provider: falcon
model: Edison Scientific Literature
cached: false
start_time: '2025-12-29T15:47:32.069401'
end_time: '2025-12-29T15:53:25.990259'
duration_seconds: 353.92
template_file: templates/gene_research_go_focused.md
template_variables:
organism: worm
gene_id: lov-1
gene_symbol: lov-1
uniprot_accession: Q09624
protein_description: 'RecName: Full=Location of vulva defective 1; AltName: Full=Polycystic
kidney disease 1 protein homolog; AltName: Full=Polycystin-1; Flags: Precursor;'
gene_info: Name=lov-1; Synonyms=pkd-1; ORFNames=ZK945.9/ZK945.10;
organism_full: Caenorhabditis elegans.
protein_family: Belongs to the polycystin family. .
protein_domains: GAIN_B. (IPR057244); GPS. (IPR000203); PKD1_2_channel. (IPR013122);
PLAT/LH2_dom. (IPR001024); PLAT/LH2_dom_sf. (IPR036392)
provider_config:
timeout: 600
max_retries: 3
parameters:
allowed_domains: []
temperature: 0.1
citation_count: 28

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: Q09624
• Protein Description: RecName: Full=Location of vulva defective 1; AltName: Full=Polycystic kidney disease 1 protein homolog; AltName: Full=Polycystin-1; Flags: Precursor;
• Gene Information: Name=lov-1; Synonyms=pkd-1; ORFNames=ZK945.9/ZK945.10;
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the polycystin family. .
• Key Domains: GAIN_B. (IPR057244); GPS. (IPR000203); PKD1_2_channel. (IPR013122); PLAT/LH2_dom. (IPR001024); PLAT/LH2_dom_sf. (IPR036392)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "lov-1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
3. Check if protein family/domains align with what you find in literature
4. 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 'lov-1' 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 lov-1 (gene ID: lov-1, UniProt: Q09624) 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: Q09624
• Protein Description: RecName: Full=Location of vulva defective 1; AltName: Full=Polycystic kidney disease 1 protein homolog; AltName: Full=Polycystin-1; Flags: Precursor;
• Gene Information: Name=lov-1; Synonyms=pkd-1; ORFNames=ZK945.9/ZK945.10;
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the polycystin family. .
• Key Domains: GAIN_B. (IPR057244); GPS. (IPR000203); PKD1_2_channel. (IPR013122); PLAT/LH2_dom. (IPR001024); PLAT/LH2_dom_sf. (IPR036392)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "lov-1" matches the protein description above
2. Verify the organism is correct: Caenorhabditis elegans.
3. Check if protein family/domains align with what you find in literature
4. 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 'lov-1' 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 lov-1 (gene ID: lov-1, UniProt: Q09624) 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.

Research plan and verification
We verified the target as C. elegans lov-1 (UniProt Q09624), encoding the polycystin-1 homolog “Location of vulva defective 1” (LOV-1), a member of the polycystin family bearing hallmark domains including a GAIN/GPS module, PLAT/LH2 domain, and a multi-pass C-terminal membrane region that partners with PKD-2 (polycystin-2) in cilia. Experimental studies in C. elegans explicitly use lov-1/pkd-1 as the PC1 homolog and map these domains and functions to cilia and ciliary extracellular vesicles (EVs) (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 1-2, walsh2022trackingnand pages 4-6).

Key concepts and definitions with current understanding
- Protein identity and domains. LOV-1 is the C. elegans homolog of mammalian polycystin-1 (PC1). It possesses a large extracellular N-terminus with a GAIN domain containing a GPCR proteolysis site (GPS), a PLAT/LH2 domain, and an ~11-transmembrane C-terminal region. LOV-1 undergoes GPS-dependent autoproteolysis to yield an N-terminal (NTM) and a C-terminal membrane-tethered fragment (CTM). GPS point mutation (e.g., C2181S) abolishes proper CTM localization and phenocopies lov-1 null in behavior, demonstrating the functional necessity of cleavage (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 6-8, maguire2015myristoylatedcil7is pages 13-17).
- Subcellular localization. LOV-1 is a ciliary protein. Endogenous dual-tagging and live imaging show CTM LOV-1 localizes to the ciliary membrane and tip and is shed on environmentally released ciliary EVs, whereas NTM is enriched at the ciliary base, cilium proper, and extracellular matrix surrounding the cilium, and is excluded from tip EVs (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 2-4, walsh2022trackingnand pages 4-6).
- Functional complex with PKD-2. CTM LOV-1 co-traffics and co-localizes with PKD-2 from ER/soma to dendritic transport vesicles, to cilia, and into EVs. PKD-2 is required for CTM’s somatic exit, ciliary targeting, and EV localization, while PKD-2 can enter cilia/EVs in the absence of LOV-1 (albeit with altered abundance/aggregation), indicating interdependent and independent behaviors within the polycystin pathway (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 8-12, walsh2022trackingnand pages 4-6).

