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gene_id: mks-6
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protein_description: 'SubName: Full=C2 domain-containing protein {ECO:0000313|EMBL:CAA95830.1};'
gene_info: Name=mks-6 {ECO:0000313|EMBL:CAA95830.1, ECO:0000313|WormBase:K07G5.3};
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organism_full: Caenorhabditis elegans.
protein_family: Not specified in UniProt
protein_domains: C2_dom. (IPR000008); C2_domain_sf. (IPR035892); CC2D2AN-C2. (IPR028928);
CEPT76/DRC7_peptidase-like_dom. (IPR056290); Tectonic-like_complex_comp. (IPR052434)
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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: Q21303
• Protein Description: SubName: Full=C2 domain-containing protein {ECO:0000313|EMBL:CAA95830.1};
• Gene Information: Name=mks-6 {ECO:0000313|EMBL:CAA95830.1, ECO:0000313|WormBase:K07G5.3}; ORFNames=CELE_K07G5.3 {ECO:0000313|EMBL:CAA95830.1}, K07G5.3 {ECO:0000313|WormBase:K07G5.3};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: C2_dom. (IPR000008); C2_domain_sf. (IPR035892); CC2D2AN-C2. (IPR028928); CEPT76/DRC7_peptidase-like_dom. (IPR056290); Tectonic-like_complex_comp. (IPR052434)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "mks-6" 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-6' 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-6 (gene ID: mks-6, UniProt: Q21303) 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: Q21303
• Protein Description: SubName: Full=C2 domain-containing protein {ECO:0000313|EMBL:CAA95830.1};
• Gene Information: Name=mks-6 {ECO:0000313|EMBL:CAA95830.1, ECO:0000313|WormBase:K07G5.3}; ORFNames=CELE_K07G5.3 {ECO:0000313|EMBL:CAA95830.1}, K07G5.3 {ECO:0000313|WormBase:K07G5.3};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Not specified in UniProt
• Key Domains: C2_dom. (IPR000008); C2_domain_sf. (IPR035892); CC2D2AN-C2. (IPR028928); CEPT76/DRC7_peptidase-like_dom. (IPR056290); Tectonic-like_complex_comp. (IPR052434)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "mks-6" 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-6' 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-6 (gene ID: mks-6, UniProt: Q21303) 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 report: mks-6 (CC2D2A ortholog) in Caenorhabditis elegans (UniProt Q21303)

Verification of gene/protein identity and domain architecture
- Identity and orthology: mks-6 encodes the C. elegans ortholog of human CC2D2A, a Meckel syndrome/Joubert syndrome-associated transition zone (TZ) protein. Multiple studies explicitly list “MKS-6 (Cc2d2a)” as an MKS-module component in C. elegans TZ research (Jensen et al., 2015, The EMBO Journal, published Oct 2015: https://doi.org/10.15252/embj.201488044; Li et al., 2016, PLOS Biology, published Mar 2016: https://doi.org/10.1371/journal.pbio.1002416) (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3).
- Domain features: mks-6/CC2D2A is described as a coiled-coil protein containing a C2 domain, consistent with membrane- and scaffold-associated functions at the TZ (Park, 2019, review; see cilia section; publication year 2019) (park2019ciliumlengthregulationa pages 21-24, park2019ciliumlengthregulation pages 21-24). This matches the UniProt domain annotation (C2) provided by the user and aligns with CC2D2A-N/C2 domain family classifications.
- Organism correctness: All cited works explicitly perform or interpret experiments in C. elegans (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2022compositionorganizationand pages 6-8).

1) Key concepts and definitions with current understanding
- Transition zone (TZ) and gating: The TZ is the proximal ciliary domain containing Y-links and the ciliary necklace that establishes a selective diffusion barrier controlling protein and lipid composition of the cilium (“ciliary gate”). These features and functions are conserved across eukaryotes and were defined by ultrastructure and genetic/proteomic mapping (Gonçalves & Pelletier, 2017, Molecules and Cells, published Apr 2017: https://doi.org/10.14348/molcells.2017.0054; Park & Leroux, 2022, EMBO Reports, published Nov 2022: https://doi.org/10.15252/embr.202255420) (goncalves2017theciliarytransition pages 1-3, park2022compositionorganizationand pages 6-8).
- MKS and NPHP modules: TZ proteins partition into at least two major, partially redundant modules—MKS and NPHP—identified by genetic interactions and localization dependencies; CEP-290 acts as a central assembly factor, and MKS-5/RPGRIP1L is an upstream scaffold that coordinates both modules (Li et al., 2016, PLOS Biology; Jensen et al., 2015, The EMBO Journal) (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2).
- Position of MKS-6: MKS-6/CC2D2A is a canonical MKS-module component at the TZ. Its organization and function are considered alongside other MKS-module proteins such as MKS-1, MKS-2 (TMEM216), MKS-3 (TMEM67), the B9 complex (MKSR-1/B9D1, MKSR-2/B9D2), and TMEM family members (TMEM231, TMEM107, TMEM218) (Jensen et al., 2015; Li et al., 2016; Park & Leroux, 2022) (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2022compositionorganizationand pages 6-8).

