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Question

Gene Research for Functional Annotation

⚠️ CRITICAL: Gene/Protein Identification Context

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

Target Gene/Protein Identity (from UniProt):

• UniProt Accession: Q20046
• Protein Description: SubName: Full=Meckelin {ECO:0000313|EMBL:CCD70508.1};
• Gene Information: Name=mks-3 {ECO:0000313|EMBL:CCD70508.1, ECO:0000313|WormBase:F35D2.4}; ORFNames=CELE_F35D2.4 {ECO:0000313|EMBL:CCD70508.1}, F35D2.4 {ECO:0000313|WormBase:F35D2.4};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: Meckelin. (IPR019170); Meckelin (PF09773)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "mks-3" 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 'mks-3' 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 mks-3 (gene ID: mks-3, UniProt: Q20046) 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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: Q20046
• Protein Description: SubName: Full=Meckelin {ECO:0000313|EMBL:CCD70508.1};
• Gene Information: Name=mks-3 {ECO:0000313|EMBL:CCD70508.1, ECO:0000313|WormBase:F35D2.4}; ORFNames=CELE_F35D2.4 {ECO:0000313|EMBL:CCD70508.1}, F35D2.4 {ECO:0000313|WormBase:F35D2.4};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: Meckelin. (IPR019170); Meckelin (PF09773)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "mks-3" 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 'mks-3' 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 mks-3 (gene ID: mks-3, UniProt: Q20046) 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.

Plan
Objective 1 (completed): Verified target identity and orthology. The C. elegans gene mks-3 (UniProt Q20046) encodes the Meckelin ortholog of human TMEM67/MKS3, a membrane protein localized to the ciliary transition zone (TZ) within the Meckel syndrome (MKS) module. This identity and localization are consistently reported in authoritative studies and reviews (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8).
Objective 2 (completed): Retrieved recent and authoritative literature, prioritizing 2022–2024 where available. Key sources include a 2022 EMBO Reports TZ review (Park & Leroux, 2022), foundational experimental studies defining MKS/NPHP module organization and gating (2015–2016), and a 2024 bioRxiv mechanistic preprint on TMEM67 cleavage by ADAMTS9 that separates ciliogenesis/TZ functions from Wnt signaling (Ahmed et al., 2024) (park2022compositionorganizationand pages 6-8, li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2, lambacher2016tmem107recruitsciliopathy pages 20-20, ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23).
Objective 3 (completed): Extracted function, localization, and module context; summarized below with citations.
Objective 4 (completed): Compiled applications/real-world implementations, including variant interpretation in C. elegans for TMEM67 VUS and disease relevance via orthology (lange2021interpretingciliopathyassociatedmissense pages 1-4, park2022compositionorganizationand pages 6-8).
Objective 5 (completed): Synthesized expert opinions, statistics, and data; included URLs and publication dates for all major sources.
Objective 6: Provide final comprehensive, well-cited research report.

Comprehensive Research Report: mks-3 (C. elegans Meckelin; ortholog of human TMEM67/MKS3)

1) Key concepts and definitions with current understanding
- Identity and orthology: mks-3 encodes the C. elegans ortholog of human TMEM67 (also called MKS3/Meckelin), a conserved transmembrane protein of the ciliary transition zone (TZ) that functions in the MKS module of TZ proteins. The MKS module cooperates with the NPHP module to assemble a functional TZ diffusion barrier (“ciliary gate”) (Park & Leroux, EMBO Reports, Nov 2022, https://doi.org/10.15252/embr.202255420; Li et al., PLoS Biology, Mar 2016, https://doi.org/10.1371/journal.pbio.1002416; Jensen et al., EMBO J, Oct 2015, https://doi.org/10.15252/embj.201488044) (park2022compositionorganizationand pages 6-8, li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2).
- Protein family/domains: UniProt Q20046 is annotated as Meckelin with Meckelin domains (PF09773, IPR019170). In the literature, Meckelin/TMEM67 is a membrane protein enriched at the TZ membrane, consistent with Meckelin domain annotations and MKS-module membership (Park & Leroux 2022; Li et al. 2016; Jensen et al. 2015) (park2022compositionorganizationand pages 6-8, li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2).
- Cellular localization: MKS-3 localizes to the ciliary transition zone membrane and forms part of the MKS module superstructure. Super-resolution mapping showed that TMEM67/MKS-3 occupies radial and axial subdomains of the TZ membrane, forming discrete clustered rings consistent with association to Y-links and ciliary necklace features (Lambacher et al., Nat Cell Biol, Nov 2016, https://doi.org/10.1038/ncb3273) (lambacher2016tmem107recruitsciliopathy pages 20-20).
- Functional role: As an MKS-module component, MKS-3 contributes to establishing/maintaining the TZ diffusion barrier (gate) that preserves ciliary compartmentalization. The MKS module acts largely in parallel with the NPHP module; together they ensure proper TZ ultrastructure (including Y-links), anchoring, ciliogenesis, and gating of membrane proteins and lipids (Park & Leroux 2022; Li et al. 2016; Jensen et al. 2015) (park2022compositionorganizationand pages 6-8, li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2).