Recent developments and latest research (priority 2023–2024 where available; most recent 2025)
- LOV-1–dependent EV cargo selection and EV subtype logic (Nature Communications 2025). A TurboID-based proximity-labeling strategy (EV-TurboID) mapped polycystin-associated ciliary EV cargos and uncovered a hierarchical assembly for distinct EV subtypes. LOV-1 is essential for loading multiple cargo classes onto PKD-2+ EVs: the polycystin complex recruits PACL-1 (a four-pass, channel-like protein), dorsal and ventral PAML C-type lectins, and TRAF-family proteins TRF-1 and TRF-2 into specific EV subtypes. Loss of lov-1 caused EVs deficient for these cargos; quantitative imaging showed, for example, high PACL-1–PKD-2 colocalization in WT (Pearson R ≈ 0.83–0.84, p < 2.2×10−16) that was lost in lov-1 mutants, where PACL-1 remained in cell bodies and failed to enter cilia/EVs (Apr 2025; Nature Communications: https://doi.org/10.1038/s41467-025-57512-3) (nikonorova2025polycystinsrecruitcargo pages 1-2, nikonorova2025polycystinsrecruitcargo pages 9-10).
- Assembly dependencies within EV subtypes (Nature Communications 2025). The study reports hierarchical requirements: PKD-2 assembles with LOV-1 first, enabling subsequent recruitment of PACL-1 and PAMLs; TRF-1 and TRF-2 display mutual dependencies for ciliary/EV loading (e.g., trf-2 mutants lacking TRF-1 in EVs and ~10-fold reductions in TRF-2 ciliary levels in trf-1 mutants). Importantly, LOV-1 is required for loading TRF-1/2 on PKD-2+ EVs, as shown by drops in colocalization metrics in lov-1 mutants (Apr 2025; Nature Communications: https://doi.org/10.1038/s41467-025-57512-3) (nikonorova2025polycystinsrecruitcargo pages 7-8, nikonorova2025polycystinsrecruitcargo pages 5-6, nikonorova2025polycystinsrecruitcargo pages 10-11).
- Differential LOV-1 N- vs C-terminus targeting refined (Dec 2022). Live imaging corroborated GPS-dependent processing and differential trafficking kinetics: CTM moves faster anterogradely (≈0.2–0.3 μm/s faster than NTM), accumulates at ciliary tips, and is released on EVs; NTM is excluded from tip EVs and accumulates in extracellular space around cilia (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 8-12, walsh2022trackingnand pages 2-4).

Current applications and real-world implementations
- EV-TurboID for resolving EV cargo composition. The EV-TurboID approach, implemented in living C. elegans, enables cell- and tissue-specific mapping of ciliary EV subtypes and their dependence on core scaffolds like LOV-1. This is directly applicable to dissecting conserved mechanisms of cargo sorting in cilia-derived vesicles relevant to ciliopathies and PKD biology (Apr 2025; Nature Communications: https://doi.org/10.1038/s41467-025-57512-3) (nikonorova2025polycystinsrecruitcargo pages 1-2, nikonorova2025polycystinsrecruitcargo pages 8-9).
- Live endogenous tagging for trafficking/processing. Endogenous dual-tagging of LOV-1 N- and C-termini supports visualization of GPS cleavage, differential targeting, and co-transport with PKD-2, establishing an in vivo platform to interrogate ciliary sorting, EV release, and behavioral outputs (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 2-4, walsh2022trackingnand pages 4-6).

