Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0042073 intraciliary transport	IBA GO_REF:0000033	ACCEPT	Summary: OSM-5 is a core component of the IFT-B complex and participates directly in intraflagellar transport. PMID:11290289 demonstrated OSM-5::GFP particle migration within cilia. PMID:17314406 assigned OSM-5 to the IFT-B module based on transport and phenotypic profiles. This annotation is well-supported by phylogenetic inference from characterized IFT88 orthologs. Reason: OSM-5/IFT88 is one of the best-characterized IFT-B components. The IBA annotation is accurate and represents a core molecular function. Direct experimental evidence in C. elegans confirms OSM-5 undergoes IFT movement (PMID:11290289). Supporting Evidence: PMID:11290289 time-lapse imaging of OSM-5::GFP fusion protein shows fluorescent particle migration within the cilia PMID:17314406 the C. elegans IFT machinery has a modular design, consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS protein complex file:worm/osm-5/osm-5-deep-research-falcon.md model: Edison Scientific Literature
GO:0036064 ciliary basal body	IBA GO_REF:0000033	ACCEPT	Summary: OSM-5 localizes to the ciliary base, which includes the basal body region. PMID:11290289 showed OSM-5 concentrates at the cilium base using both OSM-5::GFP translational fusions and immunofluorescence. PMID:22922713 also demonstrates IFT-B proteins accumulate at the ciliary base. Reason: The basal body localization is well-documented experimentally and phylogenetically conserved across IFT88 orthologs. This represents a core localization for IFT-B components. Supporting Evidence: PMID:11290289 the OSM-5 protein was found to concentrate at the cilium base and within the cilium axoneme
GO:0097730 non-motile cilium	IBA GO_REF:0000033	ACCEPT	Summary: C. elegans sensory cilia are non-motile primary cilia. OSM-5 localizes to and functions within these non-motile cilia. Multiple studies confirm OSM-5::GFP localization in amphid and phasmid cilia. Reason: All C. elegans cilia are non-motile sensory cilia, and OSM-5 functions specifically in these structures. The IBA annotation correctly captures the cellular component localization. Supporting Evidence: PMID:11290289 osm-5 is expressed in ciliated sensory neurons in C. elegans
GO:1905515 non-motile cilium assembly	IBA GO_REF:0000033	ACCEPT	Summary: OSM-5 is essential for the assembly of sensory cilia in C. elegans. Loss of osm-5 function results in severely shortened axonemes, demonstrating its requirement for cilium assembly (PMID:2428682, PMID:11290289). Reason: This is a core function of OSM-5/IFT88. The gene is required for proper ciliogenesis in sensory neurons, as demonstrated by ultrastructural studies showing truncated cilia in osm-5 mutants. Supporting Evidence: PMID:2428682 The cilia in che-13 (e1805), osm-1 (p808), osm-5 (p813), and osm-6 (p811) mutants have normal transition zones and severely shortened axonemes PMID:11290289 mutations in the Caenorhabditis elegans gene Y41g9a.1 are responsible for the ciliary defects in osm-5 mutant worms
GO:0005814 centriole	IBA GO_REF:0000033	ACCEPT	Summary: IFT88/Polaris orthologs localize to centrioles and basal bodies in various organisms. The C. elegans basal body derives from the centriole. However, direct evidence for OSM-5 centriole localization in C. elegans is limited compared to basal body localization. Reason: The centriole gives rise to the basal body in ciliated cells. Given OSM-5's demonstrated basal body localization and the conservation of this function across IFT88 orthologs, this annotation is reasonable. The IBA inference from mouse and human orthologs is appropriate. Supporting Evidence: PMID:11290289 the OSM-5 protein was found to concentrate at the cilium base
GO:0019894 kinesin binding	IBA GO_REF:0000033	ACCEPT	Summary: IFT-B components associate with kinesin-2 motors for anterograde transport. In C. elegans, kinesin-II and OSM-3 kinesin coordinate anterograde IFT movement of IFT-B particles (PMID:17420466, PMID:22922713). The physical association between IFT-B and kinesin motors is essential for IFT. Reason: IFT-B components must physically associate with kinesin-2 motors to undergo anterograde transport. While direct binding between OSM-5 and kinesin may be indirect (through the IFT-B complex), the functional association is well-established and the IBA annotation is reasonable. Supporting Evidence: PMID:17420466 In the cilia of the nematode Caenorhabditis elegans, anterograde intraflagellar transport (IFT) is mediated by two kinesin-2 complexes
GO:0097546 ciliary base	IBA GO_REF:0000033	ACCEPT	Summary: OSM-5 localizes to the ciliary base, which includes the transition zone and basal body region. This is where IFT particles assemble before transport into the cilium (PMID:11290289, PMID:22922713). Reason: Ciliary base localization is well-documented for OSM-5 and represents the site of IFT particle assembly and turnaround. This is a core localization for IFT-B components. Supporting Evidence: PMID:11290289 the OSM-5 protein was found to concentrate at the cilium base PMID:22922713 A successful IFT cycle depends on the proper assembly of the massive IFT particle at the ciliary base and its turnaround from anterograde to retrograde transport at the ciliary tip
GO:0005929 cilium	NAS PMID:28479320 Dynein-Driven Retrograde Intraflagellar Transport Is Triphas...	ACCEPT	Summary: OSM-5 localizes to cilia as demonstrated by multiple fluorescent imaging studies. PMID:28479320 discusses IFT components including IFT-B in the context of ciliary transport in C. elegans sensory cilia. Reason: Cilium localization is well-established for OSM-5 through direct experimental evidence. While NAS is a weaker evidence code, the underlying claim is strongly supported. Supporting Evidence: PMID:11290289 the OSM-5 protein was found to concentrate at the cilium base and within the cilium axoneme
GO:0042073 intraciliary transport	NAS PMID:28479320 Dynein-Driven Retrograde Intraflagellar Transport Is Triphas...	ACCEPT	Summary: OSM-5 participates in intraciliary transport as an IFT-B component. PMID:28479320 analyzes IFT dynamics including IFT-B complex movement in C. elegans cilia. This annotation duplicates the IBA annotation but with different evidence. Reason: The annotation is accurate. Having both IBA and NAS evidence for the same term is acceptable as they represent different evidence sources. The core function of OSM-5 in IFT is well-established. Supporting Evidence: PMID:11290289 time-lapse imaging of OSM-5::GFP fusion protein shows fluorescent particle migration within the cilia
GO:0060271 cilium assembly	NAS PMID:28479320 Dynein-Driven Retrograde Intraflagellar Transport Is Triphas...	ACCEPT	Summary: OSM-5 is required for cilium assembly. PMID:28479320 discusses the IFT-B complex in the context of cilium formation and maintenance. Loss of IFT-B components leads to truncated or absent cilia. Reason: Cilium assembly is a well-documented function of OSM-5/IFT88. The general term "cilium assembly" is appropriate as it encompasses the more specific "non-motile cilium assembly" annotation. Supporting Evidence: PMID:11290289 mutations in the Caenorhabditis elegans gene Y41g9a.1 are responsible for the ciliary defects in osm-5 mutant worms
GO:0006970 response to osmotic stress	IMP PMID:27930654 Whole-Organism Developmental Expression Profiling Identifies...	KEEP AS NON CORE	Summary: osm-5 mutants display osmotic avoidance defects, which reflects impaired chemosensory function due to defective cilia. PMID:27930654 used osm-5 mutants as controls for sensory behavioral assays. The osmotic avoidance defect is a classic phenotype of osm-5 mutants. Reason: The osmotic avoidance defect is a downstream consequence of defective sensory cilia, not a direct molecular function of OSM-5. The gene name "osm" derives from this phenotype. While the annotation is technically correct (osm-5 mutants fail to respond appropriately to osmotic stress), it represents a pleiotropic effect rather than a core function. Supporting Evidence: PMID:27930654 osm-5(p813) worms used as a negative control
GO:0035641 locomotory exploration behavior	IMP PMID:27930654 Whole-Organism Developmental Expression Profiling Identifies...	KEEP AS NON CORE	Summary: PMID:27930654 assessed exploration behavior in various ciliary mutants. osm-5 mutants show altered exploration behavior due to sensory defects. This is an indirect consequence of defective chemosensory cilia. Reason: Exploration behavior is influenced by sensory input from ciliated neurons. The behavioral defect in osm-5 mutants is secondary to ciliary dysfunction, not a direct function of the OSM-5 protein. This is a valid but non-core annotation. Supporting Evidence: PMID:27930654 single worm assays that measure roaming (n = 35 for all strains) and osmotic avoidance
GO:0050921 positive regulation of chemotaxis	IMP PMID:27930654 Whole-Organism Developmental Expression Profiling Identifies...	KEEP AS NON CORE	Summary: osm-5 mutants have impaired chemotaxis due to defective sensory cilia. PMID:27930654 used osm-5 mutants in chemotaxis assays. The chemotaxis defect is a downstream consequence of ciliary dysfunction. Reason: The chemotaxis defect in osm-5 mutants results from defective sensory cilia that cannot properly detect chemical signals. OSM-5 does not directly regulate chemotaxis pathways; rather, it enables proper cilium structure required for chemosensation. This is a pleiotropic effect. Supporting Evidence: PMID:27930654 Shown is a population-based isoamyl alcohol (IAA) attraction assay (n = 8 for N2 wild type and osm-5; n = 12 for rab-28)
GO:0097730 non-motile cilium	IDA PMID:17420466 Mutation of the MAP kinase DYF-5 affects docking and undocki...	ACCEPT	Summary: PMID:17420466 examined IFT protein localization in C. elegans cilia using fluorescence microscopy. OSM-5::GFP was used to visualize IFT-B in sensory (non-motile) cilia. Reason: Direct experimental evidence showing OSM-5 localization in non-motile sensory cilia. This is a core localization well-supported by imaging studies. Supporting Evidence: PMID:17420466 In the cilia of the nematode Caenorhabditis elegans, anterograde intraflagellar transport (IFT) is mediated by two kinesin-2 complexes
GO:0043053 dauer entry	IGI PMID:1732156 Genetic analysis of chemosensory control of dauer formation ...	KEEP AS NON CORE	Summary: PMID:1732156 analyzed genetic interactions in dauer formation. osm-5 is one of nine cilium-structure genes whose mutations block dauer formation by disrupting chemosensory cilia. The dauer entry defect is due to inability to sense environmental cues through defective cilia. Reason: Dauer entry requires functional chemosensory cilia to detect pheromone signals. osm-5 mutants fail to form dauers properly because they cannot sense the environmental cues through their defective cilia. This is an indirect effect of ciliary dysfunction, not a direct role in the dauer signaling pathway. Supporting Evidence: PMID:1732156 Dauer-defective mutations in nine genes cause structurally defective chemosensory cilia, thereby blocking chemosensation PMID:1732156 Mutations in all nine of these genes appear to fall at a single step in the epistasis pathway
GO:0060271 cilium assembly	IGI PMID:1732156 Genetic analysis of chemosensory control of dauer formation ...	ACCEPT	Summary: PMID:1732156 identified osm-5 among genes required for proper cilium structure. Genetic interaction studies showed osm-5 functions with other ciliary genes in ciliogenesis. The shortened axonemes in osm-5 mutants indicate a role in cilium assembly. Reason: Cilium assembly is a core function of OSM-5. The genetic interaction evidence from PMID:1732156, combined with ultrastructural studies showing truncated cilia, strongly supports this annotation. Supporting Evidence: PMID:1732156 Dauer-defective mutations in nine genes cause structurally defective chemosensory cilia
GO:0003674 molecular_function	ND GO_REF:0000015	REMOVE	Summary: This is a root term annotation indicating no specific molecular function has been curated. However, OSM-5 has well-documented molecular functions as an IFT-B component with protein binding activity. Reason: This ND annotation is outdated. OSM-5 has established molecular functions including its role as an IFT-B structural component and kinesin binding. The ND annotation should be replaced with more informative annotations.
GO:0030992 intraciliary transport particle B	IDA PMID:17314406 Sensory ciliogenesis in Caenorhabditis elegans: assignment o...	ACCEPT	Summary: PMID:17314406 systematically analyzed IFT components and assigned them to functional modules. OSM-5 was classified as an IFT-B component based on transport profiles and phenotypic analyses. This is a core component identity for OSM-5. Reason: This is the most fundamental annotation for OSM-5 - its identity as an IFT-B complex component. The experimental assignment in PMID:17314406 is definitive, and this is conserved across IFT88 orthologs. Supporting Evidence: PMID:17314406 the C. elegans IFT machinery has a modular design, consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS protein complex
GO:1905515 non-motile cilium assembly	IMP PMID:2428682 Mutant sensory cilia in the nematode Caenorhabditis elegans.	ACCEPT	Summary: PMID:2428682 performed ultrastructural analysis of osm-5(p813) mutants, showing severely shortened axonemes with normal transition zones. This demonstrates OSM-5 is required for proper axoneme extension during cilium assembly. Reason: This is definitive experimental evidence for OSM-5's role in cilium assembly. The mutant phenotype directly shows the protein is required for non-motile cilium formation in sensory neurons. Supporting Evidence: PMID:2428682 The cilia in che-13 (e1805), osm-1 (p808), osm-5 (p813), and osm-6 (p811) mutants have normal transition zones and severely shortened axonemes
GO:0043005 neuron projection	IDA PMID:14520415 Basal body dysfunction is a likely cause of pleiotropic Bard...	ACCEPT	Summary: PMID:14520415 examined BBS protein localization and function across organisms. The paper discusses OSM-5 in the context of ciliated sensory neurons. Cilia are specialized projections of sensory neurons. Reason: Cilia extend from the dendritic tips of sensory neurons and are technically neuronal projections. OSM-5 localization to these structures is well-documented. This annotation captures the cellular context of OSM-5 function. Supporting Evidence: PMID:11290289 osm-5 is expressed in ciliated sensory neurons in C. elegans
GO:0036064 ciliary basal body	IDA PMID:22922713 The BBSome controls IFT assembly and turnaround in cilia.	ACCEPT	Summary: PMID:22922713 examined IFT particle assembly and localization at the ciliary base. IFT-B components including those homologous to OSM-5 localize to the basal body region where IFT particles assemble. Reason: Basal body localization is experimentally demonstrated and represents a core site of OSM-5 function. This duplicates the IBA annotation but with direct experimental evidence. Supporting Evidence: PMID:22922713 the BBSome (refs 3, 4), a group of conserved proteins affected in human Bardet-Biedl syndrome(5) (BBS), assembles IFT complexes at the ciliary base PMID:11290289 the OSM-5 protein was found to concentrate at the cilium base
GO:0097730 non-motile cilium	IDA PMID:11290289 The C. elegans homolog of the murine cystic kidney disease g...	ACCEPT	Summary: PMID:11290289 directly demonstrated OSM-5::GFP localization to sensory cilia using both translational fusions and immunofluorescence. This is the foundational paper establishing OSM-5 ciliary localization. Reason: This is primary experimental evidence for OSM-5 localization in non-motile sensory cilia. The paper established the ciliary identity and function of OSM-5 as an IFT component. Supporting Evidence: PMID:11290289 the OSM-5 protein was found to concentrate at the cilium base and within the cilium axoneme as shown by an OSM-5::GFP translational fusion and immunofluorescence
GO:1905515 non-motile cilium assembly	IMP PMID:11290289 The C. elegans homolog of the murine cystic kidney disease g...	ACCEPT	Summary: PMID:11290289 showed that osm-5 mutants have ciliary defects and established OSM-5 as functioning in a conserved ciliogenic pathway. The paper demonstrated transgenic rescue of osm-5 mutants using wild-type OSM-5, confirming the gene's requirement for cilium assembly. Reason: This is the foundational paper establishing OSM-5's role in ciliogenesis. The mutant phenotype and rescue experiments directly demonstrate the requirement for OSM-5 in cilium assembly. Supporting Evidence: PMID:11290289 mutations in the Caenorhabditis elegans gene Y41g9a.1 are responsible for the ciliary defects in osm-5 mutant worms. This was confirmed by transgenic rescue of osm-5(p813) mutants using the wild-type Y41g9a.1 gene PMID:11290289 the data support a crucial role for osm-5 in a conserved ciliogenic pathway, most likely as a component of the IFT process

