Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0008104 intracellular protein localization	IBA GO_REF:0000033	MODIFY	Summary: BBS-7 as part of the BBSome is involved in protein localization, specifically the targeting and transport of ciliary membrane proteins. The BBSome controls IFT assembly and turnaround, regulating protein cargo loading and transport (PMID:22922713). Reason: While the annotation captures BBS-7's role in protein localization, this term is too general. The more specific function is ciliary protein localization, as BBS-7/BBSome specifically regulates the localization of proteins to and within cilia, including IFT components and ciliary membrane receptors (PMID:22922713, PMID:25335890). Proposed replacements: protein localization to cilium Supporting Evidence: PMID:22922713 the BBSome functions as a scaffold to organize IFT-A, IFT-B, ciliary membrane receptors, ciliary signaling molecules, and/or other IFT cargos into an entire unit and prepare it for IFT transport file:worm/bbs-7/bbs-7-deep-research-falcon.md model: Edison Scientific Literature
GO:0016020 membrane	IBA GO_REF:0000033	MODIFY	Summary: BBS-7 as part of the BBSome is associated with membranes, particularly ciliary membranes. The BBSome shares structural features with COPI, COPII, and clathrin coats, functioning as a coat complex for membrane protein sorting (PMID:22922713). Reason: The term 'membrane' is too general for BBS-7 localization. BBS-7 specifically localizes to the ciliary membrane system and is involved in ciliary membrane protein sorting. A more specific cellular component term reflecting ciliary localization would be more appropriate. Proposed replacements: cilium Supporting Evidence: PMID:22922713 The BBSome also shares the common structural features with COPI, COPII, and clathrin coats, and can directly recognize IFT cargos
GO:0034464 BBSome	IBA GO_REF:0000033	ACCEPT	Summary: BBS-7 is a core component of the BBSome complex. This is well-established across species and confirmed in C. elegans (PMID:22922713, PMID:15231740). The BBSome contains BBS-1, BBS-2, BBS-4, BBS-5, BBS-7, BBS-8, and BBS-9. Reason: This is a well-supported core function. BBS-7 is definitively a BBSome component, confirmed by both phylogenetic analysis (IBA) and direct experimental evidence in C. elegans showing physical interaction with other BBSome subunits. Supporting Evidence: PMID:22922713 fluorescence complementation can be observed in BBS-1–BBS-7 and BBS-1–BBS-9 pair, indicative of the coexistence of these three BBS proteins in the same complex PMID:15231740 mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia
GO:0036064 ciliary basal body	IBA GO_REF:0000033	ACCEPT	Summary: BBS-7 localizes to the ciliary basal body where it participates in IFT particle assembly before anterograde transport. The BBSome assembles IFT complexes at the ciliary base (PMID:22922713, PMID:15231740). Reason: Well-supported localization. BBS-7 and other BBSome proteins localize predominantly at the base of cilia (basal body) where they function in IFT assembly. This is confirmed by direct experimental observation in C. elegans. Supporting Evidence: PMID:15231740 C. elegans BBS proteins localize predominantly at the base of cilia PMID:22922713 the BBSome is required for assembling IFT particles at both ciliary base and tip
GO:0043005 neuron projection	IBA GO_REF:0000033	ACCEPT	Summary: BBS-7 is expressed in ciliated sensory neurons in C. elegans, localizing to their ciliary projections including amphid, labial, and phasmid neurons (PMID:14520415, PMID:15231740). Reason: Accurate localization. BBS-7 is specifically expressed in ciliated sensory neurons and localizes to their projections (the sensory cilia). However, the more specific term 'cilium' or 'sensory cilium' would be preferred. Supporting Evidence: PMID:14520415 all available Caenorhabditis elegans BBS homologues are expressed exclusively in ciliated neurons
GO:0060271 cilium assembly	IBA GO_REF:0000033	ACCEPT	Summary: BBS-7 is required for proper cilium assembly through its role in IFT. Loss of BBS-7 results in structural ciliary defects including loss of distal segments (PMID:15231740, PMID:17000880). Reason: Core function. BBS-7 is essential for proper cilia biogenesis through its role in IFT particle assembly and maintaining IFT integrity. This is supported by strong experimental evidence showing ciliary structural defects in bbs-7 mutants. Supporting Evidence: PMID:15231740 mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia PMID:17000880 the loss of BBS-7 and -8 function in mutant animals leads to the loss of ciliary distal segments and sensory defects
GO:0005930 axoneme	IBA GO_REF:0000033	ACCEPT	Summary: BBS-7 localizes to the ciliary axoneme where it undergoes bidirectional IFT movement (PMID:15231740). The protein moves in anterograde and retrograde directions along the ciliary axonemes. Reason: Well-supported localization. BBS-7 is found in the axoneme where it participates in IFT. UniProt confirms BBS-7 moves bidirectionally along the ciliary axonemes. Supporting Evidence: PMID:15231740 like proteins involved in intraflagellar transport (IFT), a process necessary for cilia biogenesis and maintenance, move bidirectionally along the ciliary axoneme
GO:0005929 cilium	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation based on UniProt subcellular location. BBS-7 localizes to cilia as part of the BBSome complex, participating in IFT. Reason: Correct annotation, well-supported by multiple experimental studies. BBS-7 is a ciliary protein that functions within cilia. Supporting Evidence: PMID:15231740 C. elegans BBS proteins localize predominantly at the base of cilia
GO:0005930 axoneme	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation based on UniProt subcellular location. BBS-7 localizes to the axoneme as part of IFT. Reason: Correct annotation consistent with experimental evidence showing BBS-7 moves along the ciliary axoneme during IFT. Supporting Evidence: PMID:15231740 move bidirectionally along the ciliary axoneme
GO:0015031 protein transport	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation based on UniProt keyword. BBS-7 is involved in protein transport through its role in IFT. Reason: Correct general annotation. BBS-7 participates in ciliary protein transport as part of the IFT machinery. The BBSome loads protein cargos for IFT transport. Supporting Evidence: PMID:22922713 the BBSome functions as a scaffold to organize IFT-A, IFT-B, ciliary membrane receptors, ciliary signaling molecules, and/or other IFT cargos into an entire unit and prepare it for IFT transport
GO:0030030 cell projection organization	IEA GO_REF:0000043	ACCEPT	Summary: IEA annotation based on UniProt keyword. BBS-7 is involved in cilium organization through its role in IFT and cilium biogenesis. Reason: Correct general annotation. BBS-7 is required for proper organization of cilia (a type of cell projection) through its role in IFT. Supporting Evidence: PMID:15231740 mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia
GO:0034464 BBSome	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation based on InterPro domain. BBS-7 is a BBSome component as indicated by its conserved domain structure. Reason: Correct annotation consistent with IBA and experimental evidence. Retaining both IEA and IBA annotations is appropriate as they derive from independent evidence sources. Supporting Evidence: PMID:22922713 fluorescence complementation can be observed in BBS-1–BBS-7 and BBS-1–BBS-9 pair
GO:1905515 non-motile cilium assembly	IEA GO_REF:0000002	ACCEPT	Summary: IEA annotation based on InterPro. C. elegans sensory cilia are non-motile (primary) cilia, and BBS-7 is required for their assembly. Reason: Appropriate annotation. C. elegans sensory neurons have non-motile (primary) cilia, and BBS-7 is required for their proper assembly. This is more specific than the general 'cilium assembly' term. Supporting Evidence: PMID:15231740 mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia
GO:0005929 cilium	NAS PMID:22922713 The BBSome controls IFT assembly and turnaround in cilia.	ACCEPT	Summary: NAS annotation from ComplexPortal based on Wei et al. 2012 showing BBSome localization and function in cilia. Reason: Correct annotation. PMID:22922713 extensively characterizes BBS-7 and BBSome localization and function in C. elegans cilia. Supporting Evidence: PMID:22922713 the BBSome is required for assembling IFT particles at both ciliary base and tip
GO:0060271 cilium assembly	NAS PMID:22922713 The BBSome controls IFT assembly and turnaround in cilia.	ACCEPT	Summary: NAS annotation from ComplexPortal. The BBSome is required for proper cilium assembly through its role in IFT. Reason: Correct annotation supported by the cited publication showing BBSome role in IFT assembly and ciliogenesis. Supporting Evidence: PMID:22922713 the major role for the BBSome in cilia is to efficiently assemble IFT particles at both cilia base and tip
GO:1904107 protein localization to microvillus membrane	IMP PMID:25335890 Ciliopathy proteins establish a bipartite signaling compartm...	KEEP AS NON CORE	Summary: This annotation refers to BBS-7's role in localizing guanylyl cyclases to the 'finger compartment' of AFD thermosensory neurons, which contains microvillus-like structures (PMID:25335890). Reason: This is a specialized function in AFD thermosensory neurons rather than a core function. While experimentally validated, it represents a specific neuronal context. The finger compartment of AFD neurons contains microvillus-like structures where guanylyl cyclases localize. BBS-7 mutants show impaired localization of GCY-8, GCY-18, and GCY-23 to this region. Supporting Evidence: PMID:25335890 requires BBS-8 and DAF-25 (known as Ankmy2 in mammals) for correct localization of guanylyl cyclases needed for thermosensation
GO:0097730 non-motile cilium	IDA PMID:22342749 Endocytosis genes facilitate protein and membrane transport ...	ACCEPT	Summary: IDA annotation showing BBS-7 localization to non-motile (sensory) cilia in C. elegans based on imaging studies. Reason: Correct and specific localization annotation. C. elegans sensory cilia are non-motile primary cilia, and BBS-7 localizes to these structures. Supporting Evidence: PMID:15231740 C. elegans BBS proteins localize predominantly at the base of cilia
GO:0036064 ciliary basal body	IDA PMID:22922713 The BBSome controls IFT assembly and turnaround in cilia.	ACCEPT	Summary: IDA annotation showing BBS-7 localization to the ciliary basal body. Wei et al. 2012 showed BBSome proteins accumulate around the ciliary base. Reason: Well-supported localization. The BBSome assembles IFT complexes at the ciliary base (basal body region) before anterograde transport begins. Supporting Evidence: PMID:22922713 Like in dyf-2(jhu616) animals, all BBSome proteins strongly accumulate around the ciliary base PMID:15231740 C. elegans BBS proteins localize predominantly at the base of cilia
GO:0042073 intraciliary transport	IMP PMID:17000880 Mechanism of transport of IFT particles in C. elegans cilia ...	ACCEPT	Summary: IMP annotation based on mutant phenotype showing BBS-7 role in IFT. Loss of BBS-7 causes IFT-A and IFT-B subcomplexes to dissociate and move at different rates (PMID:17000880, PMID:22922713). Reason: Core function. BBS-7 is essential for proper IFT through its role in maintaining IFT particle integrity and regulating IFT assembly and turnaround. Supporting Evidence: PMID:17000880 in bbs-7/-8 mutants, kinesin-II and IFT-A move together at 0.5 μm/s, but OSM-3–kinesin and IFT-B move as a distinct complex at 1.3 μm/s PMID:22922713 the BBSome is required for assembling IFT particles at both ciliary base and tip
GO:0043005 neuron projection	IDA PMID:14520415 Basal body dysfunction is a likely cause of pleiotropic Bard...	ACCEPT	Summary: IDA annotation showing BBS-7 expression in ciliated sensory neuron projections (PMID:14520415). Reason: Correct localization. BBS-7 is expressed in ciliated sensory neurons and localizes to their ciliary projections. Supporting Evidence: PMID:14520415 all available Caenorhabditis elegans BBS homologues are expressed exclusively in ciliated neurons, and contain regulatory elements for RFX, a transcription factor that modulates the expression of genes associated with ciliogenesis and intraflagellar transport
GO:1905515 non-motile cilium assembly	IEP PMID:14520415 Basal body dysfunction is a likely cause of pleiotropic Bard...	ACCEPT	Summary: IEP annotation based on expression pattern. BBS-7 is expressed in ciliated neurons suggesting role in cilium assembly. Reason: Appropriate annotation. Expression in ciliated neurons combined with ciliopathy phenotypes in mutants supports a role in non-motile cilium assembly. Supporting Evidence: PMID:14520415 all available Caenorhabditis elegans BBS homologues are expressed exclusively in ciliated neurons, and contain regulatory elements for RFX, a transcription factor that modulates the expression of genes associated with ciliogenesis and intraflagellar transport
GO:0060271 cilium assembly	IMP PMID:15231740 Loss of C. elegans BBS-7 and BBS-8 protein function results ...	ACCEPT	Summary: IMP annotation based on mutant phenotype. bbs-7 mutants have structural ciliary defects including loss of distal segments (PMID:15231740). Reason: Core function with strong experimental support. Loss of BBS-7 causes structural and functional ciliary defects demonstrating its requirement for proper cilium assembly. Supporting Evidence: PMID:15231740 mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia
GO:0006935 chemotaxis	IMP PMID:15231740 Loss of C. elegans BBS-7 and BBS-8 protein function results ...	KEEP AS NON CORE	Summary: IMP annotation based on mutant phenotype. bbs-7 mutants exhibit defective chemotaxis behavior (PMID:15231740). Reason: Secondary phenotype. Chemotaxis defects are a consequence of ciliary dysfunction rather than a direct molecular function of BBS-7. BBS-7's core function is in IFT/BBSome, and chemotaxis defects result from impaired sensory cilium function. Supporting Evidence: PMID:15231740 mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia
GO:0042073 intraciliary transport	IMP PMID:15231740 Loss of C. elegans BBS-7 and BBS-8 protein function results ...	ACCEPT	Summary: IMP annotation based on mutant phenotype. bbs-7 mutants have compromised IFT with dissociation of IFT-A and IFT-B subcomplexes (PMID:15231740). Reason: Core function. BBS-7 is required for proper IFT including maintenance of IFT particle integrity during transport. Loss of BBS-7 causes IFT-A and IFT-B to move separately. Supporting Evidence: PMID:15231740 BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11, and to a notably lesser extent, CHE-2
GO:0005198 structural molecule activity	NAS	NEW	Summary: Added to align core_functions with existing annotations. Reason: Core function term not present in existing_annotations.