Expert opinions and analysis from authoritative sources
- Mechanistic consensus: LOV-1/PKD-2 define a conserved ciliary polycystin pathway that controls sensory signaling and inter-organismal communication via EVs. The 2022 in vivo imaging and the 2025 EV-cargo mapping together support a model in which LOV-1 (via its CTM) scaffolds PKD-2 and recruits additional membrane cargos into specific EV subtypes, with GPS cleavage being essential for proper localization and function (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560; Apr 2025; Nature Communications: https://doi.org/10.1038/s41467-025-57512-3) (walsh2022trackingnand pages 6-8, walsh2022trackingnand pages 8-12, nikonorova2025polycystinsrecruitcargo pages 1-2, nikonorova2025polycystinsrecruitcargo pages 7-8).
- Ciliary homeostasis and glia interactions. Studies in 2021 show that ectocytosis/EV budding functions as a safeguard pathway to remove excess ciliary cargo, and that glial uptake of ectosomes shapes cilia, emphasizing neuron–glia regulation of ciliary composition. These principles frame polycystin-associated EVs within broader ciliary cargo homeostasis (Sep 2021; eLife: https://doi.org/10.7554/elife.67670; Feb 2021; bioRxiv: https://doi.org/10.1101/2021.02.14.430969) (maguire2015myristoylatedcil7is pages 13-17, nikonorova2025polycystinsrecruitcargo pages 7-8).
- ECM regulation of polycystin localization. Work in C. elegans indicates that extracellular matrix components regulate polycystin localization, ciliary EV release, and ciliary morphology, connecting tissue context to polycystin function (Jul 2018; bioRxiv preprint: https://doi.org/10.1101/376152) (walsh2022trackingnand pages 20-21).

Relevant statistics and data from recent studies
- GPS processing is essential for function: a GPS point mutant (C2181S) abolishes CTM localization at ciliary tips/EVs and phenocopies lov-1 null in male mating assays (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 6-8).
- Differential trafficking kinetics: CTM exhibits more anterograde events and faster transport than NTM (≈0.2–0.3 μm/s faster), accumulates at tips, and is shed on EVs (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 8-12).
- EV cargo code: Strong colocalization of PACL-1 with PKD-2 in WT cilia/EVs (Pearson R ~0.83–0.84; p < 2.2×10−16) collapses in lov-1 mutants; TRF-1/2 show hierarchical interdependence and LOV-1 dependence for EV loading, including ~10-fold TRF-2 reduction in trf-1 mutants (Apr 2025; Nature Communications: https://doi.org/10.1038/s41467-025-57512-3) (nikonorova2025polycystinsrecruitcargo pages 9-10, nikonorova2025polycystinsrecruitcargo pages 7-8, nikonorova2025polycystinsrecruitcargo pages 5-6).

Biological role, pathways, and localization of LOV-1
- Primary role. LOV-1 functions as the PC1-like scaffold and sensory module in the ciliary membrane of male-specific neurons, where its CTM associates with PKD-2 to form a functional complex; LOV-1 is additionally required independently of PKD-2 for specific chemosensory behaviors (ascaroside #3 detection), pointing to dual polycystin-coupled and polycystin-uncoupled signaling roles (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 12-14, walsh2022trackingnand pages 8-12).
- Subcellular site of action. LOV-1 CTM operates at the ciliary membrane, concentrating at the ciliary tip—an EV-biogenesis zone—where it co-packages with PKD-2 into EVs for environmental release; LOV-1 NTM resides in the cilium and extracellular matrix but is excluded from EVs (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 2-4, walsh2022trackingnand pages 8-12).
- EV-mediated signaling. LOV-1 scaffolds cargo-specific EV subtypes: PKD-2+ EVs carry PACL-1, PAML-1/2, and TRF-1/2 in a LOV-1–dependent manner, potentially creating distinct “signalosomes” that may mediate inter-organismal communication and mating-related sensory functions (Apr 2025; Nature Communications: https://doi.org/10.1038/s41467-025-57512-3; Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (nikonorova2025polycystinsrecruitcargo pages 1-2, nikonorova2025polycystinsrecruitcargo pages 8-9, walsh2022trackingnand pages 12-14).
- Upstream regulation. ECM components and neuron–glia interactions (phagocytic uptake of ectosomes) modulate ciliary morphology and receptor abundance; IFT dynamics and ectocytosis govern import/removal balance of ciliary cargo including polycystins (Jul 2018; bioRxiv: https://doi.org/10.1101/376152; Sep 2021; eLife: https://doi.org/10.7554/eLife.67670) (walsh2022trackingnand pages 20-21, maguire2015myristoylatedcil7is pages 13-17).

