intraflagellar transport (IFT)-A and -B complexes mediate retrograde and anterograde ciliary protein trafficking, respectively.
GO:0030992 intraciliary transport particle B	IBA GO_REF:0000033	ACCEPT	Summary: Part of intraciliary transport particle B (IBA). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: Membership of the IFT-B complex is the defining feature of IFT52 and is established biochemically (Chlamydomonas IFT-B core/peripheral fractionation; human VIP mapping) and structurally. Supporting Evidence: PMID:15955805 revealing a 500-kDa core that contains IFT88, IFT81, IFT74/72, IFT52, IFT46, and IFT27. PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively.
GO:0030992 intraciliary transport particle B	IEA GO_REF:0000107	ACCEPT	Summary: Part of intraciliary transport particle B (IEA). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: Membership of the IFT-B complex is the defining feature of IFT52 and is established biochemically (Chlamydomonas IFT-B core/peripheral fractionation; human VIP mapping) and structurally. Supporting Evidence: PMID:15955805 revealing a 500-kDa core that contains IFT88, IFT81, IFT74/72, IFT52, IFT46, and IFT27. PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively.
GO:0030992 intraciliary transport particle B	IPI PMID:26980730 Overall Architecture of the Intraflagellar Transport (IFT)-B...	ACCEPT	Summary: Part of intraciliary transport particle B (IPI). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: Membership of the IFT-B complex is the defining feature of IFT52 and is established biochemically (Chlamydomonas IFT-B core/peripheral fractionation; human VIP mapping) and structurally. Supporting Evidence: PMID:15955805 revealing a 500-kDa core that contains IFT88, IFT81, IFT74/72, IFT52, IFT46, and IFT27. PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively.
GO:0030992 intraciliary transport particle B	ISS GO_REF:0000024	ACCEPT	Summary: Part of intraciliary transport particle B (ISS). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: Membership of the IFT-B complex is the defining feature of IFT52 and is established biochemically (Chlamydomonas IFT-B core/peripheral fractionation; human VIP mapping) and structurally. Supporting Evidence: PMID:15955805 revealing a 500-kDa core that contains IFT88, IFT81, IFT74/72, IFT52, IFT46, and IFT27. PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively.
GO:0030992 intraciliary transport particle B	ISS GO_REF:0000024	ACCEPT	Summary: Part of intraciliary transport particle B (ISS). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: Membership of the IFT-B complex is the defining feature of IFT52 and is established biochemically (Chlamydomonas IFT-B core/peripheral fractionation; human VIP mapping) and structurally. Supporting Evidence: PMID:15955805 revealing a 500-kDa core that contains IFT88, IFT81, IFT74/72, IFT52, IFT46, and IFT27. PMID:26980730 Using the visible immunoprecipitation assay, which we recently developed as a convenient protein-protein interaction assay, we determined the overall architecture of the IFT-B complex, which can be divided into core and peripheral subcomplexes composed of 10 and 6 subunits, respectively.
GO:0031514 motile cilium	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Located in motile cilium (ISS). IFT is also required to assemble motile cilia and flagella. Reason: IFT is conserved in motile cilia and flagella (it was discovered in Chlamydomonas flagella), so the location is correct; it is kept as non-core because the core role reviewed here is assembly of cilia in general, with most human data from primary cilia. Supporting Evidence: PMID:11062270 Intraflagellar transport (IFT) is a rapid movement of multi-subunit protein particles along flagellar microtubules and is required for assembly and maintenance of eukaryotic flagella.
GO:0032391 photoreceptor connecting cilium	IDA PMID:31637240 SANS (USH1G) Molecularly Links the Human Usher Syndrome Prot...	KEEP AS NON CORE	Summary: Located in photoreceptor connecting cilium (IDA). IFT52 co-localizes with SANS at the ciliary base of mouse photoreceptors. Reason: Correct cell-type-specific ciliary location. Non-core relative to the general IFT role. Supporting Evidence: PMID:31637240 Quantitative immunofluorescence microscopy revealed the co-localization of SANS with IFT20, IFT52, and IFT57 particularly at ciliary base of wild type mouse photoreceptor cells.
GO:0032391 photoreceptor connecting cilium	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Located in photoreceptor connecting cilium (IEA, GO_REF:0000107). Photoreceptor outer segments are modified primary cilia built and maintained by IFT through the connecting cilium. Reason: Correct cell-type-specific ciliary location; retinal degeneration in patients with IFT52 variants is consistent with a requirement for IFT in photoreceptor cilia. Non-core relative to the general IFT role.