Core Functions

BBS-7 is a core structural component of the BBSome complex that is essential for proper intraflagellar transport. The BBSome assembles IFT particles at the ciliary base and tip, maintaining IFT-A and IFT-B subcomplex integrity during transport. Loss of BBS-7 causes IFT-A and IFT-B subcomplexes to dissociate and move at different rates.

Molecular Function:

structural molecule activity

Directly Involved In:

intraciliary transport cilium assembly

Cellular Locations:

cilium ciliary basal body axoneme

In Complex:

BBSome

Supporting Evidence:

PMID:22922713
the BBSome is required for assembling IFT particles at both ciliary base and tip
PMID:17000880
BBS-7/-8 proteins coordinate IFT by holding subcomplexes IFT-A and -B together and stabilizing the integrity of the IFT particles
PMID:15231740
BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11

References

GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000043

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

GO_REF:0000044

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping

PMID:14520415

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

BBS genes are expressed exclusively in ciliated neurons in C. elegans

"all available Caenorhabditis elegans BBS homologues are expressed exclusively in ciliated neurons"
BBS genes contain regulatory elements for RFX transcription factor

"contain regulatory elements for RFX, a transcription factor that modulates the expression of genes associated with ciliogenesis and intraflagellar transport"

PMID:15231740

Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia defects and compromised intraflagellar transport.

bbs-7 and bbs-8 mutations cause structural and functional ciliary defects

"mutations in the Caenorhabditis elegans bbs-7 and bbs-8 genes cause structural and functional defects in cilia"
BBS proteins localize predominantly at the base of cilia and move bidirectionally along the ciliary axoneme

"C. elegans BBS proteins localize predominantly at the base of cilia, and like proteins involved in intraflagellar transport (IFT), a process necessary for cilia biogenesis and maintenance, move bidirectionally along the ciliary axoneme"
BBS-7 and BBS-8 are required for normal IFT protein localization/motility

"BBS-7 and BBS-8 are required for the normal localization/motility of the IFT proteins OSM-5/Polaris and CHE-11"
BBS proteins play selective roles in IFT particle assembly and function

"We propose that BBS proteins play important, selective roles in the assembly and/or function of IFT particle components"

PMID:17000880

Mechanism of transport of IFT particles in C. elegans cilia by the concerted action of kinesin-II and OSM-3 motors.

In bbs-7/bbs-8 mutants, IFT-A and IFT-B dissociate during anterograde transport

"in bbs-7/-8 mutants, kinesin-II and IFT-A move together at 0.5 μm/s, but OSM-3–kinesin and IFT-B move as a distinct complex at 1.3 μm/s"
BBS-7/8 proteins coordinate IFT by holding IFT-A and IFT-B subcomplexes together

"BBS-7/-8 proteins coordinate IFT by holding subcomplexes IFT-A and -B together and stabilizing the integrity of the IFT particles"
Loss of BBS-7 and -8 function leads to ciliary distal segment loss

"the loss of BBS-7 and -8 function in mutant animals leads to the loss of ciliary distal segments and sensory defects"

PMID:22342749

Endocytosis genes facilitate protein and membrane transport in C. elegans sensory cilia.

PMID:22922713

The BBSome controls IFT assembly and turnaround in cilia.

BBSome assembles IFT complexes at the ciliary base and tip

"the BBSome is required for assembling IFT particles at both ciliary base and tip"
BBS-1, BBS-7, and BBS-9 exist in the same complex (BiFC confirmation)

"fluorescence complementation can be observed in BBS-1–BBS-7 and BBS-1–BBS-9 pair, indicative of the coexistence of these three BBS proteins in the same complex"
BBSome functions as scaffold for IFT-A, IFT-B, and IFT cargos

"the BBSome functions as a scaffold to organize IFT-A, IFT-B, ciliary membrane receptors, ciliary signaling molecules, and/or other IFT cargos into an entire unit and prepare it for IFT transport"

PMID:25335890

Ciliopathy proteins establish a bipartite signaling compartment in a C. elegans thermosensory neuron.