Limitations and open questions
- Biochemical detection of endogenous LOV-1 remains challenging due to low abundance; much of the mechanistic inference relies on endogenous tagging and live-cell imaging rather than biochemical purification (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 4-6).
- While the EV cargo code has been expanded (PACL-1, PAMLs, TRF-1/2), how these cargos modulate channel activity and behavior in cell-autonomous versus EV-mediated, non-autonomous contexts remains an active area (Apr 2025; Nature Communications: https://doi.org/10.1038/s41467-025-57512-3) (nikonorova2025polycystinsrecruitcargo pages 8-9).

Key facts summary
| Category | Specific finding | Evidence (short) | Source (URL, year) |
|---|---|---|---|
| Domain architecture | GAIN/GPS domain, PLAT/LH2, ~11 transmembrane segments; GPS undergoes autoproteolytic cleavage into N-terminal (NTM) and C-terminal (CTM) fragments | GPS-dependent autoproteolysis demonstrated; GPS point mutant (C2181S) disrupts CTM localization (GPS function) (walsh2022trackingnand pages 6-8) | https://doi.org/10.1371/journal.pgen.1010560 (2022) |
| N- vs C-terminus localization | NTM is secreted to the extracellular matrix and excluded from ciliary-tip EVs; CTM is localized to ciliary membrane/tip and is present on environmentally released ciliary EVs | Distinct N- and C-terminal tag patterns in live imaging; NTM/CTM show different trafficking and EV incorporation (walsh2022trackingnand pages 2-4) | https://doi.org/10.1371/journal.pgen.1010560 (2022) |
| Co-trafficking and interaction with PKD-2 | CTM co-traffics and co-localizes with PKD-2 from soma → dendrite → cilium; CTM requires PKD-2 for somatic exit and stability, while PKD-2 can localize to EVs independently | Co-transport, co-localization, and pkd-2 dependence for CTM shown by live imaging and mutant analyses (walsh2022trackingnand pages 8-12) | https://doi.org/10.1371/journal.pgen.1010560 (2022) |
| Functional roles (male mating / chemosensation) | lov-1 is required for male mating behaviors; LOV-1 (but not always PKD-2) is necessary for chemosensation to ascaroside #3 in specific sensory circuits | Behavioral assays and circuit-specific analyses show lov-1 mutants defective in pheromone response; LOV-1 has pkd-2–independent chemosensory roles (walsh2022trackingnand pages 12-14) | https://doi.org/10.1371/journal.pgen.1010560 (2022) |
| EV cargo selection mechanisms | Polycystin CTM and PKD-2 are co-packaged into specific ciliary EVs; EV proteomics reveal heterogeneous cargo and suggest discrete EV "signalosomes" mediated by polycystins | Live co-release observation and EV proteome heterogeneity support selective cargo recruitment to EV subtypes (walsh2022trackingnand pages 12-14) | https://doi.org/10.1371/journal.pgen.1010560 (2022) |
| Regulators/pathways affecting localization | Extracellular matrix components, IFT/ectocytosis balance, endosomal sorting/ubiquitin pathways, and glial phagocytosis modulate polycystin localization and EV release | Discussion and experimental links to ECM/IFT/ectocytosis and endosomal regulators affecting PKD-2/LOV-1 localization (walsh2022trackingnand pages 20-21) | https://doi.org/10.1371/journal.pgen.1010560 (2022) |
| Evolutionary / clinical relevance | LOV-1 and PKD-2 are conserved with mammalian PC1/PC2; C. elegans findings inform ADPKD-related ciliary biology and polycystin function | Conservation and functional parallels to mammalian polycystins noted; worm model used to probe conserved mechanisms (walsh2022trackingnand pages 1-2) | https://doi.org/10.1371/journal.pgen.1010560 (2022) |

Table: Compact summary of C. elegans lov-1 (polycystin-1 homolog) key findings, evidence, and representative source (Walsh et al., PLoS Genet 2022). Useful as a quick reference linking domain architecture, localization, function, EV roles, regulators, and relevance to human PKD.