2) Recent developments and latest research (prioritize 2023–2024 sources)
- Proteolytic regulation creates two functional TMEM67 forms: A 2024 preprint reported that the extracellular protease ADAMTS9 cleaves TMEM67, generating a cleaved C-terminal form that localizes to the TZ and is essential for ciliogenesis and MKS/B9 assembly, while the non-cleaved full-length protein mediates Wnt signaling. A non-cleavable Tmem67 mouse phenocopied Tmem67-null for ciliopathy manifestations yet retained Wnt signaling, mechanistically separating TMEM67’s TZ versus Wnt roles. C. elegans assays were used alongside mammalian models to probe TMEM67/mks-3 requirements (Ahmed et al., bioRxiv, Sep 2024, https://doi.org/10.1101/2024.09.04.611229) (ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23).
- Updated TZ conceptual framework: The 2022 EMBO Reports review synthesized module organization (MKS vs NPHP), hierarchical assembly (MKS-5/RPGRIP1L and CEP-290 scaffolding), and gating mechanisms (lipid microdomain, picket-fence, size-selective sieve). It places MKS-3/TMEM67 as a canonical MKS-module TZ protein within this hierarchy (Park & Leroux, EMBO Reports, Nov 2022, https://doi.org/10.15252/embr.202255420) (park2022compositionorganizationand pages 6-8).

3) Current applications and real-world implementations
- Variant interpretation pipeline using C. elegans mks-3: CRISPR/Cas9 knock-in of human TMEM67 missense variants into the endogenous worm mks-3 locus, coupled to quantitative cilia structure and function assays, distinguished known benign from pathogenic alleles and classified eight VUS (three benign: Cys173Arg, Thr176Ile, Gly979Arg; five pathogenic: Cys170Tyr, His782Arg, Gly786Glu, His790Arg, Ser961Tyr). This demonstrates a tractable in vivo platform that can inform clinical classification of TMEM67 variants relevant to Meckel/Joubert spectrum ciliopathies (Lange et al., bioRxiv, posted Sep 22, 2021, https://doi.org/10.1101/2021.06.17.448799) (lange2021interpretingciliopathyassociatedmissense pages 1-4).

4) Expert opinions and analysis from authoritative sources
- TZ modules and genetic redundancy: Authoritative studies define the TZ as comprising two functional modules. MKS-3 belongs to the MKS module; CEP-290 and MKS-5/RPGRIP1L act as core assembly factors. Disruption of single-module components is often partially tolerated, but combined MKS–NPHP defects cause severe ciliogenesis and TZ ultrastructural defects, reflecting parallel, cooperative pathways (Park & Leroux 2022; Li et al. 2016; Jensen et al. 2015) (park2022compositionorganizationand pages 6-8, li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2).
- Spatial organization of MKS-3 at the TZ: Super-resolution imaging shows conserved clustering of TMEM67/MKS-3 in rings at the TZ membrane, implying association with Y-links and necklace structures that support barrier function (Lambacher et al. 2016, https://doi.org/10.1038/ncb3273) (lambacher2016tmem107recruitsciliopathy pages 20-20).
- Separation of signaling and ciliogenesis roles: The 2024 preprint argues that proteolytic cleavage of TMEM67 by ADAMTS9 separates ciliogenesis/TZ assembly from TMEM67-mediated Wnt signaling, which has implications for interpreting genotype–phenotype relationships and therapeutic strategies (Ahmed et al. 2024, https://doi.org/10.1101/2024.09.04.611229) (ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23).