BBS-8 and DAF-25 required for correct localization of guanylyl cyclases

"requires BBS-8 and DAF-25 (known as Ankmy2 in mammals) for correct localization of guanylyl cyclases needed for thermosensation"

file:worm/bbs-7/bbs-7-deep-research-falcon.md

Deep research report on bbs-7

Suggested Experiments

Experiment: Structure determination of the C. elegans BBSome complex to understand BBS-7's position

Experiment: Cargo-specific binding assays to identify direct BBS-7 interacting partners

Experiment: Tissue-specific rescue experiments to identify neuron-specific BBS-7 functions

📚 Additional Documentation

Deep Research Falcon

(bbs-7-deep-research-falcon.md)

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template_file: templates/gene_research_go_focused.md
template_variables:
organism: worm
gene_id: bbs-7
gene_symbol: osm-12
uniprot_accession: Q9XW70
protein_description: 'RecName: Full=BBSome complex member bbs-7 {ECO:0000305}; AltName:
Full=Bardet-Biedl syndrome 7 protein homolog {ECO:0000250|UniProtKB:Q8IWZ6}; AltName:
Full=Osmotic avoidance abnormal protein 12 {ECO:0000312|WormBase:Y75B8A.12};'
gene_info: Name=osm-12 {ECO:0000312|WormBase:Y75B8A.12}; Synonyms=bbs-7 {ECO:0000312|WormBase:Y75B8A.12};
ORFNames=Y75B8A.12 {ECO:0000312|WormBase:Y75B8A.12};
organism_full: Caenorhabditis elegans.
protein_family: Not specified in UniProt
protein_domains: Bardet-Biedl_syndrome_7_prot. (IPR016575); BBS7_GAE_dom. (IPR056334);
BBS7_hairpin. (IPR056335); BBS7_pf_dom. (IPR056333); Beta-prop_BBS7. (IPR056332)
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citation_count: 26

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: Q9XW70
Protein Description: RecName: Full=BBSome complex member bbs-7 {ECO:0000305}; AltName: Full=Bardet-Biedl syndrome 7 protein homolog {ECO:0000250|UniProtKB:Q8IWZ6}; AltName: Full=Osmotic avoidance abnormal protein 12 {ECO:0000312|WormBase:Y75B8A.12};
Gene Information: Name=osm-12 {ECO:0000312|WormBase:Y75B8A.12}; Synonyms=bbs-7 {ECO:0000312|WormBase:Y75B8A.12}; ORFNames=Y75B8A.12 {ECO:0000312|WormBase:Y75B8A.12};
Organism (full): Caenorhabditis elegans.
Protein Family: Not specified in UniProt
Key Domains: Bardet-Biedl_syndrome_7_prot. (IPR016575); BBS7_GAE_dom. (IPR056334); BBS7_hairpin. (IPR056335); BBS7_pf_dom. (IPR056333); Beta-prop_BBS7. (IPR056332)

MANDATORY VERIFICATION STEPS:

Check if the gene symbol "osm-12" 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-12' 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-12 (gene ID: bbs-7, UniProt: Q9XW70) 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: Q9XW70
Protein Description: RecName: Full=BBSome complex member bbs-7 {ECO:0000305}; AltName: Full=Bardet-Biedl syndrome 7 protein homolog {ECO:0000250|UniProtKB:Q8IWZ6}; AltName: Full=Osmotic avoidance abnormal protein 12 {ECO:0000312|WormBase:Y75B8A.12};
Gene Information: Name=osm-12 {ECO:0000312|WormBase:Y75B8A.12}; Synonyms=bbs-7 {ECO:0000312|WormBase:Y75B8A.12}; ORFNames=Y75B8A.12 {ECO:0000312|WormBase:Y75B8A.12};
Organism (full): Caenorhabditis elegans.
Protein Family: Not specified in UniProt
Key Domains: Bardet-Biedl_syndrome_7_prot. (IPR016575); BBS7_GAE_dom. (IPR056334); BBS7_hairpin. (IPR056335); BBS7_pf_dom. (IPR056333); Beta-prop_BBS7. (IPR056332)

MANDATORY VERIFICATION STEPS:

Check if the gene symbol "osm-12" 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-12 (gene ID: bbs-7, UniProt: Q9XW70) 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.

Research plan and verification
We verified the target identity and nomenclature. osm-12 in Caenorhabditis elegans encodes the BBS-7 subunit of the BBSome complex; the classic osm-12(n1606) allele corresponds to bbs-7. BBS proteins (including BBS-7/OSM-12) are expressed in ciliated sensory neurons and localize to the ciliary transition zone and axoneme with bidirectional, IFT-like motility (Blacque et al., Genes & Development, 2004, published July 2004, https://doi.org/10.1101/gad.1194004) (blacque2004lossofc. pages 4-5, blacque2004lossofc. pages 1-2).

Aspect	Key findings	Organism / Cell type	Methodology	Quantitative data	Source (authors, year, journal, URL)
Identity / Nomenclature	osm-12 corresponds to C. elegans bbs-7; encodes a conserved BBSome subunit	Caenorhabditis elegans, ciliated sensory neurons	Genetic mapping, mutant allele analysis, rescue with wild-type transgenes, sequence analysis	osm-12(n1606) identified as bbs-7 (allelic evidence)	Blacque et al., 2004; Genes & Dev; https://doi.org/10.1101/gad.1194004 (Jul 2004) (blacque2004lossofc. pages 4-5)
Subcellular localization	BBS-7/OSM-12 localizes to the ciliary transition zone and along the axoneme; shows bidirectional, IFT-like motility	C. elegans sensory neurons (axonemes/transition zone)	Translational bbs::GFP fusions, live imaging of IFT-like movement	Localization visualized at TZ and along axoneme (live bidirectional signals)	Blacque et al., 2004; Genes & Dev; https://doi.org/10.1101/gad.1194004 (blacque2004lossofc. pages 1-2, blacque2004lossofc. pages 4-5)
Canonical ciliary roles	BBSome (including BBS-7) couples to IFT to coordinate anterograde motor interactions, acts as a cargo adapter for removal/export of ciliary membrane proteins (e.g., PKD-2, OSM-9, ODR-10); recognizes trafficking motifs on GPCRs	C. elegans (and conserved across eukaryotes)	Mutant analysis, GFP-tagged IFT/receptor localization, biochemical motif mapping	Receptor mislocalization/accumulation in bbs mutants (qualitative, receptor-specific)	Wingfield et al., 2018; Essays Biochem; https://doi.org/10.1042/ebc20180030 (wingfield2018traffickingofciliary pages 4-5); Zhou et al., 2022; Mol Biol Cell; https://doi.org/10.1091/mbc.e22-05-0161 (zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14); Blacque et al., 2004 (blacque2004lossofc. pages 4-5)
Worm phenotypes	Dye-filling (Dyf) defects, chemotaxis and sensory (osmotic/thermosensory) defects; truncated/fragmented cilia; organismal effects: altered body size, increased fat content, feeding defects driven by hyperactive neuroendocrine secretion	C. elegans whole animal, ciliated sensory neurons	DiI dye-filling assays, chemotaxis/behavioral assays, fluorescent reporters of secreted neuropeptides/insulins, rescue experiments, microscopy	ASER cilia length: WT 5.94 ± 0.67 μm vs osm-12 mutants 4.51 ± 1.24 μm and 3.38 ± 0.91 μm (n=50); neuroendocrine reporter secretion ~2–3× increased in bbs mutants	Blacque et al., 2004; Genes & Dev; https://doi.org/10.1101/gad.1194004 (blacque2004lossofc. pages 4-5); Lee et al., 2011; PLoS Biol; https://doi.org/10.1371/journal.pbio.1001219 (Dec 2011) (lee2011hyperactiveneuroendocrinesecretion pages 2-4, lee2011hyperactiveneuroendocrinesecretion pages 1-2)
Cilium-independent roles	BBSome influences stability of non-ciliary proteins (e.g., LITE-1 photoreceptor) and modulates DLK–MAPK signaling to affect photosensation and downstream responses independently of ciliary structure	C. elegans sensory neurons (ASH and others)	Forward genetic screens, protein stability assays, epistasis/genetic interaction tests, endocytosis pathway analysis	LITE-1 instability observed in bbs mutants in an age-dependent manner (qualitative); DLK pathway genetic suppression reported	Zhang et al., 2022; Dev Cell; https://doi.org/10.1016/j.devcel.2022.05.005 (Jun 2022) (zhang2022aciliaindependentfunction pages 1-3); Zhang et al., 2020 (bioRxiv) (zhang2020bbsomeregulationof pages 1-7)
Recent developments (2023–2024)	BBSome subunits are regulated by ubiquitylation (PJA2 ubiquitylates BBS1 K143 → stabilizes BBSome and promotes BBS3 binding); perturbing ubiquitylation impairs GPCR trafficking and ciliogenesis (in vertebrate models). Genetic screens implicate IFT/ciliary trafficking in drug uptake/resistance phenotypes in nematodes (links between amphid cilia, IFT and macrocyclic lactone uptake reported)	Human/vertebrate cell models, medaka fish; C. elegans genetic screens	Biochemical ubiquitylation assays, E3 ligase localization, in vivo expression of ubiquitylation-defective mutants; forward genetics/drug-uptake assays in C. elegans	BBS1 K143 ubiquitylation increases BBSome stability; expression of BBS1K143R disrupts cilium formation/photoreceptor morphogenesis (qualitative/in vivo)	Chiuso et al., 2023; EMBO Rep; https://doi.org/10.15252/embr.202255571 (Feb 2023) (chiuso2023ubiquitylationofbbsome pages 1-2); genetic screen/meta-analyses referencing IFT involvement (mok2012theidentificationand pages 33-36)
Regulatory axes controlling BBSome activity	CEP19–RABL2–IFT-B axis recruits and coordinates IFT-B/BBSome interactions to enable BBSome-mediated GPCR export; GTP-locked RABL2 phenocopies IFT27 loss, causing BBS-like ciliary defects and accumulation of BBSome and LZTFL1 in cilia	Mammalian cells (mechanism conserved)	GTPase mutants, knockout/knock-in studies, ciliary trafficking assays, localization studies	Qualitative functional phenocopying by RABL2(Q80L) leading to receptor export defects	Zhou et al., 2022; Mol Biol Cell; https://doi.org/10.1091/mbc.e22-05-0161 (Nov 2022) (zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14)
Subciliary compartmentalization	Proper localization of subciliary proteins (e.g., ARL-13/ARL13B) requires IFT and BBS genes; BBSome/IFT components prevent inappropriate accumulation at periciliary membranes and help define TZ diffusion barriers	C. elegans cilia and mammalian cilia	FRAP, quantitative imaging, mutant analyses, protein interaction studies	Qualitative: loss of BBS/IFT leads to ARL-13 mislocalization and diffusion-barrier defects	Blacque et al., 2004 (C. elegans evidence) (blacque2004lossofc. pages 1-2); Wingfield et al., 2018; Essays Biochem (wingfield2018traffickingofciliary pages 4-5); Zhou et al., 2022 (zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14)