2) Recent developments and latest research (priority to 2023–2024)
- While direct 2023–2024 mks-6-specific primary reports are limited in the retrieved evidence, an updated synthesis in 2022 (Park & Leroux, EMBO Reports) consolidates TZ architecture and gating mechanisms across organisms, emphasizing the hierarchical assembly anchored by MKS-5 and CEP-290 and the integration of MKS components (including MKS-6/CC2D2A) into the gate’s structural and functional model (published Nov 2022: https://doi.org/10.15252/embr.202255420) (park2022compositionorganizationand pages 6-8).
- Broad conceptual advances emphasized by the 2022 review include multiple, potentially cooperative gating mechanisms: protein “picket fences,” specialized lipids, membrane curvature/thickness effects, and size-selective sieving integrated with intraflagellar transport (IFT) systems—frameworks that contextualize the role of MKS-6 in maintaining ciliary compartmentalization (park2022compositionorganizationand pages 6-8).

3) Current applications and real-world implementations
- Disease modeling and variant interpretation: Because mks-6 is orthologous to human CC2D2A, a gene mutated in ciliopathies (Meckel, Joubert syndromes), C. elegans provides a tractable system to model TZ assembly defects, assess gating phenotypes and ultrastructure, and test genetic interactions that mirror human disease complexity (Jensen et al., 2015; Li et al., 2016; Park & Leroux, 2022) (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2022compositionorganizationand pages 6-8).
- Assays and readouts: Established readouts include TZ protein localization dependencies, membrane protein leakage into cilia (e.g., mislocalization/accumulation of periciliary membrane proteins), and transmission electron microscopy (TEM) to visualize TZ Y-links and basal body–membrane attachments. These assays are routinely applied to MKS-module mutants (including mks-6) and to combinations with NPHP-module mutants to reveal synthetic defects (Jensen et al., 2015; Li et al., 2016) (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3).

4) Expert opinions and analysis from authoritative sources
- Park & Leroux (2022) integrates genetic, structural, and biochemical perspectives to argue that TZ integrity results from an interdigitated network of MKS/NPHP components and accessory factors, with MKS-5 and CEP-290 orchestrating assembly and MKS-6/CC2D2A contributing as a conserved MKS-module component at the membrane–axoneme interface (EMBO Reports; published Nov 2022: https://doi.org/10.15252/embr.202255420) (park2022compositionorganizationand pages 6-8).
- Jensen et al. (2015) introduced the “ciliary zone of exclusion” (CIZE) concept at the TZ, linking MKS-5-dependent assembly to control of signaling protein compartmentalization and PIP2 levels, thus providing a mechanistic framework for how MKS-module components, including MKS-6, maintain ciliary composition (The EMBO Journal; published Oct 2015: https://doi.org/10.15252/embj.201488044) (jensen2015formationofthe pages 1-2).
- Li et al. (2016) demonstrated a hierarchical assembly pathway in which MKS-5 scaffolds the TZ and CEP-290 promotes assembly/localization of many MKS components—principles that encompass MKS-6 and rationalize genetic interaction patterns in C. elegans and human ciliopathies (PLOS Biology; published Mar 2016: https://doi.org/10.1371/journal.pbio.1002416) (li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 9-11, li2016mks5andcep290 pages 3-5).

5) Relevant statistics and data from recent studies (mks-6 within module context)
- Gating phenotypes: Loss of core TZ assembly factors disrupts barrier function with membrane-associated proteins mislocalized into cilia; in C. elegans, this includes aberrant presence or leakage of markers such as ARL-13 and periciliary proteins, quantified in cep-290 and related TZ mutants, and conceptually applies to MKS-module defects encompassing mks-6 (Li et al., 2016; Jensen et al., 2015) (li2016mks5andcep290 pages 9-11, jensen2015formationofthe pages 1-2).
- Ultrastructure: Severe TZ defects in C. elegans double mutants that combine MKS- and NPHP-module losses include loss of Y-links, failure of basal body–TZ membrane anchoring, and disorganized or shortened axonemal microtubules; these data emerge from systematic TEM analyses across genotypes and define the synthetic nature of MKS–NPHP interactions (Li et al., 2016; Jensen et al., 2015) (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2).