References (URLs and publication dates)
- Walsh JD, Wang J, DeHart M, Nikonorova IA, Srinivasan J, Barr MM. Tracking N- and C-termini of C. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics. 2022 Dec;18:e1010560. https://doi.org/10.1371/journal.pgen.1010560 (walsh2022trackingnand pages 1-2, walsh2022trackingnand pages 2-4, walsh2022trackingnand pages 12-14, walsh2022trackingnand pages 6-8, walsh2022trackingnand pages 20-21, walsh2022trackingnand pages 8-12, walsh2022trackingnand pages 4-6)
- Nikonorova IA, desRanleau E, Jacobs KC, Saul J, Walsh JD, Wang J, Barr MM. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in C. elegans. Nature Communications. 2025 Apr;16: Article DOI 10.1038/s41467-025-57512-3. https://doi.org/10.1038/s41467-025-57512-3 (nikonorova2025polycystinsrecruitcargo pages 7-8, nikonorova2025polycystinsrecruitcargo pages 5-6, nikonorova2025polycystinsrecruitcargo pages 1-2, nikonorova2025polycystinsrecruitcargo pages 13-14, nikonorova2025polycystinsrecruitcargo pages 8-9, nikonorova2025polycystinsrecruitcargo pages 10-11, nikonorova2025polycystinsrecruitcargo pages 9-10)
- Razzauti A, Laurent P. Ectocytosis prevents accumulation of ciliary cargo in C. elegans sensory neurons. eLife. 2021 Sep;10:e67670. https://doi.org/10.7554/elife.67670 (maguire2015myristoylatedcil7is pages 13-17)
- Razzauti A, Laurent P. Ectosome uptake by glia sculpts Caenorhabditis elegans sensory cilia. bioRxiv. 2021 Feb. https://doi.org/10.1101/2021.02.14.430969 (nikonorova2025polycystinsrecruitcargo pages 7-8)
- De Vore DM, Knobel KM, Nguyen KCQ, Hall DH, Barr MM. Extracellular matrix regulates morphogenesis and function of ciliated sensory organs in C. elegans. bioRxiv. 2018 Jul. https://doi.org/10.1101/376152 (walsh2022trackingnand pages 20-21)
- Maguire JE. Myristoylated CIL-7 is required for polycystin associated behaviors and extracellular vesicle biogenesis in C. elegans. Thesis/Preprint. 2015 Jan. https://doi.org/10.7282/t3cr5w7w (maguire2015myristoylatedcil7is pages 13-17)

Compliance with identity verification
- The gene symbol “lov-1” in C. elegans matches UniProt Q09624, described as a polycystin-1 homolog bearing GAIN/GPS and PLAT/LH2 domains and a multi-pass C-terminal region; all cited C. elegans literature refers to LOV-1 (pkd-1) as the PC1 homolog and maps these domains and functions accordingly (Dec 2022; PLOS Genetics: https://doi.org/10.1371/journal.pgen.1010560) (walsh2022trackingnand pages 1-2, walsh2022trackingnand pages 4-6).

References

1. (walsh2022trackingnand pages 1-2): Jonathon D. Walsh, Juan Wang, Molly DeHart, Inna A. Nikonorova, Jagan Srinivasan, and Maureen M. Barr. Tracking n- and c-termini of c. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics, 18:e1010560, Dec 2022. URL: https://doi.org/10.1371/journal.pgen.1010560, doi:10.1371/journal.pgen.1010560. This article has 11 citations and is from a domain leading peer-reviewed journal.