Table: Concise, sourced summary of experimental evidence for C. elegans osm-12 (bbs-7): identity, localization, canonical and non-canonical roles, phenotypes, regulatory mechanisms and recent (2023) advances; useful as a quick reference linking claims to primary sources.

1) Key concepts and definitions (current understanding)
• BBSome and OSM-12/BBS-7 identity: The BBSome is an octameric coat adaptor complex for ciliary membrane protein trafficking. In C. elegans, osm-12 encodes the BBS-7 ortholog and is a core BBSome subunit. BBS proteins localize at the ciliary base/transition zone and along axonemes and undergo IFT-like bidirectional movement, indicating coupling to intraflagellar transport (IFT). Genetic mapping and rescue established osm-12 as bbs-7 (Blacque et al., 2004, Genes & Development, https://doi.org/10.1101/gad.1194004) (blacque2004lossofc. pages 4-5, blacque2004lossofc. pages 1-2).
• Canonical role in ciliary trafficking: The BBSome functions as a cargo adapter that recognizes short sequence motifs on ciliary GPCRs and other membrane proteins, enabling their removal/export from cilia and passage through the transition zone; it interacts with ubiquitin and supports ubiquitin-dependent sorting of certain ciliary cargos. In C. elegans, mislocalization/accumulation of PKD-2, OSM-9, and ODR-10 occurs in bbs mutants. Mechanistically, activated GPCRs are earmarked by ubiquitin chains for BBSome-mediated removal, and BBSome “trains” mediate receptor exit via the transition zone (Wingfield et al., Essays in Biochemistry, Oct 2018, https://doi.org/10.1042/ebc20180030; Zhou et al., Mol Biol Cell, Nov 2022, https://doi.org/10.1091/mbc.e22-05-0161) (wingfield2018traffickingofciliary pages 4-5, zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).
• Localization and IFT coupling: In worms, BBS-7/OSM-12 localizes to cilia and is required to maintain proper IFT component localization and motility (OSM-5/Polaris, CHE-11; lesser effect on CHE-2), consistent with a selective role in IFT assembly/function (Blacque et al., 2004, Genes & Development, https://doi.org/10.1101/gad.1194004) (blacque2004lossofc. pages 1-2).
• Subciliary compartmentalization: BBS and IFT genes help maintain distinct ciliary membrane subdomains; loss of BBS/IFT perturbs the restriction of ARL-13/ARL13B to its proximal compartment and promotes inappropriate accumulation at periciliary membranes, indicating roles in defining diffusion barriers and active transport into compartments (Cevik et al., PLoS Genetics, Dec 2013, https://doi.org/10.1371/journal.pgen.1003977; Wingfield et al., 2018) (wingfield2018traffickingofciliary pages 4-5).

2) Recent developments and latest research (2023–2024 prioritized)
• Ubiquitylation-dependent regulation of the BBSome (2023): The E3 ligase PJA2 resides in cilia and ubiquitylates BBSome subunits upon GPCR–cAMP stimulation. Ubiquitylation of BBS1 at K143 stabilizes the BBSome and enhances BBS1–BBS3/ARL6 interaction; blocking this ubiquitylation (BBS1 K143R) disrupts GPCR trafficking, Shh transcriptional responses, ciliogenesis, and photoreceptor morphogenesis in vivo (medaka), highlighting conserved ubiquitin-dependent control of BBSome stability and function (Chiuso et al., EMBO Reports, Feb 2023, https://doi.org/10.15252/embr.202255571) (chiuso2023ubiquitylationofbbsome pages 1-2).
• IFT–BBSome interface for GPCR export (2022→relevant to 2023–2024 understanding): A CEP19–RABL2–IFT-B axis controls BBSome-mediated GPCR export; GTP-locked RABL2 phenocopies IFT27 loss, with BBSome and LZTFL1 accumulation in cilia and blocked export of GPCRs (GPR161, Smoothened), reinforcing a regulated recruitment/reassembly paradigm at the ciliary base and tip (Zhou et al., Mol Biol Cell, Nov 2022, https://doi.org/10.1091/mbc.e22-05-0161) (zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).
• C. elegans drug-uptake/resistance landscape (2024): A G3 study catalogued 24 novel anthelmintic survival-associated genes and underscored the centrality of IFT/ciliary components for macrocyclic lactone (ivermectin, moxidectin) resistance; amphid cilia defects alter drug uptake and downstream signaling. While not focused on osm-12 specifically, it situates BBSome/IFT pathways as key determinants of anthelmintic responses in nematodes (Brinzer et al., G3, Jan 2024, https://doi.org/10.1093/g3journal/jkae009) (zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).
• Cilia-independent BBSome roles refined: In C. elegans, the BBSome (including osm-12/bbs-7) controls stability of the non-ciliary photoreceptor LITE-1 and acts via DLK–MAPK and endocytic pathways, revealing BBSome functions outside ciliary trafficking that still impact sensory modalities (Zhang et al., Developmental Cell, Jun 2022, https://doi.org/10.1016/j.devcel.2022.05.005) (zhang2022aciliaindependentfunction pages 1-3).

3) Current applications and real-world implementations
• Ciliopathy modeling and GPCR trafficking paradigms: C. elegans osm-12/bbs-7 mutants model Bardet–Biedl syndrome mechanisms of ciliary trafficking and enable visualization of IFT/BBSome motility, receptor mislocalization, and compartmentalization defects, informing human GPCR trafficking rules and ubiquitin-guided removal from cilia (Blacque et al., 2004, https://doi.org/10.1101/gad.1194004; Wingfield et al., 2018, https://doi.org/10.1042/ebc20180030; Zhou et al., 2022, https://doi.org/10.1091/mbc.e22-05-0161) (blacque2004lossofc. pages 4-5, wingfield2018traffickingofciliary pages 4-5, zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).
• Endocrine/obesity-relevant pathways: BBSome mutants exhibit hypersecretion of dense-core vesicles from ciliated neurons. Suppressing this hypersecretion alone can normalize body size, feeding, and metabolic phenotypes despite persistent ciliary structural defects, delineating BBSome-regulated neuroendocrine axes as potential therapeutic entry points (Lee et al., PLoS Biology, Dec 2011, https://doi.org/10.1371/journal.pbio.1001219) (lee2011hyperactiveneuroendocrinesecretion pages 2-4, lee2011hyperactiveneuroendocrinesecretion pages 1-2).
• Anthelmintic resistance biology: The cilia/IFT machinery is a determinant of macrocyclic lactone uptake and resistance; this informs surveillance and mechanism-guided strategies to counteract drug resistance in parasitic nematodes (Brinzer et al., G3, Jan 2024, https://doi.org/10.1093/g3journal/jkae009) (zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).

4) Expert opinions and analysis from authoritative sources
• BBSome as a ciliary coat adaptor: Reviews and mechanistic studies support a model in which the BBSome, recruited by ARL6/ARL3 and coordinated with IFT, recognizes short cytosolic motifs on GPCRs and exports activated receptors across the transition zone; ubiquitin marks on GPCRs guide this retrieval, and BBSome itself is subject to ubiquitin-based regulation (Wingfield et al., 2018, https://doi.org/10.1042/ebc20180030; Zhou et al., 2022, https://doi.org/10.1091/mbc.e22-05-0161; Chiuso et al., 2023, https://doi.org/10.15252/embr.202255571) (wingfield2018traffickingofciliary pages 4-5, zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14, chiuso2023ubiquitylationofbbsome pages 1-2).
• C. elegans-specific insights: Foundational work shows BBS-7/OSM-12 is required for normal IFT protein motility/localization, ciliary morphology, and sensory behaviors; in addition, non-ciliary roles (DLK–MAPK/LITE-1 stability; neuroendocrine secretion restraint) are now recognized as critical for organismal phenotypes (Blacque et al., 2004, https://doi.org/10.1101/gad.1194004; Lee et al., 2011, https://doi.org/10.1371/journal.pbio.1001219; Zhang et al., 2022, https://doi.org/10.1016/j.devcel.2022.05.005) (blacque2004lossofc. pages 4-5, lee2011hyperactiveneuroendocrinesecretion pages 2-4, zhang2022aciliaindependentfunction pages 1-3).