GO:0035720 intraciliary anterograde transport	IMP PMID:27466190 IFT52 mutations destabilize anterograde complex assembly, di...	ACCEPT	Summary: Involved in intraciliary anterograde transport (IMP, PMID:27466190). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: IFT-B forms the backbone of anterograde IFT trains that are moved from the ciliary base to the tip by heterotrimeric kinesin-2; IFT52 is an integral subunit of these trains. Supporting Evidence: PMID:27466190 These data demonstrate that IFT52 is essential for anterograde complex integrity and for the biosynthesis and maintenance of cilia. PMID:27466190 The IFT52 mutant cells synthesized a significantly reduced amount of IFT52 protein, leading to reduced synthesis of IFT74, IFT81, IFT88 and ARL13B, other key anterograde complex members.
GO:0035720 intraciliary anterograde transport	NAS PMID:26980730 Overall Architecture of the Intraflagellar Transport (IFT)-B...	ACCEPT	Summary: Involved in intraciliary anterograde transport (NAS, PMID:26980730). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: IFT-B forms the backbone of anterograde IFT trains that are moved from the ciliary base to the tip by heterotrimeric kinesin-2; IFT52 is an integral subunit of these trains. Supporting Evidence: PMID:36354106 The IFT-B complex constitutes the backbone of polymeric IFT trains carrying cargo between the cilium and the cell body. Reactome:R-HSA-5625416 Anterograde trains travel along the axoneme of the cilium at an estimated rate of 2 micrometers per second in an ATP- and kinesin-2-dependent fashion
GO:0036064 ciliary basal body	IEA GO_REF:0000107	ACCEPT	Summary: Located at ciliary basal body (IEA, GO_REF:0000107). IFT complexes assemble into trains and are loaded at the ciliary base (basal body / transition fibres) before entering the cilium. Reason: A large pool of IFT52 resides at the ciliary base, where IFT trains are assembled and where RABL2-mediated capture of IFT-B occurs; this is a well-documented location for IFT subunits. Supporting Evidence: PMID:28625565 GTP-bound RABL2 then binds to the IFT-B holocomplex via the IFT74/81 heterodimer to capture and trigger the entry of IFT-B into cilia, prior to classical motor-driven intraflagellar transport.
GO:0042073 intraciliary transport	IBA GO_REF:0000033	ACCEPT	Summary: Involved in intraciliary transport (IBA). IFT52 is a core (IFT-B1) subunit of the IFT-B complex. Reason: Intraciliary transport is the defining process of IFT complex subunits. The PAINT/IBA node placement is consistent with the conserved IFT machinery. Supporting Evidence: PMID:11062270 Intraflagellar transport (IFT) is a rapid movement of multi-subunit protein particles along flagellar microtubules and is required for assembly and maintenance of eukaryotic flagella. PMID:15955805 Anterograde movement of particles away from the cell body is mediated by kinesin-2, whereas retrograde movement away from the flagellar tip is powered by cytoplasmic dynein 1b/2.
GO:0044292 dendrite terminus	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Located in dendrite terminus (IEA, Ensembl Compara from mouse). Reason: In sensory neurons (e.g. olfactory neurons) cilia emanate from the dendritic terminus/knob, so this reflects the ciliary base pool of IFT52 in neurons. Correct only in that cell-type context; non-core.
GO:0060271 cilium assembly	IBA GO_REF:0000033	ACCEPT	Summary: Involved in cilium assembly (IBA, GO_REF:0000033). Reason: IFT is required to build cilia; loss of IFT52 function impairs ciliogenesis or cilium structure in model organisms and/or patient cells. IFT52 participates directly as a component of the IFT machinery that delivers axonemal precursors, not merely as an upstream requirement. Supporting Evidence: PMID:27466190 These data demonstrate that IFT52 is essential for anterograde complex integrity and for the biosynthesis and maintenance of cilia.
GO:0060271 cilium assembly	IMP PMID:27466190 IFT52 mutations destabilize anterograde complex assembly, di...	ACCEPT	Summary: Involved in cilium assembly (IMP, PMID:27466190). Reason: IFT is required to build cilia; loss of IFT52 function impairs ciliogenesis or cilium structure in model organisms and/or patient cells. IFT52 participates directly as a component of the IFT machinery that delivers axonemal precursors, not merely as an upstream requirement. Supporting Evidence: PMID:27466190 These data demonstrate that IFT52 is essential for anterograde complex integrity and for the biosynthesis and maintenance of cilia.
GO:0060271 cilium assembly	NAS PMID:26980730 Overall Architecture of the Intraflagellar Transport (IFT)-B...	ACCEPT	Summary: Involved in cilium assembly (NAS, PMID:26980730). Reason: IFT is required to build cilia; loss of IFT52 function impairs ciliogenesis or cilium structure in model organisms and/or patient cells. IFT52 participates directly as a component of the IFT machinery that delivers axonemal precursors, not merely as an upstream requirement. Supporting Evidence: PMID:27466190 These data demonstrate that IFT52 is essential for anterograde complex integrity and for the biosynthesis and maintenance of cilia.