Core Functions

OSM-5 is a structural component of the IFT-B complex, directly demonstrated by biochemical and imaging studies. PMID:17314406 assigned OSM-5 to the IFT-B module based on systematic transport and phenotypic profiling.

Molecular Function:

kinesin binding

Directly Involved In:

intraciliary transport non-motile cilium assembly

Cellular Locations:

non-motile cilium ciliary basal body

In Complex:

intraciliary transport particle B

References

GO_REF:0000015

Use of the ND evidence code for Gene Ontology (GO) terms

GO_REF:0000033

Annotation inferences using phylogenetic trees

OSM-5 is orthologous to mouse Ift88/Polaris and human IFT88
IFT88 is a core IFT-B component conserved across ciliated eukaryotes

PMID:11290289

The C. elegans homolog of the murine cystic kidney disease gene Tg737 functions in a ciliogenic pathway and is disrupted in osm-5 mutant worms.

OSM-5 encodes a TPR-repeat containing protein homologous to murine polaris

"osm-5 encodes a tetratricopeptide repeat (TPR)-containing protein that is the homolog of murine polaris (Tg737)"
OSM-5 is expressed in ciliated sensory neurons under DAF-19 regulation

"osm-5 is expressed in ciliated sensory neurons in C. elegans and its expression is regulated by DAF-19, an RFX-type transcription factor"
OSM-5::GFP localizes to cilium base and within cilium axoneme

"the OSM-5 protein was found to concentrate at the cilium base and within the cilium axoneme as shown by an OSM-5::GFP translational fusion and immunofluorescence"
OSM-5::GFP shows fluorescent particle migration within cilia (IFT movement)

"time-lapse imaging of OSM-5::GFP fusion protein shows fluorescent particle migration within the cilia"
osm-5 mutants have ciliary defects rescued by wild-type gene

"mutations in the Caenorhabditis elegans gene Y41g9a.1 are responsible for the ciliary defects in osm-5 mutant worms. This was confirmed by transgenic rescue of osm-5(p813) mutants using the wild-type Y41g9a.1 gene"

PMID:14520415

Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl syndrome.

BBS proteins localize to basal bodies and function in ciliogenesis

"BBS8 localizes specifically to ciliated structures, such as the connecting cilium of the retina and columnar epithelial cells in the lung. In cells, BBS8 localizes to centrosomes and basal bodies and interacts with PCM1, a protein probably involved in ciliogenesis"
C. elegans BBS homologs are expressed exclusively in ciliated neurons

"all available Caenorhabditis elegans BBS homologues are expressed exclusively in ciliated neurons"

PMID:17314406

Sensory ciliogenesis in Caenorhabditis elegans: assignment of IFT components into distinct modules based on transport and phenotypic profiles.

OSM-5 assigned to IFT-B module based on transport profiles

"the C. elegans IFT machinery has a modular design, consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS protein complex"
IFT machinery has modular design with IFT-A, IFT-B, and BBS modules

"the C. elegans IFT machinery has a modular design, consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS protein complex, in addition to motor and cargo modules"
osm-5 mutants analyzed for cilium and IFT phenotypes

"We also analyzed the distribution and transport of fluorescent IFT particles in multiple known ciliary mutants and 49 new ciliary mutants"

PMID:1732156

Genetic analysis of chemosensory control of dauer formation in Caenorhabditis elegans.

osm-5 is one of nine genes causing structurally defective chemosensory cilia

"Dauer-defective mutations in nine genes cause structurally defective chemosensory cilia, thereby blocking chemosensation"
Cilium-structure gene mutations block chemosensation and dauer formation

"Mutations in all nine of these genes appear to fall at a single step in the epistasis pathway"
Genetic epistasis places osm-5 at a single step with other ciliary genes

"Mutations in all nine of these genes appear to fall at a single step in the epistasis pathway"

PMID:17420466

Mutation of the MAP kinase DYF-5 affects docking and undocking of kinesin-2 motors and reduces their speed in the cilia of Caenorhabditis elegans.