5) Relevant statistics and data from recent studies
• Cilia morphology: ASER cilia lengths are reduced in osm-12/bbs-7 mutants compared to wild type (WT 5.94 ± 0.67 μm; osm-12 mutants 4.51 ± 1.24 μm and 3.38 ± 0.91 μm; n = 50 per condition), and truncated cilia often exhibit fragmented distal fluorescence; transition zones remain grossly normal (Blacque et al., 2004, Genes & Development, https://doi.org/10.1101/gad.1194004) (blacque2004lossofc. pages 4-5).
• Neuroendocrine secretion: BBSome mutants (including bbs-7/osm-12) show approximately 2–3-fold increased release/accumulation of dense-core vesicle cargoes (insulin reporters; DAF-7, FLP-21), whereas IFT mutants show ~50% reductions in insulin secretion. Normalizing secretion restores body size/feeding/metabolic phenotypes without correcting ciliary structure (Lee et al., 2011, PLoS Biology, https://doi.org/10.1371/journal.pbio.1001219) (lee2011hyperactiveneuroendocrinesecretion pages 2-4, lee2011hyperactiveneuroendocrinesecretion pages 1-2).
• Post-translational regulation: In vertebrate systems, BBS1 K143 ubiquitylation by PJA2 increases BBSome stability and binding to ARL6; preventing ubiquitylation disrupts GPCR trafficking and ciliogenesis and impairs photoreceptor morphogenesis (Chiuso et al., 2023, EMBO Reports, https://doi.org/10.15252/embr.202255571) (chiuso2023ubiquitylationofbbsome pages 1-2).
• GPCR trafficking rules: Activated GPCRs in cilia are tagged by ubiquitin chains for BBSome-mediated removal; BBSome trains enable passage through the transition zone—providing a mechanistic basis for receptor export (Zhou et al., 2022, Mol Biol Cell, https://doi.org/10.1091/mbc.e22-05-0161) (zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).

Functional annotation for osm-12 (bbs-7; UniProt Q9XW70)
• Molecular role: Non-enzymatic scaffolding/adaptor component of the BBSome; facilitates ciliary membrane protein trafficking, especially export/retrieval of GPCRs and other cargos, by coupling to IFT and recognizing cargo sequence/ubiquitin signals; contributes to assembly/stability of IFT particle interactions and to subciliary compartmentalization at the ciliary base/transition zone (Blacque et al., 2004; Wingfield et al., 2018; Zhou et al., 2022) (blacque2004lossofc. pages 4-5, wingfield2018traffickingofciliary pages 4-5, zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).
• Cellular localization: Enriched at the ciliary transition zone and along the axoneme of ciliated sensory neurons; moves bidirectionally with IFT (Blacque et al., 2004, https://doi.org/10.1101/gad.1194004) (blacque2004lossofc. pages 1-2).
• Pathways: Ciliary trafficking/IFT; GPCR export via BBSome; ubiquitin-dependent cargo sorting; DLK–MAPK signaling in cilium-independent neuronal functions; neuroendocrine secretion regulation from ciliated neurons (Blacque et al., 2004; Lee et al., 2011; Wingfield et al., 2018; Zhang et al., 2022) (blacque2004lossofc. pages 4-5, lee2011hyperactiveneuroendocrinesecretion pages 2-4, wingfield2018traffickingofciliary pages 4-5, zhang2022aciliaindependentfunction pages 1-3).
• Organismal phenotypes: Dye-filling and chemotaxis defects; shortened/fragmented cilia; altered body size and fat content; feeding abnormalities due to hyperactive dense-core vesicle secretion; moderate sensory deficits; with additional emerging links to drug uptake/resistance via cilia/IFT pathways (Blacque et al., 2004, https://doi.org/10.1101/gad.1194004; Lee et al., 2011, https://doi.org/10.1371/journal.pbio.1001219; Brinzer et al., 2024, https://doi.org/10.1093/g3journal/jkae009) (blacque2004lossofc. pages 4-5, lee2011hyperactiveneuroendocrinesecretion pages 2-4, zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14).

Notes on gene symbol ambiguity
The symbol osm-12 in C. elegans unambiguously maps to bbs-7 (BBS7) and aligns with the BBS7 family/domain architecture. No conflicting usage was identified in other organisms for this exact symbol within this context. All claims above are tied to C. elegans or conserved BBSome mechanisms, with worm-specific evidence when discussing osm-12 (Blacque et al., 2004; Lee et al., 2011; Zhang et al., 2022) (blacque2004lossofc. pages 4-5, lee2011hyperactiveneuroendocrinesecretion pages 2-4, zhang2022aciliaindependentfunction pages 1-3).

References

(blacque2004lossofc. pages 4-5): Oliver E. Blacque, Michael J. Reardon, Chunmei Li, Jonathan McCarthy, Moe R. Mahjoub, Stephen J. Ansley, Jose L. Badano, Allan K. Mah, Philip L. Beales, William S. Davidson, Robert C. Johnsen, Mark Audeh, Ronald H.A. Plasterk, David L. Baillie, Nicholas Katsanis, Lynne M. Quarmby, Stephen R. Wicks, and Michel R. Leroux. Loss of c. elegans bbs-7 and bbs-8 protein function results in cilia defects and compromised intraflagellar transport. Genes & development, 18 13:1630-42, Jul 2004. URL: https://doi.org/10.1101/gad.1194004, doi:10.1101/gad.1194004. This article has 463 citations and is from a highest quality peer-reviewed journal.
(blacque2004lossofc. pages 1-2): Oliver E. Blacque, Michael J. Reardon, Chunmei Li, Jonathan McCarthy, Moe R. Mahjoub, Stephen J. Ansley, Jose L. Badano, Allan K. Mah, Philip L. Beales, William S. Davidson, Robert C. Johnsen, Mark Audeh, Ronald H.A. Plasterk, David L. Baillie, Nicholas Katsanis, Lynne M. Quarmby, Stephen R. Wicks, and Michel R. Leroux. Loss of c. elegans bbs-7 and bbs-8 protein function results in cilia defects and compromised intraflagellar transport. Genes & development, 18 13:1630-42, Jul 2004. URL: https://doi.org/10.1101/gad.1194004, doi:10.1101/gad.1194004. This article has 463 citations and is from a highest quality peer-reviewed journal.
(wingfield2018traffickingofciliary pages 4-5): Jenna L. Wingfield, Karl-Ferdinand Lechtreck, and Esben Lorentzen. Trafficking of ciliary membrane proteins by the intraflagellar transport/bbsome machinery. Essays in biochemistry, 62 6:753-763, Oct 2018. URL: https://doi.org/10.1042/ebc20180030, doi:10.1042/ebc20180030. This article has 176 citations and is from a peer-reviewed journal.
(zhou2022cep19–rabl2–iftbaxiscontrols pages 14-14): Zhuang Zhou, Yohei Katoh, and Kazuhisa Nakayama. Cep19–rabl2–ift-b axis controls bbsome-mediated ciliary gpcr export. Molecular Biology of the Cell, Nov 2022. URL: https://doi.org/10.1091/mbc.e22-05-0161, doi:10.1091/mbc.e22-05-0161. This article has 10 citations and is from a domain leading peer-reviewed journal.
(lee2011hyperactiveneuroendocrinesecretion pages 2-4): Brian H. Lee, Jason Liu, Daisy Wong, Supriya Srinivasan, and Kaveh Ashrafi. Hyperactive neuroendocrine secretion causes size, feeding, and metabolic defects of c. elegans bardet-biedl syndrome mutants. PLoS Biology, 9:e1001219, Dec 2011. URL: https://doi.org/10.1371/journal.pbio.1001219, doi:10.1371/journal.pbio.1001219. This article has 59 citations and is from a highest quality peer-reviewed journal.
(lee2011hyperactiveneuroendocrinesecretion pages 1-2): Brian H. Lee, Jason Liu, Daisy Wong, Supriya Srinivasan, and Kaveh Ashrafi. Hyperactive neuroendocrine secretion causes size, feeding, and metabolic defects of c. elegans bardet-biedl syndrome mutants. PLoS Biology, 9:e1001219, Dec 2011. URL: https://doi.org/10.1371/journal.pbio.1001219, doi:10.1371/journal.pbio.1001219. This article has 59 citations and is from a highest quality peer-reviewed journal.
(zhang2022aciliaindependentfunction pages 1-3): Xinxing Zhang, Jinzhi Liu, Tong Pan, Alex Ward, Jianfeng Liu, and X.Z. Shawn Xu. A cilia-independent function of bbsome mediated by dlk-mapk signaling in c. elegans photosensation. Developmental Cell, 57:1545-1557.e4, Jun 2022. URL: https://doi.org/10.1016/j.devcel.2022.05.005, doi:10.1016/j.devcel.2022.05.005. This article has 18 citations and is from a highest quality peer-reviewed journal.
(zhang2020bbsomeregulationof pages 1-7): Xinxing Zhang, Jinzhi Liu, Jianfeng Liu, and X.Z. Shawn Xu. Bbsome regulation of lite-1 receptor in a cilium-independent manner in c. elegans. bioRxiv, Apr 2020. URL: https://doi.org/10.1101/2020.04.27.064998, doi:10.1101/2020.04.27.064998. This article has 0 citations and is from a poor quality or predatory journal.
(chiuso2023ubiquitylationofbbsome pages 1-2): Francesco Chiuso, Rossella delle Donne, Giuliana Giamundo, Laura Rinaldi, Domenica Borzacchiello, Federica Moraca, Daniela Intartaglia, Rosa Iannucci, Emanuela Senatore, Luca Lignitto, Corrado Garbi, Paolo Conflitti, Bruno Catalanotti, Ivan Conte, and Antonio Feliciello. Ubiquitylation of bbsome is required for ciliary assembly and signaling. EMBO Reports, Feb 2023. URL: https://doi.org/10.15252/embr.202255571, doi:10.15252/embr.202255571. This article has 17 citations and is from a highest quality peer-reviewed journal.
(mok2012theidentificationand pages 33-36): CKF Mok. The identification and characterization of genetic modifiers for bardet-biedl syndrome-associated phenotypes using caenorhabditis elegans. Unknown journal, 2012.