5) Relevant statistics and data from recent studies
- Hierarchical TZ assembly and gating: Experimental work in C. elegans established that CEP-290 and MKS-5 organize MKS-module components, enforcing ciliary compartmentalization by limiting inappropriate membrane protein entry and retaining ARL-13/Arl13b within the cilium; combined MKS–NPHP disruptions cause pronounced loss of TZ Y-links and ciliogenesis failures (Li et al., PLoS Biology, Mar 2016, https://doi.org/10.1371/journal.pbio.1002416; Jensen et al., EMBO J, Oct 2015, https://doi.org/10.15252/embj.201488044) (li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2).
- Variant assay outcomes in C. elegans: In a CRISPR knock-in study of TMEM67/mks-3 variants, worm assays accurately discriminated known benign versus pathogenic variants and classified eight VUS, with three predicted benign and five pathogenic (Lange et al., bioRxiv, Sep 2021, https://doi.org/10.1101/2021.06.17.448799) (lange2021interpretingciliopathyassociatedmissense pages 1-4).
- Subdomain mapping: Super-resolution mapping resolved periodic radial and axial subdomains of MKS-3/TMEM67 at the TZ membrane, forming clustered rings thought to align with Y-link architecture, supporting a structural basis for gating (Lambacher et al., Nat Cell Biol, Nov 2016, https://doi.org/10.1038/ncb3273) (lambacher2016tmem107recruitsciliopathy pages 20-20).
- Proteolytic cleavage and functional separation (2024): The ADAMTS9 cleavage study demonstrated that preventing TMEM67 cleavage phenocopied Tmem67-null ciliopathy for ciliogenesis/TZ assembly while preserving Wnt signaling, implying two functional forms with distinct roles (Ahmed et al., bioRxiv, Sep 2024, https://doi.org/10.1101/2024.09.04.611229) (ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23).

Detailed functional narrative for C. elegans mks-3
- Primary role: MKS-3 is an MKS-module transition zone membrane protein required for forming a functional TZ diffusion barrier that compartmentalizes proteins and lipids within the cilium. In the MKS-5→CEP-290-dependent assembly hierarchy, MKS-3 is among the MKS transmembrane components positioned at the TZ membrane, contributing to the establishment/maintenance of the ciliary zone of exclusion and to correct ciliary composition (Li et al., 2016; Jensen et al., 2015; Park & Leroux, 2022) (li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8).
- Localization and structure: Super-resolution imaging in nematodes and mammals shows MKS/TMEM proteins occupying discrete clustered rings along the TZ length; TMEM67/MKS-3 localizes at the membrane-proximal subdomain, suggesting association with Y-links and necklace structures that define the barrier’s architecture (Lambacher et al., 2016) (lambacher2016tmem107recruitsciliopathy pages 20-20).
- Genetic interactions and pathway context: MKS and NPHP module components act in parallel. While loss of individual MKS components (including mks-3) can yield modest effects, combined loss with NPHP-1 or NPHP-4 leads to severe defects: loss of basal body–TZ membrane anchoring, disrupted Y-links, axonemal defects, and compromised gating. This demonstrates cooperative action between modules to support ciliogenesis and ciliary signaling (Li et al., 2016; Jensen et al., 2015; Park & Leroux, 2022) (li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8).
- Signaling implications: By maintaining TZ integrity and the ciliary diffusion barrier, MKS-3 indirectly supports ciliary signaling by ensuring correct compartmentalization of signaling receptors and regulators, and by controlling ciliary lipid composition (e.g., limiting PIP2 abundance within cilia via TZ-dependent CIZE) (Jensen et al., 2015; Park & Leroux, 2022) (jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8).
- Recent mechanistic advance relevant to mks-3: Although demonstrated in vertebrate systems with complementary C. elegans assays, ADAMTS9-mediated cleavage of TMEM67 generates a TZ-localizing form essential for ciliogenesis/TZ assembly, while full-length TMEM67 retains Wnt signaling functions. This separation provides a mechanistic lens for interpreting worm mks-3 function: the membrane-proximal, TZ-resident form likely corresponds to the functional species fulfilling MKS-3’s role in the MKS module (Ahmed et al., 2024) (ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23).

Mandatory verification of identity and scope
- Gene/protein symbol and organism: The report concerns C. elegans mks-3 (UniProt Q20046), orthologous to human TMEM67/MKS3/Meckelin; all cited organism-specific functional conclusions are based on C. elegans experimental frameworks and conserved TZ biology drawn from authoritative sources (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8).
- Protein family/domains: Consistent with UniProt (PF09773/IPR019170 Meckelin domain), literature places MKS-3/TMEM67 as a membrane protein of the TZ MKS module (park2022compositionorganizationand pages 6-8, li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2).
- Ambiguity check: The symbol mks-3 can refer to MKS3/TMEM67 in various species; this report does not rely on similarly named, distinct genes from other organisms except to draw orthology-based insights. Where vertebrate data are referenced (e.g., TMEM67 cleavage), they are explicitly framed as orthology-informed context or mechanistic cross-validation, not as species substitution (ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23).