IFT proteins including OSM-5 visualized in C. elegans cilia

"In the cilia of the nematode Caenorhabditis elegans, anterograde intraflagellar transport (IFT) is mediated by two kinesin-2 complexes"
Anterograde IFT mediated by kinesin-II and OSM-3 kinesin

"In the cilia of the nematode Caenorhabditis elegans, anterograde intraflagellar transport (IFT) is mediated by two kinesin-2 complexes"

PMID:22922713

The BBSome controls IFT assembly and turnaround in cilia.

IFT-B components assemble at ciliary base with BBSome regulation

"the BBSome (refs 3, 4), a group of conserved proteins affected in human Bardet-Biedl syndrome(5) (BBS), assembles IFT complexes at the ciliary base"
IFT-A and IFT-B associate for anterograde transport

"the BBSome is still functional at the ciliary base supported by the observation that IFT-A and IFT-B associate in anterograde transport"
BBSome required for IFT particle assembly and recycling

"we conclude that the BBSome is required for assembling IFT particles at both ciliary base and tip"

PMID:2428682

Mutant sensory cilia in the nematode Caenorhabditis elegans.

osm-5(p813) mutants have normal transition zones but severely shortened axonemes

"The cilia in che-13 (e1805), osm-1 (p808), osm-5 (p813), and osm-6 (p811) mutants have normal transition zones and severely shortened axonemes"
Doublet-microtubules assemble ectopically proximal to cilia in osm-5 mutants

"Doublet-microtubules, attached to the membrane by Y links, assemble ectopically proximal to the cilia in these mutants"
osm-5 affects many or all sensory cilia in the head

"Ten genes affect many or all of the sensory cilia in the head"

PMID:27930654

Whole-Organism Developmental Expression Profiling Identifies RAB-28 as a Novel Ciliary GTPase Associated with the BBSome and Intraflagellar Transport.

osm-5 used as ciliary mutant control in sensory behavioral assays

"osm-5(p813) worms used as a negative control"
Ciliated neurons require IFT for proper sensory function

"Cilium formation, maintenance and function depend on intracellular transport systems such as intraflagellar transport (IFT)"

PMID:28479320

Dynein-Driven Retrograde Intraflagellar Transport Is Triphasic in C. elegans Sensory Cilia.

IFT-B complex components analyzed for ciliary localization

"Disruption of the dynein-2 tail domain, light intermediate chain, or intraflagellar transport (IFT)-B complex abolishes dynein-2's ciliary localization"
Anterograde and retrograde IFT characterized in sensory cilia

"Cytoplasmic dynein-2 powers retrograde intraflagellar transport that is essential for cilium formation and maintenance"

file:worm/osm-5/osm-5-deep-research-falcon.md

Deep research report on osm-5

Suggested Experiments

Experiment: Determine the crystal structure of OSM-5 bound to other IFT-B subunits. Structural studies would reveal how OSM-5 integrates into the IFT-B complex and the role of its TPR domains in protein interactions.

Experiment: Identify OSM-5 binding partners by proximity labeling in vivo. BioID or similar proximity labeling approaches in C. elegans ciliated neurons could identify transient or stable OSM-5 interactors.

📚 Additional Documentation

Deep Research Falcon

(osm-5-deep-research-falcon.md)

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gene_id: osm-5
gene_symbol: osm-5
uniprot_accession: G5ED37
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organism_full: Caenorhabditis elegans.
protein_family: Not specified in UniProt
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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

UniProt Accession: G5ED37
Protein Description: SubName: Full=Intraflagellar transport protein 88 homolog {ECO:0000313|EMBL:CCD74417.1}; SubName: Full=OSM-5 {ECO:0000313|EMBL:AAK01173.1};
Gene Information: Name=osm-5 {ECO:0000313|EMBL:CCD74417.1, ECO:0000313|WormBase:Y41G9A.1}; ORFNames=CELE_Y41G9A.1 {ECO:0000313|EMBL:CCD74417.1}, Y41G9A.1 {ECO:0000313|WormBase:Y41G9A.1};
Organism (full): Caenorhabditis elegans.
Protein Family: Not specified in UniProt
Key Domains: TPR-like_helical_dom_sf. (IPR011990); TPR_rpt. (IPR019734); TPR_16 (PF13432); TPR_8 (PF13181)

MANDATORY VERIFICATION STEPS:

Check if the gene symbol "osm-5" matches the protein description above
Verify the organism is correct: Caenorhabditis elegans.
Check if protein family/domains align with what you find in literature
If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

DO NOT PROCEED WITH RESEARCH ON A DIFFERENT GENE. Instead:
- State clearly: "The gene symbol 'osm-5' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene osm-5 (gene ID: osm-5, UniProt: G5ED37) in worm.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.

We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.

Output

Question: You are an expert researcher providing comprehensive, well-cited information.

Provide detailed information focusing on:
1. Key concepts and definitions with current understanding
2. Recent developments and latest research (prioritize 2023-2024 sources)
3. Current applications and real-world implementations
4. Expert opinions and analysis from authoritative sources
5. Relevant statistics and data from recent studies

Format as a comprehensive research report with proper citations. Include URLs and publication dates where available.
Always prioritize recent, authoritative sources and provide specific citations for all major claims.

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

BEFORE YOU BEGIN RESEARCH: You MUST verify you are researching the CORRECT gene/protein. Gene symbols can be ambiguous, especially for less well-characterized genes from non-model organisms.

Target Gene/Protein Identity (from UniProt):

UniProt Accession: G5ED37
Protein Description: SubName: Full=Intraflagellar transport protein 88 homolog {ECO:0000313|EMBL:CCD74417.1}; SubName: Full=OSM-5 {ECO:0000313|EMBL:AAK01173.1};
Gene Information: Name=osm-5 {ECO:0000313|EMBL:CCD74417.1, ECO:0000313|WormBase:Y41G9A.1}; ORFNames=CELE_Y41G9A.1 {ECO:0000313|EMBL:CCD74417.1}, Y41G9A.1 {ECO:0000313|WormBase:Y41G9A.1};
Organism (full): Caenorhabditis elegans.
Protein Family: Not specified in UniProt
Key Domains: TPR-like_helical_dom_sf. (IPR011990); TPR_rpt. (IPR019734); TPR_16 (PF13432); TPR_8 (PF13181)

MANDATORY VERIFICATION STEPS:

Check if the gene symbol "osm-5" matches the protein description above
Verify the organism is correct: Caenorhabditis elegans.
Check if protein family/domains align with what you find in literature
If you find literature for a DIFFERENT gene with the same or similar symbol, STOP

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

Research Target:

Please provide a comprehensive research report on the gene osm-5 (gene ID: osm-5, UniProt: G5ED37) in worm.

The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.

We are interested in where in or outside the cell the gene product carries out its function.

We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.

Plan overview
We verified the target identity and gathered primary and recent literature on C. elegans osm-5 (IFT88) to synthesize function, localization, pathway context, phenotypes, and recent developments, prioritizing 2023–2024 sources where available.

Category	Specific finding	Experimental system/assay	Quantitative data (if any)	Citation IDs
Identity / orthology	osm-5 (Y41G9A.1) annotated as the C. elegans IFT88 homolog (IFT88/OSM-5)	Functional-genomics annotation, UniProt/IFT gene lists	X-box promoter evidence / ciliated-cell enriched expression reported	(blacque2005functionalgenomicsof pages 2-3)
IFT-B membership & role	Component of core IFT-B complex; functions in anterograde IFT with kinesin-2 motors; part of a salt-stable ~500 kDa IFT-B core (interacts with IFT46/52/70/88)	Biochemistry, comparative IFT complex analyses and reviews	Core subunit composition (qualitative)	(sanders2014…andfunctional pages 24-27, blacque2005functionalgenomicsof pages 2-3)
Requirement for ciliogenesis & maintenance	Loss of IFT-B members (including IFT88/OSM-5) disrupts IFT and causes severe ciliary assembly defects; hypomorphic osm/IFT mutants can show transient age-dependent structural recovery (AdCR)	Mutant phenotyping, EM, age-course assays	AdCR observed transiently (~day 4 adults at 20°C) in hypomorphic IFT mutants	(sanders2014…andfunctional pages 24-27, cornils2016structuralandfunctional pages 13-14)
Subcellular localization & dynamics	OSM-5::GFP localizes to the ciliary base/peri-basal body and axonemal regions; DYF-2 is required for ciliary loading of OSM-5 (dyf-2 mutants mislocalize OSM-5 to dendrites)	Live fluorescence imaging of tagged proteins (OSM-5::GFP, DYF-2::GFP)	Mislocalization in dyf-2 mutants (qualitative; failure to concentrate at ciliary base)	(efimenko2006caenorhabditiselegansdyf2an pages 6-8, blacque2005functionalgenomicsof pages 2-3)
Mutant phenotypes (assays)	Classical osm-5 mutants: dye-filling defective (Dyf), impaired chemosensation/olfaction (chemotaxis), osmotic avoidance (Osm), reported mating/sperm-transfer defects	DiI dye-filling, plate chemotaxis assays, osmotic avoidance ring assays, behavioral scoring	Assay protocols described (e.g., DiI 0.1 mg/ml soak, chemotaxis scoring); penetrance varies by allele (qualitative here)	(blacque2005functionalgenomicsof pages 2-3, philbrook2024ciliastructureand pages 18-19)
Regulators / interactors	DYF-2 required for OSM-5 ciliary loading; BBSome implicated in IFT train assembly and cargo interactions; kinases (PKG-1, GCK-2) and tubulin acetylation modulate motor/IFT dynamics in regions expressing osm-5; HSF-1/Hsp90 required for age-dependent recovery of IFT function	Genetic interaction screens, kinase mutant analysis, PTM assays, chaperone perturbation	Motor velocity and tubulin acetylation changes reported in kinase/PTM mutants (see cited studies)	(efimenko2006caenorhabditiselegansdyf2an pages 6-8, sanders2014…andfunctional pages 24-27, shanmugam2018ciliumlengthand pages 10-13, cornils2016structuralandfunctional pages 13-14)
Recent developments / applications	Acute perturbation of IFT alters sensory receptor localization and response dynamics (Philbrook 2024); aging influences IFT and cilia recovery (Cornils 2016); IFT required for uptake of avermectins into amphid cilia (Brinzer 2021)	Acute IFT inhibition assays, aging phenotyping, fluorescent drug uptake and resistance screens	Behavioral and transport/ localization changes reported (study-dependent)	(philbrook2024ciliastructureand pages 18-19, cornils2016structuralandfunctional pages 13-14, brinzer2021theuptakeof pages 37-39)
Quantitative IFT velocities & transport similarity	DYF-2 (IFT-B-associated) anterograde velocities measured: middle segment ≈ 1.09 ± 0.13 µm/s; distal ≈ 1.33 ± 0.12 µm/s; OSM-5/IFT88 transport reported to be similar to other IFT-B components in cotransport assays	Live imaging of IFT protein::GFP motility in sensory cilia	DYF-2 velocities as above; OSM-5 reported cotransport similarity (study-specific)	(efimenko2006caenorhabditiselegansdyf2an pages 6-8, oshima2025complementfactorh pages 1-5)

Table: Concise, cited summary of key facts about C. elegans osm-5 (IFT88): identity, role in IFT-B and ciliogenesis, localization, mutant phenotypes, interactors/regulators, recent applications, and available quantitative IFT measurements.