GO:0097542 ciliary tip	IEA GO_REF:0000107	ACCEPT	Summary: Located in ciliary tip (IEA). IFT trains are remodelled at the ciliary tip, where anterograde trains disassemble and retrograde trains assemble. Reason: The ciliary tip is the turnaround compartment of IFT; IFT subunits transiently concentrate there. Correct location reflecting the IFT cycle. Supporting Evidence: Reactome:R-HSA-5625421 anterograde IFT trains are believed to disassemble at the ciliary tip, releasing cargo and the IFT motors.
GO:0097542 ciliary tip	TAS Reactome:R-HSA-5624952	ACCEPT	Summary: Located in ciliary tip (TAS). IFT trains are remodelled at the ciliary tip, where anterograde trains disassemble and retrograde trains assemble. Reason: The ciliary tip is the turnaround compartment of IFT; IFT subunits transiently concentrate there. Correct location reflecting the IFT cycle. Supporting Evidence: Reactome:R-HSA-5624952 Remodelling of IFT trains is thought to occur at the ciliary tip
GO:0097542 ciliary tip	TAS Reactome:R-HSA-5625416	ACCEPT	Summary: Located in ciliary tip (TAS). IFT trains are remodelled at the ciliary tip, where anterograde trains disassemble and retrograde trains assemble. Reason: The ciliary tip is the turnaround compartment of IFT; IFT subunits transiently concentrate there. Correct location reflecting the IFT cycle. Supporting Evidence: Reactome:R-HSA-5625416 Anterograde trains travel along the axoneme of the cilium at an estimated rate of 2 micrometers per second in an ATP- and kinesin-2-dependent fashion
GO:0097542 ciliary tip	TAS Reactome:R-HSA-5625421	ACCEPT	Summary: Located in ciliary tip (TAS). IFT trains are remodelled at the ciliary tip, where anterograde trains disassemble and retrograde trains assemble. Reason: The ciliary tip is the turnaround compartment of IFT; IFT subunits transiently concentrate there. Correct location reflecting the IFT cycle. Supporting Evidence: Reactome:R-HSA-5625421 anterograde IFT trains are believed to disassemble at the ciliary tip, releasing cargo and the IFT motors.
GO:0097542 ciliary tip	TAS Reactome:R-HSA-5625426	ACCEPT	Summary: Located in ciliary tip (TAS). IFT trains are remodelled at the ciliary tip, where anterograde trains disassemble and retrograde trains assemble. Reason: The ciliary tip is the turnaround compartment of IFT; IFT subunits transiently concentrate there. Correct location reflecting the IFT cycle. Supporting Evidence: Reactome:R-HSA-5625426 Retrograde trains are shorter than anterograde particles and travel along the cilliary axoneme at an estimated rate of 3 micrometers per second
GO:0097546 ciliary base	IDA PMID:31637240 SANS (USH1G) Molecularly Links the Human Usher Syndrome Prot...	ACCEPT	Summary: Located at ciliary base (IDA) in mouse photoreceptors. Reason: IFT52 concentrates at the ciliary base where IFT-B trains assemble. Supporting Evidence: PMID:31637240 Quantitative immunofluorescence microscopy revealed the co-localization of SANS with IFT20, IFT52, and IFT57 particularly at ciliary base of wild type mouse photoreceptor cells.
GO:0097546 ciliary base	IEA GO_REF:0000107	ACCEPT	Summary: Located at ciliary base (IEA, GO_REF:0000107). IFT complexes assemble into trains and are loaded at the ciliary base (basal body / transition fibres) before entering the cilium. Reason: A large pool of IFT52 resides at the ciliary base, where IFT trains are assembled and where RABL2-mediated capture of IFT-B occurs; this is a well-documented location for IFT subunits. Supporting Evidence: PMID:28625565 GTP-bound RABL2 then binds to the IFT-B holocomplex via the IFT74/81 heterodimer to capture and trigger the entry of IFT-B into cilia, prior to classical motor-driven intraflagellar transport.
GO:0097733 photoreceptor cell cilium	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: Located in photoreceptor cell cilium (IEA, GO_REF:0000107). Photoreceptor outer segments are modified primary cilia built and maintained by IFT through the connecting cilium. Reason: Correct cell-type-specific ciliary location; retinal degeneration in patients with IFT52 variants is consistent with a requirement for IFT in photoreceptor cilia. Non-core relative to the general IFT role.

Gene Description

Existing Annotations Review

Core Functions

IFT52 is a structural hub of the IFT-B complex that bridges the two IFT-B1 subcomplexes and links IFT-B1 to IFT-B2; it is required for IFT-B integrity, anterograde IFT and ciliogenesis. No specific molecular-function term beyond complex scaffolding is established.

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