Functional summary for mks-6 (primary role, processes, localization, and pathway placement)
- Primary role and molecular function: MKS-6 is a conserved MKS-module component with coiled-coil and C2 domains acting within the TZ as part of the ciliary gate. Its molecular role is structural/scaffold-associated rather than enzymatic, helping establish and maintain compartmentalization of ciliary proteins and lipids in cooperation with other MKS/TZ components (Park, 2019; Jensen et al., 2015; Li et al., 2016; Park & Leroux, 2022) (park2019ciliumlengthregulationa pages 21-24, jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2022compositionorganizationand pages 6-8).
- Subcellular localization: MKS-6 localizes to the ciliary TZ; within this compartment it contributes to the “zone of exclusion” that demarcates proximal cilia from periciliary membrane and regulates molecule flux (Jensen et al., 2015; Li et al., 2016) (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3).
- Complex/module membership and hierarchy: MKS-6 is embedded in the MKS module with B9 complex proteins (MKSR-1/B9D1, MKSR-2/B9D2), TMEM family members (e.g., TMEM231, TMEM107, TMEM218), and associated factors. MKS-5/RPGRIP1L acts upstream to scaffold both MKS and NPHP modules; CEP-290 is required for assembly/localization of many MKS components, positioning MKS-6 within a CEP-290–dependent TZ assembly branch (Li et al., 2016; Jensen et al., 2015; Park & Leroux, 2022) (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8).
- Genetic and pathway context: Genetic interactions between MKS and NPHP modules are partially redundant for ciliogenesis; double mutants can exhibit severe TZ ultrastructure and gating defects, whereas individual MKS mutants show compromised gating with variable effects on cilium length/structure depending on genetic background and the specific factor perturbed (Jensen et al., 2015; Li et al., 2016; Park & Leroux, 2022; Gonçalves & Pelletier, 2017) (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2022compositionorganizationand pages 6-8, goncalves2017theciliarytransition pages 1-3).

Recent reviews and synthesis relevant to 2023–2024
- The 2022 EMBO Reports review (Park & Leroux) remains a current, authoritative synthesis of TZ composition, organization, and barrier mechanisms, and directly contextualizes MKS-6 within conserved MKS module biology and TZ assembly logic (published Nov 2022: https://doi.org/10.15252/embr.202255420) (park2022compositionorganizationand pages 6-8).

Embedded summary table of key facts and sources
| Category | Summary | Key sources (year) |
|---|---|---|
| Identity / ortholog | C. elegans mks-6 corresponds to the worm ortholog of human CC2D2A (UniProt Q21303). | Jensen 2015, Li 2016, Park 2019/2022 (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2019ciliumlengthregulationa pages 21-24, park2022compositionorganizationand pages 6-8) |
| Protein / domain features | Predicted coiled-coil protein containing a C2 domain; consistent with membrane/structural roles at the TZ. | Park 2019, Jensen 2015 (park2019ciliumlengthregulationa pages 21-24, jensen2015formationofthe pages 1-2) |
| Subcellular localization | Localizes to the ciliary transition zone (TZ), contributing to proximal TZ subdomains / zone-of-exclusion that compartmentalize ciliary proteins. | Jensen 2015, Li 2016, Park 2022 (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2022compositionorganizationand pages 6-8) |
| Complex / module membership | Member of the genetically defined MKS module at the TZ (with B9 proteins and multiple TMEMs). Functionally linked to MKS-5 (RPGRIP1L) and CEP-290. | Li 2016, Jensen 2015, Park 2022 (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8) |
| Assembly dependencies / hierarchy | MKS-5 acts upstream as a scaffold; CEP-290 is required for assembling/localizing many MKS components (CEP-290–dependent branch); MKS-6 localization reflects this hierarchical assembly. | Li 2016, Jensen 2015, Park 2022 (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8) |
| Genetic & physical interactions | Genetic and proteomic links to TMEM family members (e.g., TMEM-231/107/218), the B9 complex (MKSR-1/B9D1, MKSR-2/B9D2), and cross-talk / synthetic interactions with NPHP module genes. | Li 2016, Park 2022, Jensen 2015 (li2016mks5andcep290 pages 2-3, park2022compositionorganizationand pages 6-8, jensen2015formationofthe pages 1-2) |
| Mutant phenotypes in worms | As part of MKS module, defects cause impaired TZ gating (membrane protein leakage), dye-filling abnormalities; double mks;nphp mutants show severe ciliogenesis/TZ ultrastructure loss (loss of Y-links, basal body–TZ membrane attachments, axonemal defects). | Li 2016, Jensen 2015, Park 2022 (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8) |
| Recent developments (2022–2024) | Updated TZ architecture and gating models synthesize genetic, proteomic and imaging data; new TMEM component studies and functional refinements reported in 2022–2024 reviews and preprints. | Park 2022, Gonçalves 2017, recent TMEM/TMEM67 preprints (park2022compositionorganizationand pages 6-8, goncalves2017theciliarytransition pages 1-3) |
| Applications / real-world | C. elegans mks-6 serves as a model for human CC2D2A ciliopathies, variant interpretation, and assays of TZ gating/compartmentalization (dye-fill, leakage, TEM/EM phenotyping). | Li 2016, Jensen 2015, Park 2022 (li2016mks5andcep290 pages 2-3, jensen2015formationofthe pages 1-2, park2022compositionorganizationand pages 6-8) |