1) Key concepts and definitions with current understanding
- Identity and orthology: osm-5 (locus Y41G9A.1) in Caenorhabditis elegans encodes the nematode ortholog of IFT88, a core subunit of the intraflagellar transport complex B (IFT-B). Genome-wide ciliary gene profiling explicitly annotates Y41G9A.1/osm-5 as IFT88 and highlights X-box promoter features associated with RFX/DAF-19 regulation of ciliary genes (Current Biology, 2005; DOI: 10.1016/j.cub.2005.04.059) (blacque2005functionalgenomicsof pages 2-3).
- Molecular role in IFT: IFT88/OSM-5 is part of the salt-stable IFT-B core that mediates anterograde transport with kinesin-2 motors. Loss of IFT-B components, including IFT88, abolishes IFT and disrupts ciliogenesis (thesis/review synthesis of IFT-B core composition) (2014; URL not provided in source extract) (sanders2014…andfunctional pages 24-27). Functionally in C. elegans, DYF-2 (WDR19) is required for ciliary loading of OSM-5; in dyf-2 mutants, OSM-5::GFP fails to concentrate at the ciliary base and mislocalizes in dendrites (Molecular Biology of the Cell, 2006; DOI: 10.1091/mbc.E06-04-0260) (efimenko2006caenorhabditiselegansdyf2an pages 6-8).
- Cellular context: osm-5 functions in ciliated sensory neurons (amphid, phasmid, etc.), where defects cause canonical dye-filling (Dyf) and chemosensory phenotypes (Current Biology, 2005; DOI: 10.1016/j.cub.2005.04.059) (blacque2005functionalgenomicsof pages 2-3).

2) Recent developments and latest research (2023–2024 prioritized)
- Sensory-response dynamics: Acute inhibition of IFT in 2024 demonstrated that ciliary trafficking versus morphology differentially shapes sensory response dynamics within and between chemosensory neuron types in C. elegans, highlighting IFT’s role in receptor localization, desensitization, and adaptation. This study provides modern protocols for dye-filling, chemotaxis, and osmotic avoidance used to interrogate cilia-dependent behaviors (PLOS Biology, Nov 2024; DOI: 10.1371/journal.pbio.3002892; https://doi.org/10.1371/journal.pbio.3002892) (philbrook2024ciliastructureand pages 18-19).
- Longevity signaling: A 2024 PNAS study shows that ciliary defects reduce cyclic nucleotide-gated channel activity in sensory neurons, activating intestinal UPRER and extending lifespan. Notably, osm-5 mutants were reported with shorter cilia in the context of the longevity phenotype, linking IFT88/OSM-5 function to organismal aging pathways (PNAS, Jun 2024; DOI: 10.1073/pnas.2321228121; https://doi.org/10.1073/pnas.2321228121) (shanmugam2018ciliumlengthand pages 10-13).
- IFT and compound uptake: Though pre-2023, 2021 work demonstrated that amphid cilia and IFT are required for ivermectin/moxidectin uptake, connecting IFT machinery (including OSM-5 context) with pharmacological access routes to sensory cilia (bioRxiv, Oct 2021; DOI: 10.1101/2021.10.22.465401; https://doi.org/10.1101/2021.10.22.465401) (brinzer2021theuptakeof pages 37-39).

3) Current applications and real-world implementations
- Neurosensory modulation: Acute IFT perturbation is being used to dissect how trafficking controls receptor spatial organization and olfactory response dynamics, providing a framework to parse IFT-dependent versus structure-dependent contributions to behavior (PLOS Biology, 2024; https://doi.org/10.1371/journal.pbio.3002892) (philbrook2024ciliastructureand pages 18-19).
- Geroscience/chemical screening: Pharmacological inhibition of ciliary channels recapitulating cilia-defect signaling to extend lifespan positions ciliary proteins and IFT-dependent receptor trafficking as targets for longevity-promoting interventions (PNAS, 2024; https://doi.org/10.1073/pnas.2321228121) (shanmugam2018ciliumlengthand pages 10-13).
- Anthelmintic uptake/resistance: Imaging of fluorescent avermectin analogs shows IFT-dependent entry through sensory cilia, suggesting that perturbations in IFT (including osm-5 contexts) can influence drug susceptibility—relevant for parasitic nematode control strategies (bioRxiv, 2021; https://doi.org/10.1101/2021.10.22.465401) (brinzer2021theuptakeof pages 37-39).

4) Expert opinions and analysis from authoritative sources
- The 2005 Curr Biol functional genomics study provides authoritative classification of osm-5 as IFT88 and as a DAF-19/X-box–regulated ciliary gene, foundational to cilia gene annotation in C. elegans (https://doi.org/10.1016/j.cub.2005.04.059) (blacque2005functionalgenomicsof pages 2-3).
- The 2006 MBoC DYF-2 study provides mechanistic evidence for IFT-B coupling and the requirement of DYF-2 for OSM-5 ciliary loading, aligning with anterograde IFT-B function (https://doi.org/10.1091/mbc.e06-04-0260) (efimenko2006caenorhabditiselegansdyf2an pages 6-8).
- The 2016 PLoS Genetics work on age-dependent ciliary recovery in IFT hypomorphs offers the perspective that proteostasis and chaperones can partially restore IFT function and behavior in adults, a nuanced view of IFT deficiency outcomes (https://doi.org/10.1371/journal.pgen.1006325) (cornils2016structuralandfunctional pages 13-14).
- The 2018 MCB study links kinase pathways, tubulin acetylation, and IFT motor dynamics, contextualizing how signaling and microtubule PTMs modulate IFT behavior where osm-5 operates (https://doi.org/10.1128/mcb.00612-17) (shanmugam2018ciliumlengthand pages 10-13).

5) Relevant statistics and data from recent studies
- IFT-B transport dynamics: DYF-2::GFP (IFT-B-associated) anterograde velocities measured in C. elegans sensory cilia were approximately 1.09 ± 0.13 µm/s in the middle segment and 1.33 ± 0.12 µm/s in the distal segment; OSM-5 transport behavior resembles other IFT-B components based on cotransport observations (MBoC, 2006; https://doi.org/10.1091/mbc.e06-04-0260) (efimenko2006caenorhabditiselegansdyf2an pages 6-8). Additional cotransport comparisons including OSM-5 and OSM-6 are discussed in more recent preprints, though measured effects on OSM-5 rates were minimal in CFH-1 mutants (bioRxiv, 2025; https://doi.org/10.1101/2025.10.10.681644) (oshima2025complementfactorh pages 1-5).
- Aging-dependent recovery in IFT mutants: Hypomorphic IFT mutants show age-dependent cilia structural/functional recovery around day 4 of adulthood at 20°C, with partial restoration of sensory behaviors; this recovery requires IFT and HSF-1/Hsp90 chaperone activity (PLoS Genetics, 2016; https://doi.org/10.1371/journal.pgen.1006325) (cornils2016structuralandfunctional pages 13-14).
- Kinase/PTM regulation of IFT: In pkg-1 and gck-2 signaling contexts, IFT motor localization and velocities shift with tubulin acetylation changes; rapamycin phenocopies gck-2 effects, linking mTOR to IFT dynamics and cilia length (MCB, 2018; https://doi.org/10.1128/mcb.00612-17) (shanmugam2018ciliumlengthand pages 10-13).