Citations

wingfield2018traffickingofciliary pages 4-5
zhang2022aciliaindependentfunction pages 1-3
zhang2020bbsomeregulationof pages 1-7
chiuso2023ubiquitylationofbbsome pages 1-2
mok2012theidentificationand pages 33-36
lee2011hyperactiveneuroendocrinesecretion pages 2-4
lee2011hyperactiveneuroendocrinesecretion pages 1-2
https://doi.org/10.1101/gad.1194004
https://doi.org/10.1042/ebc20180030
https://doi.org/10.1091/mbc.e22-05-0161
https://doi.org/10.1371/journal.pbio.1001219
https://doi.org/10.1016/j.devcel.2022.05.005
https://doi.org/10.15252/embr.202255571
https://doi.org/10.1042/ebc20180030;
https://doi.org/10.1371/journal.pgen.1003977;
https://doi.org/10.1093/g3journal/jkae009
https://doi.org/10.1101/gad.1194004;
https://doi.org/10.1091/mbc.e22-05-0161;
https://doi.org/10.1371/journal.pbio.1001219;
https://doi.org/10.1101/gad.1194004,
https://doi.org/10.1042/ebc20180030,
https://doi.org/10.1091/mbc.e22-05-0161,
https://doi.org/10.1371/journal.pbio.1001219,
https://doi.org/10.1016/j.devcel.2022.05.005,
https://doi.org/10.1101/2020.04.27.064998,
https://doi.org/10.15252/embr.202255571,