Selected references with URLs and publication dates
- Park & Leroux. Composition, organization and mechanisms of the transition zone, a gate for the cilium. EMBO Reports. Published Nov 2022. URL: https://doi.org/10.15252/embr.202255420 (park2022compositionorganizationand pages 6-8).
- Li et al. MKS5 and CEP290 dependent assembly pathway of the ciliary transition zone. PLoS Biology. Published Mar 2016. URL: https://doi.org/10.1371/journal.pbio.1002416 (li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2).
- Jensen et al. Formation of the transition zone by Mks5/Rpgrip1L establishes a ciliary zone of exclusion (CIZE). EMBO Journal. Published Oct 2015. URL: https://doi.org/10.15252/embj.201488044 (jensen2015formationofthe pages 1-2).
- Lambacher et al. TMEM107 recruits ciliopathy proteins to subdomains of the ciliary transition zone and causes Joubert syndrome. Nature Cell Biology. Published Nov 2016. URL: https://doi.org/10.1038/ncb3273 (lambacher2016tmem107recruitsciliopathy pages 20-20).
- Ahmed et al. Two functional forms of the Meckel-Gruber syndrome protein TMEM67 generated by proteolytic cleavage by ADAMTS9 mediate Wnt signaling and ciliogenesis. bioRxiv. Posted Sep 2024. URL: https://doi.org/10.1101/2024.09.04.611229 (ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23).
- Lange et al. Interpreting ciliopathy-associated missense variants of uncertain significance (VUS) in an animal model. bioRxiv. Posted Sep 22, 2021. URL: https://doi.org/10.1101/2021.06.17.448799 (lange2021interpretingciliopathyassociatedmissense pages 1-4).

Conclusions
- C. elegans mks-3 encodes the Meckelin/TMEM67 ortholog that localizes to the ciliary transition zone and functions within the MKS module to build a functional gating barrier. Its role is tightly integrated into a hierarchical TZ assembly pathway organized by MKS-5 and CEP-290. Genetic interactions between MKS and NPHP modules underscore parallel pathways that cooperatively ensure ciliogenesis and ciliary signaling. Recent evidence suggests TMEM67 possesses separable biochemical roles—TZ assembly tied to a cleaved membrane-proximal form and Wnt signaling mediated by the non-cleaved protein—which, together with C. elegans variant-assay pipelines, informs functional annotation and clinical variant interpretation of TMEM67/mks-3 (park2022compositionorganizationand pages 6-8, li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 1-2, jensen2015formationofthe pages 1-2, lambacher2016tmem107recruitsciliopathy pages 20-20, ahmed2024twofunctionalforms pages 37-39, ahmed2024twofunctionalforms pages 20-23, lange2021interpretingciliopathyassociatedmissense pages 1-4).

References

1. (li2016mks5andcep290 pages 2-3): Chunmei Li, Victor L. Jensen, Kwangjin Park, Julie Kennedy, Francesc R. Garcia-Gonzalo, Marta Romani, Roberta De Mori, Ange-Line Bruel, Dominique Gaillard, Bérénice Doray, Estelle Lopez, Jean-Baptiste Rivière, Laurence Faivre, Christel Thauvin-Robinet, Jeremy F. Reiter, Oliver E. Blacque, Enza Maria Valente, and Michel R. Leroux. Mks5 and cep290 dependent assembly pathway of the ciliary transition zone. PLOS Biology, 14:e1002416, Mar 2016. URL: https://doi.org/10.1371/journal.pbio.1002416, doi:10.1371/journal.pbio.1002416. This article has 165 citations and is from a highest quality peer-reviewed journal.

2. (jensen2015formationofthe pages 1-2): Victor L Jensen, Chunmei Li, Rachel V Bowie, Lara Clarke, Swetha Mohan, Oliver E Blacque, and Michel R Leroux. Formation of the transition zone by mks5/rpgrip1l establishes a ciliary zone of exclusion (cize) that compartmentalises ciliary signalling proteins and controls pip2 ciliary abundance. The EMBO Journal, 34:2537-2556, Oct 2015. URL: https://doi.org/10.15252/embj.201488044, doi:10.15252/embj.201488044. This article has 159 citations.

3. (park2022compositionorganizationand pages 6-8): Kwangjin Park and Michel R Leroux. Composition, organization and mechanisms of the transition zone, a gate for the cilium. EMBO reports, Nov 2022. URL: https://doi.org/10.15252/embr.202255420, doi:10.15252/embr.202255420. This article has 71 citations and is from a highest quality peer-reviewed journal.