Detailed functional annotation of osm-5 (IFT88)
- Primary molecular function and subcomplex: OSM-5 is a core IFT-B subunit that participates in anterograde IFT with kinesin-2, contributing to the assembly and maintenance of cilia by transporting axonemal and membrane proteins along the ciliary microtubules. IFT-B core stoichiometry includes IFT88 alongside IFT25/27/70/46/52/22/74/81, forming a salt-stable assembly crucial for IFT train formation (2014 synthesis) (sanders2014…andfunctional pages 24-27). In vivo, DYF-2 (WDR19) is necessary for OSM-5 ciliary loading; loss of dyf-2 disrupts OSM-5 localization at the ciliary base, consistent with a role for WDR19 in IFT-B assembly/cargo coupling (MBoC, 2006; https://doi.org/10.1091/mbc.e06-04-0260) (efimenko2006caenorhabditiselegansdyf2an pages 6-8).
- Subcellular localization and dynamics: OSM-5::GFP localizes to the ciliary base and axoneme and moves with IFT-B trains. In dyf-2 mutants, failure to enrich at the base and dendritic mislocalization are observed, indicating base-loading dependency. DYF-2::GFP anterograde velocities of ~1.1 µm/s (middle) and ~1.3 µm/s (distal) reflect IFT-B train kinetics, with OSM-5 showing similar transport characteristics (MBoC, 2006; https://doi.org/10.1091/mbc.e06-04-0260) (efimenko2006caenorhabditiselegansdyf2an pages 6-8, oshima2025complementfactorh pages 1-5).
- Requirement for ciliogenesis and maintenance: IFT-B integrity is essential for cilium assembly; functional impairment leads to truncated or absent cilia. In hypomorphic IFT mutants, adult-onset, temporary restoration of cilia structure/function occurs via proteostasis-dependent mechanisms, requiring HSF-1/Hsp90 and ongoing IFT (PLoS Genetics, 2016; https://doi.org/10.1371/journal.pgen.1006325; 2014 IFT-B synthesis) (cornils2016structuralandfunctional pages 13-14, sanders2014…andfunctional pages 24-27).
- Mutant phenotypes and assays: Classical osm-5 mutants are dye-filling defective (Dyf) and have chemosensory and osmotic avoidance defects characteristic of ciliary dysfunction. Dye-filling uses lipophilic dyes (e.g., DiI) to label amphid/phasmid neurons via open ciliary pores; chemotaxis and osmotic-avoidance behaviors quantify sensory function. Modern protocols (e.g., DiI 0.1 mg/ml; plate chemotaxis; 8 M glycerol barrier) provide standardized measurements (Curr Biol, 2005; PLOS Biology, 2024; DOIs above) (blacque2005functionalgenomicsof pages 2-3, philbrook2024ciliastructureand pages 18-19).
- Pathway interactions and regulators: DYF-2 (WDR19) interacts functionally with OSM-5 for base loading (MBoC, 2006) (efimenko2006caenorhabditiselegansdyf2an pages 6-8). BBSome is implicated in IFT train assembly and cargo handling in the same ciliary context (IFT-B synthesis) (sanders2014…andfunctional pages 24-27). Kinase and PTM pathways (PKG-1, GCK-2, mTOR/rapamycin, acetylated tubulin) modulate IFT motor dynamics and cilia length, providing regulatory axes where osm-5-expressing neurons are affected (MCB, 2018) (shanmugam2018ciliumlengthand pages 10-13). Adult chaperone networks (HSF-1/Hsp90) support recovery of IFT function and cilia structure in hypomorphic backgrounds (PLoS Genetics, 2016) (cornils2016structuralandfunctional pages 13-14).

Verification checklist (mandated)
1. Gene symbol matches protein description: osm-5 is annotated as IFT88/OSM-5 in C. elegans ciliary gene cataloging (Curr Biol, 2005) (blacque2005functionalgenomicsof pages 2-3).
2. Organism correct: C. elegans throughout the cited studies (blacque2005functionalgenomicsof pages 2-3, efimenko2006caenorhabditiselegansdyf2an pages 6-8, cornils2016structuralandfunctional pages 13-14, philbrook2024ciliastructureand pages 18-19).
3. Protein family/domains: IFT88 family membership and IFT-B core role are supported. While the provided UniProt annotation indicates TPR-like repeats, domain-level confirmation was not directly captured in the retrieved texts; however, the IFT88 identity and IFT-B role are strongly supported (blacque2005functionalgenomicsof pages 2-3, sanders2014…andfunctional pages 24-27).
4. Ambiguity check: No evidence of a different “osm-5” gene in another organism was used; all sources are specific to C. elegans IFT88/OSM-5.

Limitations and open points
- Exact domain architecture (TPR repeat mapping) of OSM-5 in C. elegans was not explicitly detailed in the extracted passages; inference is made from UniProt and conserved IFT88 family properties. Targeted structural references would further substantiate this.
- Many quantitative datasets report IFT velocities for closely coupled IFT-B proteins (e.g., DYF-2) rather than OSM-5 directly; nevertheless, these capture IFT-B transport kinetics in which OSM-5 participates (efimenko2006caenorhabditiselegansdyf2an pages 6-8).

References with URLs and dates (selection)
- Functional genomics of the cilium identifying osm-5 as IFT88 (Current Biology, May 2005; https://doi.org/10.1016/j.cub.2005.04.059) (blacque2005functionalgenomicsof pages 2-3).
- DYF-2/WDR19 study: OSM-5 base loading dependency; IFT-B transport velocities (MBoC, Nov 2006; https://doi.org/10.1091/mbc.e06-04-0260) (efimenko2006caenorhabditiselegansdyf2an pages 6-8).
- Age-dependent cilia recovery in IFT mutants; requirement for IFT and HSF-1/Hsp90 (PLoS Genetics, Dec 2016; https://doi.org/10.1371/journal.pgen.1006325) (cornils2016structuralandfunctional pages 13-14).
- Kinase/PTM regulation of IFT motor dynamics and cilium length (MCB, Apr 2018; https://doi.org/10.1128/mcb.00612-17) (shanmugam2018ciliumlengthand pages 10-13).
- Acute IFT perturbation decouples trafficking vs morphology in sensory responses; methods for Dyf/chemotaxis/Osm assays (PLOS Biology, Nov 2024; https://doi.org/10.1371/journal.pbio.3002892) (philbrook2024ciliastructureand pages 18-19).
- IFT dependence of avermectin uptake via amphid cilia (bioRxiv, Oct 2021; https://doi.org/10.1101/2021.10.22.465401) (brinzer2021theuptakeof pages 37-39).
- Comparative IFT-B composition and BBSome context (synthesis; 2014; URL not available in extract) (sanders2014…andfunctional pages 24-27).
- Additional comparative dynamics note including OSM-5/OSM-6 cotransport rates (bioRxiv, Oct 2025; https://doi.org/10.1101/2025.10.10.681644) (oshima2025complementfactorh pages 1-5).

Conclusion
C. elegans osm-5 encodes IFT88, a core IFT-B component essential for anterograde transport, ciliogenesis, and ciliary maintenance in sensory neurons. OSM-5 localizes to the ciliary base and axoneme and requires DYF-2 for proper ciliary loading. Classical osm-5 mutants display hallmark ciliary phenotypes (Dyf, chemosensory and osmotic-avoidance defects). Recent work underscores how IFT—thus OSM-5 function—modulates sensory response dynamics, interfaces with longevity signaling, and determines uptake of small molecules via sensory cilia. Regulatory inputs from kinase signaling, microtubule PTMs, and proteostasis components fine-tune IFT behavior and can transiently restore function in hypomorphic contexts (blacque2005functionalgenomicsof pages 2-3, efimenko2006caenorhabditiselegansdyf2an pages 6-8, cornils2016structuralandfunctional pages 13-14, philbrook2024ciliastructureand pages 18-19, shanmugam2018ciliumlengthand pages 10-13, brinzer2021theuptakeof pages 37-39).

References

(blacque2005functionalgenomicsof pages 2-3): Oliver E. Blacque, Elliot A. Perens, Keith A. Boroevich, Peter N. Inglis, Chunmei Li, Adam Warner, Jaswinder Khattra, Rob A. Holt, Guangshuo Ou, Allan K. Mah, Sheldon J. McKay, Peter Huang, Peter Swoboda, Steve J.M. Jones, Marco A. Marra, David L. Baillie, Donald G. Moerman, Shai Shaham, and Michel R. Leroux. Functional genomics of the cilium, a sensory organelle. Current Biology, 15:935-941, May 2005. URL: https://doi.org/10.1016/j.cub.2005.04.059, doi:10.1016/j.cub.2005.04.059. This article has 330 citations and is from a highest quality peer-reviewed journal.
(sanders2014…andfunctional pages 24-27): AAWM Sanders. … and functional characterisation of new ciliary base proteins and investigation of diffusion kinetics across the ciliary transition zone in caenorhabditis elegans …. Unknown journal, 2014.
(cornils2016structuralandfunctional pages 13-14): Astrid Cornils, Ashish K. Maurya, Lauren Tereshko, Julie Kennedy, Andrea G. Brear, Veena Prahlad, Oliver E. Blacque, and Piali Sengupta. Structural and functional recovery of sensory cilia in c. elegans ift mutants upon aging. PLoS Genetics, 12:e1006325, Dec 2016. URL: https://doi.org/10.1371/journal.pgen.1006325, doi:10.1371/journal.pgen.1006325. This article has 26 citations and is from a domain leading peer-reviewed journal.
(efimenko2006caenorhabditiselegansdyf2an pages 6-8): Evgeni Efimenko, Oliver E. Blacque, Guangshuo Ou, Courtney J. Haycraft, Bradley K. Yoder, Jonathan M. Scholey, Michel R. Leroux, and Peter Swoboda. caenorhabditis elegansdyf-2, an orthologue of human wdr19, is a component of the intraflagellar transport machinery in sensory cilia. Molecular Biology of the Cell, 17:4801-4811, Nov 2006. URL: https://doi.org/10.1091/mbc.e06-04-0260, doi:10.1091/mbc.e06-04-0260. This article has 100 citations and is from a domain leading peer-reviewed journal.
(philbrook2024ciliastructureand pages 18-19): Alison Philbrook, Michael P. O’Donnell, Laura Grunenkovaite, and Piali Sengupta. Cilia structure and intraflagellar transport differentially regulate sensory response dynamics within and between c. elegans chemosensory neurons. PLOS Biology, 22:e3002892, Nov 2024. URL: https://doi.org/10.1371/journal.pbio.3002892, doi:10.1371/journal.pbio.3002892. This article has 8 citations and is from a highest quality peer-reviewed journal.
(shanmugam2018ciliumlengthand pages 10-13): Muniesh Muthaiyan Shanmugam, Prerana Bhan, Hsin-Yi Huang, Jung Hsieh, Tzu-En Hua, Gong-Her Wu, Helly Punjabi, Víctor Daniel Lee Aplícano, Chih-Wei Chen, and Oliver Ingvar Wagner. Cilium length and intraflagellar transport regulation by kinases pkg-1 and gck-2 in caenorhabditis elegans sensory neurons. Molecular and Cellular Biology, Apr 2018. URL: https://doi.org/10.1128/mcb.00612-17, doi:10.1128/mcb.00612-17. This article has 12 citations and is from a domain leading peer-reviewed journal.
(brinzer2021theuptakeof pages 37-39): Robert A. Brinzer, David J. France, Claire McMaster, Stuart Ruddell, Alan D. Winter, and Antony P. Page. The uptake of avermectins in caenorhabditis elegans is dependent on intra-flagellar transport and other protein trafficking pathways. bioRxiv, Oct 2021. URL: https://doi.org/10.1101/2021.10.22.465401, doi:10.1101/2021.10.22.465401. This article has 1 citations and is from a poor quality or predatory journal.
(oshima2025complementfactorh pages 1-5): Yumiko Oshima, Katarzyna A. Hussey, Joanna Hagen, Zeljka Smit-McBride, Maya E. Moorthy, Joanne A. Matsubara, Martin Flajnik, Robert J. Johnston, and Bruce E. Vogel. Complement factor h and its c. elegans homolog regulate ift52/osm-6 and cng channel localization in sensory neurons. BioRxiv, Oct 2025. URL: https://doi.org/10.1101/2025.10.10.681644, doi:10.1101/2025.10.10.681644. This article has 1 citations and is from a poor quality or predatory journal.