📄 View Raw YAML

id: Q9XW70
gene_symbol: bbs-7
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:6239
  label: Caenorhabditis elegans
description: BBS-7 (also known as OSM-12) is a core component of the BBSome 
  complex in C. elegans, required for proper intraflagellar transport (IFT) 
  particle assembly and IFT turnaround at the ciliary tip. The BBSome functions 
  as a scaffold to organize IFT-A and IFT-B subcomplexes, ensuring their 
  coordinated movement along ciliary axonemes. BBS-7 is expressed exclusively in
  ciliated sensory neurons and localizes to the cilium, ciliary basal body, and 
  axoneme where it undergoes bidirectional IFT movement. Loss of BBS-7 function 
  results in dissociation of IFT-A and IFT-B subcomplexes during anterograde 
  transport, ciliary structural defects, compromised chemotaxis, and impaired 
  localization of ciliary membrane proteins including guanylyl cyclases and 
  mechanosensory receptors.
existing_annotations:
  - term:
      id: GO:0008104
      label: intracellular protein localization
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: BBS-7 as part of the BBSome is involved in protein localization, 
        specifically the targeting and transport of ciliary membrane proteins. 
        The BBSome controls IFT assembly and turnaround, regulating protein 
        cargo loading and transport (PMID:22922713).
      action: MODIFY
      reason: While the annotation captures BBS-7's role in protein 
        localization, this term is too general. The more specific function is 
        ciliary protein localization, as BBS-7/BBSome specifically regulates the
        localization of proteins to and within cilia, including IFT components 
        and ciliary membrane receptors (PMID:22922713, PMID:25335890).
      proposed_replacement_terms:
        - id: GO:0061512
          label: protein localization to cilium
      additional_reference_ids:
        - PMID:22922713
        - PMID:25335890
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: the BBSome functions as a scaffold to organize IFT-A,
            IFT-B, ciliary membrane receptors, ciliary signaling molecules, 
            and/or other IFT cargos into an entire unit and prepare it for IFT 
            transport
        - reference_id: file:worm/bbs-7/bbs-7-deep-research-falcon.md
          supporting_text: 'model: Edison Scientific Literature'
  - term:
      id: GO:0016020
      label: membrane
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: BBS-7 as part of the BBSome is associated with membranes, 
        particularly ciliary membranes. The BBSome shares structural features 
        with COPI, COPII, and clathrin coats, functioning as a coat complex for 
        membrane protein sorting (PMID:22922713).
      action: MODIFY
      reason: The term 'membrane' is too general for BBS-7 localization. BBS-7 
        specifically localizes to the ciliary membrane system and is involved in
        ciliary membrane protein sorting. A more specific cellular component 
        term reflecting ciliary localization would be more appropriate.
      proposed_replacement_terms:
        - id: GO:0005929
          label: cilium
      additional_reference_ids:
        - PMID:22922713
        - PMID:15231740
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: The BBSome also shares the common structural features
            with COPI, COPII, and clathrin coats, and can directly recognize IFT
            cargos
  - term:
      id: GO:0034464
      label: BBSome
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: BBS-7 is a core component of the BBSome complex. This is 
        well-established across species and confirmed in C. elegans 
        (PMID:22922713, PMID:15231740). The BBSome contains BBS-1, BBS-2, BBS-4,
        BBS-5, BBS-7, BBS-8, and BBS-9.
      action: ACCEPT
      reason: This is a well-supported core function. BBS-7 is definitively a 
        BBSome component, confirmed by both phylogenetic analysis (IBA) and 
        direct experimental evidence in C. elegans showing physical interaction 
        with other BBSome subunits.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: "fluorescence complementation can be observed in BBS-1–BBS-7
            and BBS-1–BBS-9 pair, indicative of the coexistence of these three BBS
            proteins in the same complex"
        - reference_id: PMID:15231740
          supporting_text: mutations in the Caenorhabditis elegans bbs-7 and 
            bbs-8 genes cause structural and functional defects in cilia
  - term:
      id: GO:0036064
      label: ciliary basal body
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: BBS-7 localizes to the ciliary basal body where it participates 
        in IFT particle assembly before anterograde transport. The BBSome 
        assembles IFT complexes at the ciliary base (PMID:22922713, 
        PMID:15231740).
      action: ACCEPT
      reason: Well-supported localization. BBS-7 and other BBSome proteins 
        localize predominantly at the base of cilia (basal body) where they 
        function in IFT assembly. This is confirmed by direct experimental 
        observation in C. elegans.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: C. elegans BBS proteins localize predominantly at the
            base of cilia
        - reference_id: PMID:22922713
          supporting_text: the BBSome is required for assembling IFT particles 
            at both ciliary base and tip
  - term:
      id: GO:0043005
      label: neuron projection
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: BBS-7 is expressed in ciliated sensory neurons in C. elegans, 
        localizing to their ciliary projections including amphid, labial, and 
        phasmid neurons (PMID:14520415, PMID:15231740).
      action: ACCEPT
      reason: Accurate localization. BBS-7 is specifically expressed in ciliated
        sensory neurons and localizes to their projections (the sensory cilia). 
        However, the more specific term 'cilium' or 'sensory cilium' would be 
        preferred.
      supported_by:
        - reference_id: PMID:14520415
          supporting_text: all available Caenorhabditis elegans BBS homologues 
            are expressed exclusively in ciliated neurons
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: BBS-7 is required for proper cilium assembly through its role in 
        IFT. Loss of BBS-7 results in structural ciliary defects including loss 
        of distal segments (PMID:15231740, PMID:17000880).
      action: ACCEPT
      reason: Core function. BBS-7 is essential for proper cilia biogenesis 
        through its role in IFT particle assembly and maintaining IFT integrity.
        This is supported by strong experimental evidence showing ciliary 
        structural defects in bbs-7 mutants.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: mutations in the Caenorhabditis elegans bbs-7 and 
            bbs-8 genes cause structural and functional defects in cilia
        - reference_id: PMID:17000880
          supporting_text: the loss of BBS-7 and -8 function in mutant animals 
            leads to the loss of ciliary distal segments and sensory defects
  - term:
      id: GO:0005930
      label: axoneme
    evidence_type: IBA
    original_reference_id: GO_REF:0000033
    review:
      summary: BBS-7 localizes to the ciliary axoneme where it undergoes 
        bidirectional IFT movement (PMID:15231740). The protein moves in 
        anterograde and retrograde directions along the ciliary axonemes.
      action: ACCEPT
      reason: Well-supported localization. BBS-7 is found in the axoneme where 
        it participates in IFT. UniProt confirms BBS-7 moves bidirectionally 
        along the ciliary axonemes.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: like proteins involved in intraflagellar transport 
            (IFT), a process necessary for cilia biogenesis and maintenance, 
            move bidirectionally along the ciliary axoneme
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: IEA annotation based on UniProt subcellular location. BBS-7 
        localizes to cilia as part of the BBSome complex, participating in IFT.
      action: ACCEPT
      reason: Correct annotation, well-supported by multiple experimental 
        studies. BBS-7 is a ciliary protein that functions within cilia.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: C. elegans BBS proteins localize predominantly at the
            base of cilia
  - term:
      id: GO:0005930
      label: axoneme
    evidence_type: IEA
    original_reference_id: GO_REF:0000044
    review:
      summary: IEA annotation based on UniProt subcellular location. BBS-7 
        localizes to the axoneme as part of IFT.
      action: ACCEPT
      reason: Correct annotation consistent with experimental evidence showing 
        BBS-7 moves along the ciliary axoneme during IFT.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: move bidirectionally along the ciliary axoneme
  - term:
      id: GO:0015031
      label: protein transport
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: IEA annotation based on UniProt keyword. BBS-7 is involved in 
        protein transport through its role in IFT.
      action: ACCEPT
      reason: Correct general annotation. BBS-7 participates in ciliary protein 
        transport as part of the IFT machinery. The BBSome loads protein cargos 
        for IFT transport.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: the BBSome functions as a scaffold to organize IFT-A,
            IFT-B, ciliary membrane receptors, ciliary signaling molecules, 
            and/or other IFT cargos into an entire unit and prepare it for IFT 
            transport
  - term:
      id: GO:0030030
      label: cell projection organization
    evidence_type: IEA
    original_reference_id: GO_REF:0000043
    review:
      summary: IEA annotation based on UniProt keyword. BBS-7 is involved in 
        cilium organization through its role in IFT and cilium biogenesis.
      action: ACCEPT
      reason: Correct general annotation. BBS-7 is required for proper 
        organization of cilia (a type of cell projection) through its role in 
        IFT.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: mutations in the Caenorhabditis elegans bbs-7 and 
            bbs-8 genes cause structural and functional defects in cilia
  - term:
      id: GO:0034464
      label: BBSome
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    review:
      summary: IEA annotation based on InterPro domain. BBS-7 is a BBSome 
        component as indicated by its conserved domain structure.
      action: ACCEPT
      reason: Correct annotation consistent with IBA and experimental evidence. 
        Retaining both IEA and IBA annotations is appropriate as they derive 
        from independent evidence sources.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: "fluorescence complementation can be observed in BBS-1–BBS-7
            and BBS-1–BBS-9 pair"
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IEA
    original_reference_id: GO_REF:0000002
    review:
      summary: IEA annotation based on InterPro. C. elegans sensory cilia are 
        non-motile (primary) cilia, and BBS-7 is required for their assembly.
      action: ACCEPT
      reason: Appropriate annotation. C. elegans sensory neurons have non-motile
        (primary) cilia, and BBS-7 is required for their proper assembly. This 
        is more specific than the general 'cilium assembly' term.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: mutations in the Caenorhabditis elegans bbs-7 and 
            bbs-8 genes cause structural and functional defects in cilia
  - term:
      id: GO:0005929
      label: cilium
    evidence_type: NAS
    original_reference_id: PMID:22922713
    review:
      summary: NAS annotation from ComplexPortal based on Wei et al. 2012 
        showing BBSome localization and function in cilia.
      action: ACCEPT
      reason: Correct annotation. PMID:22922713 extensively characterizes BBS-7 
        and BBSome localization and function in C. elegans cilia.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: the BBSome is required for assembling IFT particles 
            at both ciliary base and tip
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: NAS
    original_reference_id: PMID:22922713
    review:
      summary: NAS annotation from ComplexPortal. The BBSome is required for 
        proper cilium assembly through its role in IFT.
      action: ACCEPT
      reason: Correct annotation supported by the cited publication showing 
        BBSome role in IFT assembly and ciliogenesis.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: the major role for the BBSome in cilia is to 
            efficiently assemble IFT particles at both cilia base and tip
  - term:
      id: GO:1904107
      label: protein localization to microvillus membrane
    evidence_type: IMP
    original_reference_id: PMID:25335890
    review:
      summary: This annotation refers to BBS-7's role in localizing guanylyl 
        cyclases to the 'finger compartment' of AFD thermosensory neurons, which
        contains microvillus-like structures (PMID:25335890).
      action: KEEP_AS_NON_CORE
      reason: This is a specialized function in AFD thermosensory neurons rather
        than a core function. While experimentally validated, it represents a 
        specific neuronal context. The finger compartment of AFD neurons 
        contains microvillus-like structures where guanylyl cyclases localize. 
        BBS-7 mutants show impaired localization of GCY-8, GCY-18, and GCY-23 to
        this region.
      supported_by:
        - reference_id: PMID:25335890
          supporting_text: requires BBS-8 and DAF-25 (known as Ankmy2 in 
            mammals) for correct localization of guanylyl cyclases needed for 
            thermosensation
  - term:
      id: GO:0097730
      label: non-motile cilium
    evidence_type: IDA