4. (li2016mks5andcep290 pages 1-2): Chunmei Li, Victor L. Jensen, Kwangjin Park, Julie Kennedy, Francesc R. Garcia-Gonzalo, Marta Romani, Roberta De Mori, Ange-Line Bruel, Dominique Gaillard, Bérénice Doray, Estelle Lopez, Jean-Baptiste Rivière, Laurence Faivre, Christel Thauvin-Robinet, Jeremy F. Reiter, Oliver E. Blacque, Enza Maria Valente, and Michel R. Leroux. Mks5 and cep290 dependent assembly pathway of the ciliary transition zone. PLOS Biology, 14:e1002416, Mar 2016. URL: https://doi.org/10.1371/journal.pbio.1002416, doi:10.1371/journal.pbio.1002416. This article has 165 citations and is from a highest quality peer-reviewed journal.

5. (lambacher2016tmem107recruitsciliopathy pages 20-20): Nils J. Lambacher, Ange-Line Bruel, Teunis J. P. van Dam, Katarzyna Szymańska, Gisela G. Slaats, Stefanie Kuhns, Gavin J. McManus, Julie E. Kennedy, Karl Gaff, Ka Man Wu, Robin van der Lee, Lydie Burglen, Diane Doummar, Jean-Baptiste Rivière, Laurence Faivre, Tania Attié-Bitach, Sophie Saunier, Alistair Curd, Michelle Peckham, Rachel H. Giles, Colin A. Johnson, Martijn A. Huynen, Christel Thauvin-Robinet, and Oliver E. Blacque. Tmem107 recruits ciliopathy proteins to subdomains of the ciliary transition zone and causes joubert syndrome. Nature Cell Biology, 18:122-131, Nov 2016. URL: https://doi.org/10.1038/ncb3273, doi:10.1038/ncb3273. This article has 160 citations and is from a highest quality peer-reviewed journal.

6. (ahmed2024twofunctionalforms pages 37-39): Manu Ahmed, Sydney Fischer, Karyn L. Robert, Karen I. Lange, Michael W. Stuck, Sunayna Best, Colin A. Johnson, Gregory J. Pazour, Oliver E. Blacque, and Sumeda Nandadasa. Two functional forms of the meckel-gruber syndrome protein tmem67 generated by proteolytic cleavage by adamts9 mediate wnt signaling and ciliogenesis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.04.611229, doi:10.1101/2024.09.04.611229. This article has 0 citations and is from a poor quality or predatory journal.

7. (ahmed2024twofunctionalforms pages 20-23): Manu Ahmed, Sydney Fischer, Karyn L. Robert, Karen I. Lange, Michael W. Stuck, Sunayna Best, Colin A. Johnson, Gregory J. Pazour, Oliver E. Blacque, and Sumeda Nandadasa. Two functional forms of the meckel-gruber syndrome protein tmem67 generated by proteolytic cleavage by adamts9 mediate wnt signaling and ciliogenesis. bioRxiv, Sep 2024. URL: https://doi.org/10.1101/2024.09.04.611229, doi:10.1101/2024.09.04.611229. This article has 0 citations and is from a poor quality or predatory journal.

8. (lange2021interpretingciliopathyassociatedmissense pages 1-4): Karen I. Lange, Sunayna Best, Sofia Tsiropoulou, Ian Berry, Colin A. Johnson, and Oliver E. Blacque. Interpreting ciliopathy-associated missense variants of uncertain significance (vus) in an animal model. bioRxiv, Jun 2021. URL: https://doi.org/10.1101/2021.06.17.448799, doi:10.1101/2021.06.17.448799. This article has 0 citations and is from a poor quality or predatory journal.

Citations

1. park2022compositionorganizationand pages 6-8
2. lange2021interpretingciliopathyassociatedmissense pages 1-4
3. jensen2015formationofthe pages 1-2
4. ahmed2024twofunctionalforms pages 37-39
5. ahmed2024twofunctionalforms pages 20-23
6. https://doi.org/10.15252/embr.202255420;
7. https://doi.org/10.1371/journal.pbio.1002416;
8. https://doi.org/10.15252/embj.201488044
9. https://doi.org/10.1038/ncb3273
10. https://doi.org/10.1101/2024.09.04.611229
11. https://doi.org/10.15252/embr.202255420
12. https://doi.org/10.1101/2021.06.17.448799
13. https://doi.org/10.1371/journal.pbio.1002416
14. https://doi.org/10.1371/journal.pbio.1002416,
15. https://doi.org/10.15252/embj.201488044,
16. https://doi.org/10.15252/embr.202255420,
17. https://doi.org/10.1038/ncb3273,
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