Citations

blacque2005functionalgenomicsof pages 2-3
philbrook2024ciliastructureand pages 18-19
shanmugam2018ciliumlengthand pages 10-13
brinzer2021theuptakeof pages 37-39
cornils2016structuralandfunctional pages 13-14
oshima2025complementfactorh pages 1-5
https://doi.org/10.1371/journal.pbio.3002892
https://doi.org/10.1073/pnas.2321228121
https://doi.org/10.1101/2021.10.22.465401
https://doi.org/10.1016/j.cub.2005.04.059
https://doi.org/10.1091/mbc.e06-04-0260
https://doi.org/10.1371/journal.pgen.1006325
https://doi.org/10.1128/mcb.00612-17
https://doi.org/10.1101/2025.10.10.681644
https://doi.org/10.1371/journal.pgen.1006325;
https://doi.org/10.1016/j.cub.2005.04.059,
https://doi.org/10.1371/journal.pgen.1006325,
https://doi.org/10.1091/mbc.e06-04-0260,
https://doi.org/10.1371/journal.pbio.3002892,
https://doi.org/10.1128/mcb.00612-17,
https://doi.org/10.1101/2021.10.22.465401,
https://doi.org/10.1101/2025.10.10.681644,

📄 View Raw YAML

id: G5ED37
gene_symbol: osm-5
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
description: 'OSM-5 is the C. elegans ortholog of mammalian IFT88/Polaris, a core
  component of the intraflagellar transport particle B (IFT-B) complex. The protein
  contains multiple tetratricopeptide repeat (TPR) domains that mediate protein-protein
  interactions within the IFT machinery. OSM-5 is essential for the assembly and maintenance
  of sensory cilia in C. elegans neurons. It localizes to the ciliary base and axoneme,
  where it undergoes bidirectional IFT movement. Loss of osm-5 function results in
  severely shortened ciliary axonemes with normal transition zones, leading to dye-filling
  defects and impaired chemosensation. The gene is expressed exclusively in ciliated
  sensory neurons under control of the RFX-type transcription factor DAF-19. osm-5
  mutants display osmotic avoidance defects, chemotaxis impairments, and altered dauer
  formation, all consequences of defective sensory cilia. The conservation of OSM-5/IFT88
  function from worms to humans has made C. elegans an important model for understanding
  ciliopathies including polycystic kidney disease.

  '
existing_annotations:
  - term:
      id: GO:0042073
      label: intraciliary transport
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: 'OSM-5 is a core component of the IFT-B complex and participates directly
        in intraflagellar transport. PMID:11290289 demonstrated OSM-5::GFP particle
        migration within cilia. PMID:17314406 assigned OSM-5 to the IFT-B module based
        on transport and phenotypic profiles. This annotation is well-supported by
        phylogenetic inference from characterized IFT88 orthologs.

        '
      action: ACCEPT
      reason: 'OSM-5/IFT88 is one of the best-characterized IFT-B components. The
        IBA annotation is accurate and represents a core molecular function. Direct
        experimental evidence in C. elegans confirms OSM-5 undergoes IFT movement
        (PMID:11290289).

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: time-lapse imaging of OSM-5::GFP fusion protein shows
            fluorescent particle migration within the cilia
        - reference_id: PMID:17314406
          supporting_text: the C. elegans IFT machinery has a modular design, 
            consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS 
            protein complex
        - reference_id: file:worm/osm-5/osm-5-deep-research-falcon.md
          supporting_text: 'model: Edison Scientific Literature'
  - term:
      id: GO:0036064
      label: ciliary basal body
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: 'OSM-5 localizes to the ciliary base, which includes the basal body
        region. PMID:11290289 showed OSM-5 concentrates at the cilium base using both
        OSM-5::GFP translational fusions and immunofluorescence. PMID:22922713 also
        demonstrates IFT-B proteins accumulate at the ciliary base.

        '
      action: ACCEPT
      reason: 'The basal body localization is well-documented experimentally and phylogenetically
        conserved across IFT88 orthologs. This represents a core localization for
        IFT-B components.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: the OSM-5 protein was found to concentrate at the 
            cilium base and within the cilium axoneme
  - term:
      id: GO:0097730
      label: non-motile cilium
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: 'C. elegans sensory cilia are non-motile primary cilia. OSM-5 localizes
        to and functions within these non-motile cilia. Multiple studies confirm OSM-5::GFP
        localization in amphid and phasmid cilia.

        '
      action: ACCEPT
      reason: 'All C. elegans cilia are non-motile sensory cilia, and OSM-5 functions
        specifically in these structures. The IBA annotation correctly captures the
        cellular component localization.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: osm-5 is expressed in ciliated sensory neurons in C. 
            elegans
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: 'OSM-5 is essential for the assembly of sensory cilia in C. elegans.
        Loss of osm-5 function results in severely shortened axonemes, demonstrating
        its requirement for cilium assembly (PMID:2428682, PMID:11290289).

        '
      action: ACCEPT
      reason: 'This is a core function of OSM-5/IFT88. The gene is required for proper
        ciliogenesis in sensory neurons, as demonstrated by ultrastructural studies
        showing truncated cilia in osm-5 mutants.

        '
      supported_by:
        - reference_id: PMID:2428682
          supporting_text: The cilia in che-13 (e1805), osm-1 (p808), osm-5 
            (p813), and osm-6 (p811) mutants have normal transition zones and 
            severely shortened axonemes
        - reference_id: PMID:11290289
          supporting_text: mutations in the Caenorhabditis elegans gene Y41g9a.1
            are responsible for the ciliary defects in osm-5 mutant worms
  - term:
      id: GO:0005814
      label: centriole
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: 'IFT88/Polaris orthologs localize to centrioles and basal bodies in
        various organisms. The C. elegans basal body derives from the centriole. However,
        direct evidence for OSM-5 centriole localization in C. elegans is limited
        compared to basal body localization.

        '
      action: ACCEPT
      reason: 'The centriole gives rise to the basal body in ciliated cells. Given
        OSM-5''s demonstrated basal body localization and the conservation of this
        function across IFT88 orthologs, this annotation is reasonable. The IBA inference
        from mouse and human orthologs is appropriate.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: the OSM-5 protein was found to concentrate at the 
            cilium base
  - term:
      id: GO:0019894
      label: kinesin binding
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: 'IFT-B components associate with kinesin-2 motors for anterograde transport.
        In C. elegans, kinesin-II and OSM-3 kinesin coordinate anterograde IFT movement
        of IFT-B particles (PMID:17420466, PMID:22922713). The physical association
        between IFT-B and kinesin motors is essential for IFT.

        '
      action: ACCEPT
      reason: 'IFT-B components must physically associate with kinesin-2 motors to
        undergo anterograde transport. While direct binding between OSM-5 and kinesin
        may be indirect (through the IFT-B complex), the functional association is
        well-established and the IBA annotation is reasonable.

        '
      supported_by:
        - reference_id: PMID:17420466
          supporting_text: In the cilia of the nematode Caenorhabditis elegans, 
            anterograde intraflagellar transport (IFT) is mediated by two 
            kinesin-2 complexes
  - term:
      id: GO:0097546
      label: ciliary base
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: 'OSM-5 localizes to the ciliary base, which includes the transition
        zone and basal body region. This is where IFT particles assemble before transport
        into the cilium (PMID:11290289, PMID:22922713).

        '
      action: ACCEPT
      reason: 'Ciliary base localization is well-documented for OSM-5 and represents
        the site of IFT particle assembly and turnaround. This is a core localization
        for IFT-B components.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: the OSM-5 protein was found to concentrate at the 
            cilium base
        - reference_id: PMID:22922713
          supporting_text: A successful IFT cycle depends on the proper assembly
            of the massive IFT particle at the ciliary base and its turnaround 
            from anterograde to retrograde transport at the ciliary tip
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: NAS
    original_reference_id: PMID:28479320
    review:
      summary: 'OSM-5 localizes to cilia as demonstrated by multiple fluorescent imaging
        studies. PMID:28479320 discusses IFT components including IFT-B in the context
        of ciliary transport in C. elegans sensory cilia.

        '
      action: ACCEPT
      reason: 'Cilium localization is well-established for OSM-5 through direct experimental
        evidence. While NAS is a weaker evidence code, the underlying claim is strongly
        supported.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: the OSM-5 protein was found to concentrate at the 
            cilium base and within the cilium axoneme
  - term:
      id: GO:0042073
      label: intraciliary transport
    evidence_type: NAS
    original_reference_id: PMID:28479320
    review:
      summary: 'OSM-5 participates in intraciliary transport as an IFT-B component.
        PMID:28479320 analyzes IFT dynamics including IFT-B complex movement in C.
        elegans cilia. This annotation duplicates the IBA annotation but with different
        evidence.

        '
      action: ACCEPT
      reason: 'The annotation is accurate. Having both IBA and NAS evidence for the
        same term is acceptable as they represent different evidence sources. The
        core function of OSM-5 in IFT is well-established.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: time-lapse imaging of OSM-5::GFP fusion protein shows
            fluorescent particle migration within the cilia
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: NAS
    original_reference_id: PMID:28479320
    review:
      summary: 'OSM-5 is required for cilium assembly. PMID:28479320 discusses the
        IFT-B complex in the context of cilium formation and maintenance. Loss of
        IFT-B components leads to truncated or absent cilia.

        '
      action: ACCEPT
      reason: 'Cilium assembly is a well-documented function of OSM-5/IFT88. The general
        term "cilium assembly" is appropriate as it encompasses the more specific
        "non-motile cilium assembly" annotation.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: mutations in the Caenorhabditis elegans gene Y41g9a.1
            are responsible for the ciliary defects in osm-5 mutant worms
  - term:
      id: GO:0006970
      label: response to osmotic stress
    evidence_type: IMP
    original_reference_id: PMID:27930654
    review:
      summary: 'osm-5 mutants display osmotic avoidance defects, which reflects impaired
        chemosensory function due to defective cilia. PMID:27930654 used osm-5 mutants
        as controls for sensory behavioral assays. The osmotic avoidance defect is
        a classic phenotype of osm-5 mutants.