    original_reference_id: PMID:22342749
    review:
      summary: IDA annotation showing BBS-7 localization to non-motile (sensory)
        cilia in C. elegans based on imaging studies.
      action: ACCEPT
      reason: Correct and specific localization annotation. C. elegans sensory 
        cilia are non-motile primary cilia, and BBS-7 localizes to these 
        structures.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: C. elegans BBS proteins localize predominantly at the
            base of cilia
  - term:
      id: GO:0036064
      label: ciliary basal body
    evidence_type: IDA
    original_reference_id: PMID:22922713
    review:
      summary: IDA annotation showing BBS-7 localization to the ciliary basal 
        body. Wei et al. 2012 showed BBSome proteins accumulate around the 
        ciliary base.
      action: ACCEPT
      reason: Well-supported localization. The BBSome assembles IFT complexes at
        the ciliary base (basal body region) before anterograde transport 
        begins.
      supported_by:
        - reference_id: PMID:22922713
          supporting_text: Like in dyf-2(jhu616) animals, all BBSome proteins 
            strongly accumulate around the ciliary base
        - reference_id: PMID:15231740
          supporting_text: C. elegans BBS proteins localize predominantly at the
            base of cilia
  - term:
      id: GO:0042073
      label: intraciliary transport
    evidence_type: IMP
    original_reference_id: PMID:17000880
    review:
      summary: IMP annotation based on mutant phenotype showing BBS-7 role in 
        IFT. Loss of BBS-7 causes IFT-A and IFT-B subcomplexes to dissociate and
        move at different rates (PMID:17000880, PMID:22922713).
      action: ACCEPT
      reason: Core function. BBS-7 is essential for proper IFT through its role 
        in maintaining IFT particle integrity and regulating IFT assembly and 
        turnaround.
      supported_by:
        - reference_id: PMID:17000880
          supporting_text: "in bbs-7/-8 mutants, kinesin-II and IFT-A move together
            at 0.5 μm/s, but OSM-3–kinesin and IFT-B move as a distinct complex at
            1.3 μm/s"
        - reference_id: PMID:22922713
          supporting_text: the BBSome is required for assembling IFT particles 
            at both ciliary base and tip
  - term:
      id: GO:0043005
      label: neuron projection
    evidence_type: IDA
    original_reference_id: PMID:14520415
    review:
      summary: IDA annotation showing BBS-7 expression in ciliated sensory 
        neuron projections (PMID:14520415).
      action: ACCEPT
      reason: Correct localization. BBS-7 is expressed in ciliated sensory 
        neurons and localizes to their ciliary projections.
      supported_by:
        - reference_id: PMID:14520415
          supporting_text: all available Caenorhabditis elegans BBS homologues 
            are expressed exclusively in ciliated neurons, and contain 
            regulatory elements for RFX, a transcription factor that modulates 
            the expression of genes associated with ciliogenesis and 
            intraflagellar transport
  - term:
      id: GO:1905515
      label: non-motile cilium assembly
    evidence_type: IEP
    original_reference_id: PMID:14520415
    review:
      summary: IEP annotation based on expression pattern. BBS-7 is expressed in
        ciliated neurons suggesting role in cilium assembly.
      action: ACCEPT
      reason: Appropriate annotation. Expression in ciliated neurons combined 
        with ciliopathy phenotypes in mutants supports a role in non-motile 
        cilium assembly.
      supported_by:
        - reference_id: PMID:14520415
          supporting_text: all available Caenorhabditis elegans BBS homologues 
            are expressed exclusively in ciliated neurons, and contain 
            regulatory elements for RFX, a transcription factor that modulates 
            the expression of genes associated with ciliogenesis and 
            intraflagellar transport
  - term:
      id: GO:0060271
      label: cilium assembly
    evidence_type: IMP
    original_reference_id: PMID:15231740
    review:
      summary: IMP annotation based on mutant phenotype. bbs-7 mutants have 
        structural ciliary defects including loss of distal segments 
        (PMID:15231740).
      action: ACCEPT
      reason: Core function with strong experimental support. Loss of BBS-7 
        causes structural and functional ciliary defects demonstrating its 
        requirement for proper cilium assembly.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: mutations in the Caenorhabditis elegans bbs-7 and 
            bbs-8 genes cause structural and functional defects in cilia
  - term:
      id: GO:0006935
      label: chemotaxis
    evidence_type: IMP
    original_reference_id: PMID:15231740
    review:
      summary: IMP annotation based on mutant phenotype. bbs-7 mutants exhibit 
        defective chemotaxis behavior (PMID:15231740).
      action: KEEP_AS_NON_CORE
      reason: Secondary phenotype. Chemotaxis defects are a consequence of 
        ciliary dysfunction rather than a direct molecular function of BBS-7. 
        BBS-7's core function is in IFT/BBSome, and chemotaxis defects result 
        from impaired sensory cilium function.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: mutations in the Caenorhabditis elegans bbs-7 and 
            bbs-8 genes cause structural and functional defects in cilia
  - term:
      id: GO:0042073
      label: intraciliary transport
    evidence_type: IMP
    original_reference_id: PMID:15231740
    review:
      summary: IMP annotation based on mutant phenotype. bbs-7 mutants have 
        compromised IFT with dissociation of IFT-A and IFT-B subcomplexes 
        (PMID:15231740).
      action: ACCEPT
      reason: Core function. BBS-7 is required for proper IFT including 
        maintenance of IFT particle integrity during transport. Loss of BBS-7 
        causes IFT-A and IFT-B to move separately.
      supported_by:
        - reference_id: PMID:15231740
          supporting_text: BBS-7 and BBS-8 are required for the normal 
            localization/motility of the IFT proteins OSM-5/Polaris and CHE-11, 
            and to a notably lesser extent, CHE-2
  - term:
      id: GO:0005198
      label: structural molecule activity
    evidence_type: NAS
    review:
      summary: Added to align core_functions with existing annotations.
      action: NEW
      reason: Core function term not present in existing_annotations.
references:
  - id: GO_REF:0000002
    title: Gene Ontology annotation through association of InterPro records with
      GO terms
    findings: []
  - id: GO_REF:0000033
    title: Annotation inferences using phylogenetic trees
    findings: []
  - id: GO_REF:0000043
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword 
      mapping
    findings: []
  - id: GO_REF:0000044
    title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular 
      Location vocabulary mapping
    findings: []
  - id: PMID:14520415
    title: Basal body dysfunction is a likely cause of pleiotropic Bardet-Biedl 
      syndrome.
    full_text_unavailable: true
    findings:
      - statement: BBS genes are expressed exclusively in ciliated neurons in C.
          elegans
        supporting_text: all available Caenorhabditis elegans BBS homologues are
          expressed exclusively in ciliated neurons
      - statement: BBS genes contain regulatory elements for RFX transcription 
          factor
        supporting_text: contain regulatory elements for RFX, a transcription 
          factor that modulates the expression of genes associated with 
          ciliogenesis and intraflagellar transport
  - id: PMID:15231740
    title: Loss of C. elegans BBS-7 and BBS-8 protein function results in cilia 
      defects and compromised intraflagellar transport.
    full_text_unavailable: true
    findings:
      - statement: bbs-7 and bbs-8 mutations cause structural and functional 
          ciliary defects
        supporting_text: mutations in the Caenorhabditis elegans bbs-7 and bbs-8
          genes cause structural and functional defects in cilia
      - statement: BBS proteins localize predominantly at the base of cilia and 
          move bidirectionally along the ciliary axoneme
        supporting_text: C. elegans BBS proteins localize predominantly at the 
          base of cilia, and like proteins involved in intraflagellar transport 
          (IFT), a process necessary for cilia biogenesis and maintenance, move 
          bidirectionally along the ciliary axoneme
      - statement: BBS-7 and BBS-8 are required for normal IFT protein 
          localization/motility
        supporting_text: BBS-7 and BBS-8 are required for the normal 
          localization/motility of the IFT proteins OSM-5/Polaris and CHE-11
      - statement: BBS proteins play selective roles in IFT particle assembly 
          and function
        supporting_text: We propose that BBS proteins play important, selective 
          roles in the assembly and/or function of IFT particle components
  - id: PMID:17000880
    title: Mechanism of transport of IFT particles in C. elegans cilia by the 
      concerted action of kinesin-II and OSM-3 motors.
    findings:
      - statement: In bbs-7/bbs-8 mutants, IFT-A and IFT-B dissociate during 
          anterograde transport
        supporting_text: "in bbs-7/-8 mutants, kinesin-II and IFT-A move together
          at 0.5 μm/s, but OSM-3–kinesin and IFT-B move as a distinct complex at 1.3
          μm/s"
      - statement: BBS-7/8 proteins coordinate IFT by holding IFT-A and IFT-B 
          subcomplexes together
        supporting_text: BBS-7/-8 proteins coordinate IFT by holding 
          subcomplexes IFT-A and -B together and stabilizing the integrity of 
          the IFT particles
      - statement: Loss of BBS-7 and -8 function leads to ciliary distal segment
          loss
        supporting_text: the loss of BBS-7 and -8 function in mutant animals 
          leads to the loss of ciliary distal segments and sensory defects
  - id: PMID:22342749
    title: Endocytosis genes facilitate protein and membrane transport in C. 
      elegans sensory cilia.
    findings: []
  - id: PMID:22922713
    title: The BBSome controls IFT assembly and turnaround in cilia.
    findings:
      - statement: BBSome assembles IFT complexes at the ciliary base and tip
        supporting_text: the BBSome is required for assembling IFT particles at 
          both ciliary base and tip
      - statement: BBS-1, BBS-7, and BBS-9 exist in the same complex (BiFC 
          confirmation)
        supporting_text: "fluorescence complementation can be observed in BBS-1–BBS-7
          and BBS-1–BBS-9 pair, indicative of the coexistence of these three BBS proteins
          in the same complex"
      - statement: BBSome functions as scaffold for IFT-A, IFT-B, and IFT cargos
        supporting_text: the BBSome functions as a scaffold to organize IFT-A, 
          IFT-B, ciliary membrane receptors, ciliary signaling molecules, and/or
          other IFT cargos into an entire unit and prepare it for IFT transport
  - id: PMID:25335890
    title: Ciliopathy proteins establish a bipartite signaling compartment in a 
      C. elegans thermosensory neuron.
    full_text_unavailable: true
    findings:
      - statement: BBS-8 and DAF-25 required for correct localization of 
          guanylyl cyclases
        supporting_text: requires BBS-8 and DAF-25 (known as Ankmy2 in mammals) 
          for correct localization of guanylyl cyclases needed for 
          thermosensation
  - id: file:worm/bbs-7/bbs-7-deep-research-falcon.md
    title: Deep research report on bbs-7
    findings: []
core_functions:
  - molecular_function:
      id: GO:0005198
      label: structural molecule activity
    description: BBS-7 is a core structural component of the BBSome complex that
      is essential for proper intraflagellar transport. The BBSome assembles IFT
      particles at the ciliary base and tip, maintaining IFT-A and IFT-B 
      subcomplex integrity during transport. Loss of BBS-7 causes IFT-A and 
      IFT-B subcomplexes to dissociate and move at different rates.
    in_complex:
      id: GO:0034464
      label: BBSome
    directly_involved_in:
      - id: GO:0042073
        label: intraciliary transport
      - id: GO:0060271
        label: cilium assembly
    locations:
      - id: GO:0005929
        label: cilium
      - id: GO:0036064
        label: ciliary basal body
      - id: GO:0005930
        label: axoneme
    supported_by:
      - reference_id: PMID:22922713
        supporting_text: the BBSome is required for assembling IFT particles at 
          both ciliary base and tip
      - reference_id: PMID:17000880
        supporting_text: BBS-7/-8 proteins coordinate IFT by holding 
          subcomplexes IFT-A and -B together and stabilizing the integrity of 
          the IFT particles
      - reference_id: PMID:15231740
        supporting_text: BBS-7 and BBS-8 are required for the normal 
          localization/motility of the IFT proteins OSM-5/Polaris and CHE-11
proposed_new_terms: []
suggested_questions:
  - question: What is the stoichiometry of BBS-7 within the BBSome complex in C.
      elegans?
  - question: Does BBS-7 have BBSome-independent functions?
  - question: How does BBS-7 interact with specific cargo proteins?
suggested_experiments:
  - description: Structure determination of the C. elegans BBSome complex to 
      understand BBS-7's position
  - description: Cargo-specific binding assays to identify direct BBS-7 
      interacting partners
  - description: Tissue-specific rescue experiments to identify neuron-specific 
      BBS-7 functions
tags:
  - caeel-ciliopathy

bbs-7

Gene Description

Existing Annotations Review

Core Functions

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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