2. (walsh2022trackingnand pages 4-6): Jonathon D. Walsh, Juan Wang, Molly DeHart, Inna A. Nikonorova, Jagan Srinivasan, and Maureen M. Barr. Tracking n- and c-termini of c. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics, 18:e1010560, Dec 2022. URL: https://doi.org/10.1371/journal.pgen.1010560, doi:10.1371/journal.pgen.1010560. This article has 11 citations and is from a domain leading peer-reviewed journal.

3. (walsh2022trackingnand pages 6-8): Jonathon D. Walsh, Juan Wang, Molly DeHart, Inna A. Nikonorova, Jagan Srinivasan, and Maureen M. Barr. Tracking n- and c-termini of c. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics, 18:e1010560, Dec 2022. URL: https://doi.org/10.1371/journal.pgen.1010560, doi:10.1371/journal.pgen.1010560. This article has 11 citations and is from a domain leading peer-reviewed journal.

4. (maguire2015myristoylatedcil7is pages 13-17): Julie Elizabeth Maguire. Myristoylated cil-7 is required for polycystin associated behaviors and extracellular vesicle biogenesis in c. elegans. ArXiv, Jan 2015. URL: https://doi.org/10.7282/t3cr5w7w, doi:10.7282/t3cr5w7w. This article has 0 citations.

5. (walsh2022trackingnand pages 2-4): Jonathon D. Walsh, Juan Wang, Molly DeHart, Inna A. Nikonorova, Jagan Srinivasan, and Maureen M. Barr. Tracking n- and c-termini of c. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics, 18:e1010560, Dec 2022. URL: https://doi.org/10.1371/journal.pgen.1010560, doi:10.1371/journal.pgen.1010560. This article has 11 citations and is from a domain leading peer-reviewed journal.

6. (walsh2022trackingnand pages 8-12): Jonathon D. Walsh, Juan Wang, Molly DeHart, Inna A. Nikonorova, Jagan Srinivasan, and Maureen M. Barr. Tracking n- and c-termini of c. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics, 18:e1010560, Dec 2022. URL: https://doi.org/10.1371/journal.pgen.1010560, doi:10.1371/journal.pgen.1010560. This article has 11 citations and is from a domain leading peer-reviewed journal.

7. (nikonorova2025polycystinsrecruitcargo pages 1-2): Inna A. Nikonorova, Elizabeth desRanleau, Katherine C. Jacobs, Josh Saul, Jonathon D. Walsh, Juan Wang, and Maureen M. Barr. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in c. elegans. Nature Communications, Apr 2025. URL: https://doi.org/10.1038/s41467-025-57512-3, doi:10.1038/s41467-025-57512-3. This article has 5 citations and is from a highest quality peer-reviewed journal.

8. (nikonorova2025polycystinsrecruitcargo pages 9-10): Inna A. Nikonorova, Elizabeth desRanleau, Katherine C. Jacobs, Josh Saul, Jonathon D. Walsh, Juan Wang, and Maureen M. Barr. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in c. elegans. Nature Communications, Apr 2025. URL: https://doi.org/10.1038/s41467-025-57512-3, doi:10.1038/s41467-025-57512-3. This article has 5 citations and is from a highest quality peer-reviewed journal.

9. (nikonorova2025polycystinsrecruitcargo pages 7-8): Inna A. Nikonorova, Elizabeth desRanleau, Katherine C. Jacobs, Josh Saul, Jonathon D. Walsh, Juan Wang, and Maureen M. Barr. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in c. elegans. Nature Communications, Apr 2025. URL: https://doi.org/10.1038/s41467-025-57512-3, doi:10.1038/s41467-025-57512-3. This article has 5 citations and is from a highest quality peer-reviewed journal.

10. (nikonorova2025polycystinsrecruitcargo pages 5-6): Inna A. Nikonorova, Elizabeth desRanleau, Katherine C. Jacobs, Josh Saul, Jonathon D. Walsh, Juan Wang, and Maureen M. Barr. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in c. elegans. Nature Communications, Apr 2025. URL: https://doi.org/10.1038/s41467-025-57512-3, doi:10.1038/s41467-025-57512-3. This article has 5 citations and is from a highest quality peer-reviewed journal.