Table: Compact, evidence‑backed table summarizing identity, domain features, localization, module membership, interactions, phenotypes, recent developments (2022–2024), and applications for C. elegans mks-6 (UniProt Q21303). Citations link to extracted context IDs used in the synthesis.

References (URLs and publication dates)
- Jensen VL et al. 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. Published Oct 2015. https://doi.org/10.15252/embj.201488044 (jensen2015formationofthe pages 1-2).
- Li C et al. MKS5 and CEP290 Dependent Assembly Pathway of the Ciliary Transition Zone. PLOS Biology. Published Mar 2016. https://doi.org/10.1371/journal.pbio.1002416 (li2016mks5andcep290 pages 2-3, li2016mks5andcep290 pages 9-11, li2016mks5andcep290 pages 3-5).
- Park K. Cilium length regulation in Caenorhabditis elegans. Review. Published 2019. (Context excerpt confirming CC2D2A/C2/coiled-coil features and MKS module placement.) (park2019ciliumlengthregulationa pages 21-24, park2019ciliumlengthregulation pages 21-24).
- Park K, Leroux MR. Composition, organization and mechanisms of the transition zone, a gate for the cilium. EMBO Reports. Published Nov 2022. https://doi.org/10.15252/embr.202255420 (park2022compositionorganizationand pages 6-8).
- Gonçalves J, Pelletier L. The Ciliary Transition Zone: Finding the Pieces and Assembling the Gate. Molecules and Cells. Published Apr 2017. https://doi.org/10.14348/molcells.2017.0054 (goncalves2017theciliarytransition pages 1-3).

Notes on symbol ambiguity
- The symbol “mks-6” is used consistently in C. elegans to denote the CC2D2A ortholog localized to the TZ; literature reviewed here is explicitly in C. elegans and aligns with the UniProt entry Q21303, including C2/coiled-coil domain architecture and TZ function (jensen2015formationofthe pages 1-2, li2016mks5andcep290 pages 2-3, park2019ciliumlengthregulationa pages 21-24, park2022compositionorganizationand pages 6-8).

References

1. (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.

2. (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.

3. (park2019ciliumlengthregulationa pages 21-24): K Park. Cilium length regulation in caenorhabditis elegans. Unknown journal, 2019.

4. (park2019ciliumlengthregulation pages 21-24): K Park. Cilium length regulation in caenorhabditis elegans. Unknown journal, 2019.

5. (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.

6. (goncalves2017theciliarytransition pages 1-3): João Gonçalves and Laurence Pelletier. The ciliary transition zone: finding the pieces and assembling the gate. Molecules and Cells, 40:243-253, Apr 2017. URL: https://doi.org/10.14348/molcells.2017.0054, doi:10.14348/molcells.2017.0054. This article has 234 citations and is from a peer-reviewed journal.

7. (li2016mks5andcep290 pages 9-11): 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.

8. (li2016mks5andcep290 pages 3-5): 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.

Citations

1. park2022compositionorganizationand pages 6-8
2. jensen2015formationofthe pages 1-2
3. goncalves2017theciliarytransition pages 1-3
4. park2019ciliumlengthregulationa pages 21-24
5. park2019ciliumlengthregulation pages 21-24
6. https://doi.org/10.15252/embj.201488044;
7. https://doi.org/10.1371/journal.pbio.1002416
8. https://doi.org/10.14348/molcells.2017.0054;
9. https://doi.org/10.15252/embr.202255420
10. https://doi.org/10.15252/embj.201488044
11. https://doi.org/10.14348/molcells.2017.0054
12. https://doi.org/10.15252/embj.201488044,
13. https://doi.org/10.1371/journal.pbio.1002416,
14. https://doi.org/10.15252/embr.202255420,
15. https://doi.org/10.14348/molcells.2017.0054,