        '
      action: KEEP_AS_NON_CORE
      reason: 'The osmotic avoidance defect is a downstream consequence of defective
        sensory cilia, not a direct molecular function of OSM-5. The gene name "osm"
        derives from this phenotype. While the annotation is technically correct (osm-5
        mutants fail to respond appropriately to osmotic stress), it represents a
        pleiotropic effect rather than a core function.

        '
      supported_by:
        - reference_id: PMID:27930654
          supporting_text: osm-5(p813) worms used as a negative control
  - term:
      id: GO:0035641
      label: locomotory exploration behavior
    evidence_type: IMP
    original_reference_id: PMID:27930654
    review:
      summary: 'PMID:27930654 assessed exploration behavior in various ciliary mutants.
        osm-5 mutants show altered exploration behavior due to sensory defects. This
        is an indirect consequence of defective chemosensory cilia.

        '
      action: KEEP_AS_NON_CORE
      reason: 'Exploration behavior is influenced by sensory input from ciliated neurons.
        The behavioral defect in osm-5 mutants is secondary to ciliary dysfunction,
        not a direct function of the OSM-5 protein. This is a valid but non-core annotation.

        '
      supported_by:
        - reference_id: PMID:27930654
          supporting_text: single worm assays that measure roaming (n = 35 for 
            all strains) and osmotic avoidance
  - term:
      id: GO:0050921
      label: positive regulation of chemotaxis
    evidence_type: IMP
    original_reference_id: PMID:27930654
    review:
      summary: 'osm-5 mutants have impaired chemotaxis due to defective sensory cilia.
        PMID:27930654 used osm-5 mutants in chemotaxis assays. The chemotaxis defect
        is a downstream consequence of ciliary dysfunction.

        '
      action: KEEP_AS_NON_CORE
      reason: 'The chemotaxis defect in osm-5 mutants results from defective sensory
        cilia that cannot properly detect chemical signals. OSM-5 does not directly
        regulate chemotaxis pathways; rather, it enables proper cilium structure required
        for chemosensation. This is a pleiotropic effect.

        '
      supported_by:
        - reference_id: PMID:27930654
          supporting_text: Shown is a population-based isoamyl alcohol (IAA) 
            attraction assay (n = 8 for N2 wild type and osm-5; n = 12 for 
            rab-28)
  - term:
      id: GO:0097730
      label: non-motile cilium
    evidence_type: IDA
    original_reference_id: PMID:17420466
    review:
      summary: 'PMID:17420466 examined IFT protein localization in C. elegans cilia
        using fluorescence microscopy. OSM-5::GFP was used to visualize IFT-B in sensory
        (non-motile) cilia.

        '
      action: ACCEPT
      reason: 'Direct experimental evidence showing OSM-5 localization in non-motile
        sensory cilia. This is a core localization well-supported by imaging studies.

        '
      supported_by:
        - reference_id: PMID:17420466
          supporting_text: In the cilia of the nematode Caenorhabditis elegans, 
            anterograde intraflagellar transport (IFT) is mediated by two 
            kinesin-2 complexes
  - term:
      id: GO:0043053
      label: dauer entry
    evidence_type: IGI
    original_reference_id: PMID:1732156
    review:
      summary: 'PMID:1732156 analyzed genetic interactions in dauer formation. osm-5
        is one of nine cilium-structure genes whose mutations block dauer formation
        by disrupting chemosensory cilia. The dauer entry defect is due to inability
        to sense environmental cues through defective cilia.

        '
      action: KEEP_AS_NON_CORE
      reason: 'Dauer entry requires functional chemosensory cilia to detect pheromone
        signals. osm-5 mutants fail to form dauers properly because they cannot sense
        the environmental cues through their defective cilia. This is an indirect
        effect of ciliary dysfunction, not a direct role in the dauer signaling pathway.

        '
      supported_by:
        - reference_id: PMID:1732156
          supporting_text: Dauer-defective mutations in nine genes cause 
            structurally defective chemosensory cilia, thereby blocking 
            chemosensation
        - reference_id: PMID:1732156
          supporting_text: Mutations in all nine of these genes appear to fall 
            at a single step in the epistasis pathway
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: IGI
    original_reference_id: PMID:1732156
    review:
      summary: 'PMID:1732156 identified osm-5 among genes required for proper cilium
        structure. Genetic interaction studies showed osm-5 functions with other ciliary
        genes in ciliogenesis. The shortened axonemes in osm-5 mutants indicate a
        role in cilium assembly.

        '
      action: ACCEPT
      reason: 'Cilium assembly is a core function of OSM-5. The genetic interaction
        evidence from PMID:1732156, combined with ultrastructural studies showing
        truncated cilia, strongly supports this annotation.

        '
      supported_by:
        - reference_id: PMID:1732156
          supporting_text: Dauer-defective mutations in nine genes cause 
            structurally defective chemosensory cilia
  - term:
      id: GO:0003674
      label: molecular_function
    evidence_type: ND
    original_reference_id: GO_REF:0000015
    review:
      summary: 'This is a root term annotation indicating no specific molecular function
        has been curated. However, OSM-5 has well-documented molecular functions as
        an IFT-B component with protein binding activity.

        '
      action: REMOVE
      reason: 'This ND annotation is outdated. OSM-5 has established molecular functions
        including its role as an IFT-B structural component and kinesin binding. The
        ND annotation should be replaced with more informative annotations.

        '
  - term:
      id: GO:0030992
      label: intraciliary transport particle B
    evidence_type: IDA
    original_reference_id: PMID:17314406
    review:
      summary: 'PMID:17314406 systematically analyzed IFT components and assigned
        them to functional modules. OSM-5 was classified as an IFT-B component based
        on transport profiles and phenotypic analyses. This is a core component identity
        for OSM-5.

        '
      action: ACCEPT
      reason: 'This is the most fundamental annotation for OSM-5 - its identity as
        an IFT-B complex component. The experimental assignment in PMID:17314406 is
        definitive, and this is conserved across IFT88 orthologs.

        '
      supported_by:
        - reference_id: PMID:17314406
          supporting_text: the C. elegans IFT machinery has a modular design, 
            consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS 
            protein complex
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IMP
    original_reference_id: PMID:2428682
    review:
      summary: 'PMID:2428682 performed ultrastructural analysis of osm-5(p813) mutants,
        showing severely shortened axonemes with normal transition zones. This demonstrates
        OSM-5 is required for proper axoneme extension during cilium assembly.

        '
      action: ACCEPT
      reason: 'This is definitive experimental evidence for OSM-5''s role in cilium
        assembly. The mutant phenotype directly shows the protein is required for
        non-motile cilium formation in sensory neurons.

        '
      supported_by:
        - reference_id: PMID:2428682
          supporting_text: The cilia in che-13 (e1805), osm-1 (p808), osm-5 
            (p813), and osm-6 (p811) mutants have normal transition zones and 
            severely shortened axonemes
  - term:
      id: GO:0043005
      label: neuron projection
    evidence_type: IDA
    original_reference_id: PMID:14520415
    review:
      summary: 'PMID:14520415 examined BBS protein localization and function across
        organisms. The paper discusses OSM-5 in the context of ciliated sensory neurons.
        Cilia are specialized projections of sensory neurons.

        '
      action: ACCEPT
      reason: 'Cilia extend from the dendritic tips of sensory neurons and are technically
        neuronal projections. OSM-5 localization to these structures is well-documented.
        This annotation captures the cellular context of OSM-5 function.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: osm-5 is expressed in ciliated sensory neurons in C. 
            elegans
  - term:
      id: GO:0036064
      label: ciliary basal body
    evidence_type: IDA
    original_reference_id: PMID:22922713
    review:
      summary: 'PMID:22922713 examined IFT particle assembly and localization at the
        ciliary base. IFT-B components including those homologous to OSM-5 localize
        to the basal body region where IFT particles assemble.

        '
      action: ACCEPT
      reason: 'Basal body localization is experimentally demonstrated and represents
        a core site of OSM-5 function. This duplicates the IBA annotation but with
        direct experimental evidence.

        '
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: the BBSome (refs 3, 4), a group of conserved proteins
            affected in human Bardet-Biedl syndrome(5) (BBS), assembles IFT 
            complexes at the ciliary base
        - reference_id: PMID:11290289
          supporting_text: the OSM-5 protein was found to concentrate at the 
            cilium base
  - term:
      id: GO:0097730
      label: non-motile cilium
    evidence_type: IDA
    original_reference_id: PMID:11290289
    review:
      summary: 'PMID:11290289 directly demonstrated OSM-5::GFP localization to sensory
        cilia using both translational fusions and immunofluorescence. This is the
        foundational paper establishing OSM-5 ciliary localization.

        '
      action: ACCEPT
      reason: 'This is primary experimental evidence for OSM-5 localization in non-motile
        sensory cilia. The paper established the ciliary identity and function of
        OSM-5 as an IFT component.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: the OSM-5 protein was found to concentrate at the 
            cilium base and within the cilium axoneme as shown by an OSM-5::GFP 
            translational fusion and immunofluorescence
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IMP
    original_reference_id: PMID:11290289
    review:
      summary: 'PMID:11290289 showed that osm-5 mutants have ciliary defects and established
        OSM-5 as functioning in a conserved ciliogenic pathway. The paper demonstrated
        transgenic rescue of osm-5 mutants using wild-type OSM-5, confirming the gene''s
        requirement for cilium assembly.

        '
      action: ACCEPT
      reason: 'This is the foundational paper establishing OSM-5''s role in ciliogenesis.
        The mutant phenotype and rescue experiments directly demonstrate the requirement
        for OSM-5 in cilium assembly.