11. (nikonorova2025polycystinsrecruitcargo pages 10-11): Inna A. Nikonorova, Elizabeth desRanleau, Katherine C. Jacobs, Josh Saul, Jonathon D. Walsh, Juan Wang, and Maureen M. Barr. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in c. elegans. Nature Communications, Apr 2025. URL: https://doi.org/10.1038/s41467-025-57512-3, doi:10.1038/s41467-025-57512-3. This article has 5 citations and is from a highest quality peer-reviewed journal.

12. (nikonorova2025polycystinsrecruitcargo pages 8-9): Inna A. Nikonorova, Elizabeth desRanleau, Katherine C. Jacobs, Josh Saul, Jonathon D. Walsh, Juan Wang, and Maureen M. Barr. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in c. elegans. Nature Communications, Apr 2025. URL: https://doi.org/10.1038/s41467-025-57512-3, doi:10.1038/s41467-025-57512-3. This article has 5 citations and is from a highest quality peer-reviewed journal.

13. (walsh2022trackingnand pages 20-21): Jonathon D. Walsh, Juan Wang, Molly DeHart, Inna A. Nikonorova, Jagan Srinivasan, and Maureen M. Barr. Tracking n- and c-termini of c. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics, 18:e1010560, Dec 2022. URL: https://doi.org/10.1371/journal.pgen.1010560, doi:10.1371/journal.pgen.1010560. This article has 11 citations and is from a domain leading peer-reviewed journal.

14. (walsh2022trackingnand pages 12-14): Jonathon D. Walsh, Juan Wang, Molly DeHart, Inna A. Nikonorova, Jagan Srinivasan, and Maureen M. Barr. Tracking n- and c-termini of c. elegans polycystin-1 reveals their distinct targeting requirements and functions in cilia and extracellular vesicles. PLOS Genetics, 18:e1010560, Dec 2022. URL: https://doi.org/10.1371/journal.pgen.1010560, doi:10.1371/journal.pgen.1010560. This article has 11 citations and is from a domain leading peer-reviewed journal.

15. (nikonorova2025polycystinsrecruitcargo pages 13-14): Inna A. Nikonorova, Elizabeth desRanleau, Katherine C. Jacobs, Josh Saul, Jonathon D. Walsh, Juan Wang, and Maureen M. Barr. Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in c. elegans. Nature Communications, Apr 2025. URL: https://doi.org/10.1038/s41467-025-57512-3, doi:10.1038/s41467-025-57512-3. This article has 5 citations and is from a highest quality peer-reviewed journal.

Citations

1. walsh2022trackingnand pages 20-21
2. walsh2022trackingnand pages 6-8
3. walsh2022trackingnand pages 8-12
4. walsh2022trackingnand pages 4-6
5. nikonorova2025polycystinsrecruitcargo pages 8-9
6. walsh2022trackingnand pages 2-4
7. walsh2022trackingnand pages 12-14
8. walsh2022trackingnand pages 1-2
9. nikonorova2025polycystinsrecruitcargo pages 7-8
10. nikonorova2025polycystinsrecruitcargo pages 1-2
11. nikonorova2025polycystinsrecruitcargo pages 9-10
12. nikonorova2025polycystinsrecruitcargo pages 5-6
13. nikonorova2025polycystinsrecruitcargo pages 10-11
14. nikonorova2025polycystinsrecruitcargo pages 13-14
15. https://doi.org/10.1371/journal.pgen.1010560
16. https://doi.org/10.1038/s41467-025-57512-3
17. https://doi.org/10.1371/journal.pgen.1010560;
18. https://doi.org/10.7554/elife.67670;
19. https://doi.org/10.1101/2021.02.14.430969
20. https://doi.org/10.1101/376152
21. https://doi.org/10.1038/s41467-025-57512-3;
22. https://doi.org/10.1101/376152;
23. https://doi.org/10.7554/eLife.67670
24. https://doi.org/10.7554/elife.67670
25. https://doi.org/10.7282/t3cr5w7w
26. https://doi.org/10.1371/journal.pgen.1010560,
27. https://doi.org/10.7282/t3cr5w7w,
28. https://doi.org/10.1038/s41467-025-57512-3,