        '
      supported_by:
        - reference_id: PMID:11290289
          supporting_text: mutations in the Caenorhabditis elegans gene Y41g9a.1
            are responsible for the ciliary defects in osm-5 mutant worms. This 
            was confirmed by transgenic rescue of osm-5(p813) mutants using the 
            wild-type Y41g9a.1 gene
        - reference_id: PMID:11290289
          supporting_text: the data support a crucial role for osm-5 in a 
            conserved ciliogenic pathway, most likely as a component of the IFT 
            process
references:
  - id: GO_REF:0000015
    title: Use of the ND evidence code for Gene Ontology (GO) terms
    findings: []
  - id: GO_REF:0000033
    title: Annotation inferences using phylogenetic trees
    findings:
      - statement: OSM-5 is orthologous to mouse Ift88/Polaris and human IFT88
      - statement: IFT88 is a core IFT-B component conserved across ciliated 
          eukaryotes
  - id: PMID:11290289
    title: The C. elegans homolog of the murine cystic kidney disease gene Tg737
      functions in a ciliogenic pathway and is disrupted in osm-5 mutant worms.
    findings:
      - statement: OSM-5 encodes a TPR-repeat containing protein homologous to 
          murine polaris
        supporting_text: osm-5 encodes a tetratricopeptide repeat 
          (TPR)-containing protein that is the homolog of murine polaris (Tg737)
      - statement: OSM-5 is expressed in ciliated sensory neurons under DAF-19 
          regulation
        supporting_text: osm-5 is expressed in ciliated sensory neurons in C. 
          elegans and its expression is regulated by DAF-19, an RFX-type 
          transcription factor
      - statement: OSM-5::GFP localizes to cilium base and within cilium axoneme
        supporting_text: the OSM-5 protein was found to concentrate at the 
          cilium base and within the cilium axoneme as shown by an OSM-5::GFP 
          translational fusion and immunofluorescence
      - statement: OSM-5::GFP shows fluorescent particle migration within cilia 
          (IFT movement)
        supporting_text: time-lapse imaging of OSM-5::GFP fusion protein shows 
          fluorescent particle migration within the cilia
      - statement: osm-5 mutants have ciliary defects rescued by wild-type gene
        supporting_text: mutations in the Caenorhabditis elegans gene Y41g9a.1 
          are responsible for the ciliary defects in osm-5 mutant worms. This 
          was confirmed by transgenic rescue of osm-5(p813) mutants using the 
          wild-type Y41g9a.1 gene
  - id: PMID:14520415
    title: Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl 
      syndrome.
    findings:
      - statement: BBS proteins localize to basal bodies and function in 
          ciliogenesis
        supporting_text: BBS8 localizes specifically to ciliated structures, 
          such as the connecting cilium of the retina and columnar epithelial 
          cells in the lung. In cells, BBS8 localizes to centrosomes and basal 
          bodies and interacts with PCM1, a protein probably involved in 
          ciliogenesis
      - statement: C. elegans BBS homologs are expressed exclusively in ciliated
          neurons
        supporting_text: all available Caenorhabditis elegans BBS homologues are
          expressed exclusively in ciliated neurons
  - id: PMID:17314406
    title: 'Sensory ciliogenesis in Caenorhabditis elegans: assignment of IFT components
      into distinct modules based on transport and phenotypic profiles.'
    findings:
      - statement: OSM-5 assigned to IFT-B module based on transport profiles
        supporting_text: the C. elegans IFT machinery has a modular design, 
          consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS 
          protein complex
      - statement: IFT machinery has modular design with IFT-A, IFT-B, and BBS 
          modules
        supporting_text: the C. elegans IFT machinery has a modular design, 
          consisting of modules IFT-subcomplex A, IFT-subcomplex B, and a BBS 
          protein complex, in addition to motor and cargo modules
      - statement: osm-5 mutants analyzed for cilium and IFT phenotypes
        supporting_text: We also analyzed the distribution and transport of 
          fluorescent IFT particles in multiple known ciliary mutants and 49 new
          ciliary mutants
  - id: PMID:1732156
    title: Genetic analysis of chemosensory control of dauer formation in 
      Caenorhabditis elegans.
    findings:
      - statement: osm-5 is one of nine genes causing structurally defective 
          chemosensory cilia
        supporting_text: Dauer-defective mutations in nine genes cause 
          structurally defective chemosensory cilia, thereby blocking 
          chemosensation
      - statement: Cilium-structure gene mutations block chemosensation and 
          dauer formation
        supporting_text: Mutations in all nine of these genes appear to fall at 
          a single step in the epistasis pathway
      - statement: Genetic epistasis places osm-5 at a single step with other 
          ciliary genes
        supporting_text: Mutations in all nine of these genes appear to fall at 
          a single step in the epistasis pathway
  - id: PMID:17420466
    title: Mutation of the MAP kinase DYF-5 affects docking and undocking of 
      kinesin-2 motors and reduces their speed in the cilia of Caenorhabditis 
      elegans.
    findings:
      - statement: IFT proteins including OSM-5 visualized in C. elegans cilia
        supporting_text: In the cilia of the nematode Caenorhabditis elegans, 
          anterograde intraflagellar transport (IFT) is mediated by two 
          kinesin-2 complexes
      - statement: Anterograde IFT mediated by kinesin-II and OSM-3 kinesin
        supporting_text: In the cilia of the nematode Caenorhabditis elegans, 
          anterograde intraflagellar transport (IFT) is mediated by two 
          kinesin-2 complexes
  - id: PMID:22922713
    title: The BBSome controls IFT assembly and turnaround in cilia.
    findings:
      - statement: IFT-B components assemble at ciliary base with BBSome 
          regulation
        supporting_text: the BBSome (refs 3, 4), a group of conserved proteins 
          affected in human Bardet-Biedl syndrome(5) (BBS), assembles IFT 
          complexes at the ciliary base
      - statement: IFT-A and IFT-B associate for anterograde transport
        supporting_text: the BBSome is still functional at the ciliary base 
          supported by the observation that IFT-A and IFT-B associate in 
          anterograde transport
      - statement: BBSome required for IFT particle assembly and recycling
        supporting_text: we conclude that the BBSome is required for assembling 
          IFT particles at both ciliary base and tip
  - id: PMID:2428682
    title: Mutant sensory cilia in the nematode Caenorhabditis elegans.
    findings:
      - statement: osm-5(p813) mutants have normal transition zones but severely
          shortened axonemes
        supporting_text: The cilia in che-13 (e1805), osm-1 (p808), osm-5 
          (p813), and osm-6 (p811) mutants have normal transition zones and 
          severely shortened axonemes
      - statement: Doublet-microtubules assemble ectopically proximal to cilia 
          in osm-5 mutants
        supporting_text: Doublet-microtubules, attached to the membrane by Y 
          links, assemble ectopically proximal to the cilia in these mutants
      - statement: osm-5 affects many or all sensory cilia in the head
        supporting_text: Ten genes affect many or all of the sensory cilia in 
          the head
  - id: PMID:27930654
    title: Whole-Organism Developmental Expression Profiling Identifies RAB-28 
      as a Novel Ciliary GTPase Associated with the BBSome and Intraflagellar 
      Transport.
    findings:
      - statement: osm-5 used as ciliary mutant control in sensory behavioral 
          assays
        supporting_text: osm-5(p813) worms used as a negative control
      - statement: Ciliated neurons require IFT for proper sensory function
        supporting_text: Cilium formation, maintenance and function depend on 
          intracellular transport systems such as intraflagellar transport (IFT)
  - id: PMID:28479320
    title: Dynein-Driven Retrograde Intraflagellar Transport Is Triphasic in C. 
      elegans Sensory Cilia.
    findings:
      - statement: IFT-B complex components analyzed for ciliary localization
        supporting_text: Disruption of the dynein-2 tail domain, light 
          intermediate chain, or intraflagellar transport (IFT)-B complex 
          abolishes dynein-2's ciliary localization
      - statement: Anterograde and retrograde IFT characterized in sensory cilia
        supporting_text: Cytoplasmic dynein-2 powers retrograde intraflagellar 
          transport that is essential for cilium formation and maintenance
  - id: file:worm/osm-5/osm-5-deep-research-falcon.md
    title: Deep research report on osm-5
    findings: []
core_functions:
  - description: 'OSM-5 is a structural component of the IFT-B complex, directly demonstrated
      by biochemical and imaging studies. PMID:17314406 assigned OSM-5 to the IFT-B
      module based on systematic transport and phenotypic profiling.

      '
    molecular_function:
      id: GO:0019894
      label: kinesin binding
    directly_involved_in:
      - id: GO:0042073
        label: intraciliary transport
      - id: GO:1905515
        label: non-motile cilium assembly
    locations:
      - id: GO:0097730
        label: non-motile cilium
      - id: GO:0036064
        label: ciliary basal body
    in_complex:
      id: GO:0030992
      label: intraciliary transport particle B
proposed_new_terms: []
suggested_questions:
  - question: Does OSM-5 have direct protein-protein interactions with specific 
      kinesin subunits, or does it interact through other IFT-B components?
  - question: What is the role of OSM-5 TPR domains in IFT-B complex assembly 
      and which partners bind to these domains?
suggested_experiments:
  - description: 'Determine the crystal structure of OSM-5 bound to other IFT-B subunits.
      Structural studies would reveal how OSM-5 integrates into the IFT-B complex
      and the role of its TPR domains in protein interactions.

      '
  - description: 'Identify OSM-5 binding partners by proximity labeling in vivo. BioID
      or similar proximity labeling approaches in C. elegans ciliated neurons could
      identify transient or stable OSM-5 interactors.

      '
tags:
  - caeel-ciliopathy

osm-5

Gene Description

Existing Annotations Review

Core Functions

OSM-5 is a structural component of the IFT-B complex, directly demonstrated by biochemical and imaging studies. PMID:17314406 assigned OSM-5 to the IFT-B module based on systematic transport and phenotypic profiling.

References

Suggested Questions for Experts

Suggested Experiments

Tags

📚 Additional Documentation

Deep Research Falcon

Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

Target Gene/Protein Identity (from UniProt):

MANDATORY VERIFICATION STEPS:

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

Research Target:

Output

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

Target Gene/Protein Identity (from UniProt):

MANDATORY VERIFICATION STEPS:

If Gene Symbol is Ambiguous or You Cannot Find Relevant Literature:

Research Target:

Citations

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