provider: falcon
model: Edison Scientific Literature
cached: false
start_time: '2025-12-28T00:20:38.036510'
end_time: '2025-12-28T00:25:13.199703'
duration_seconds: 275.16
template_file: templates/gene_research_go_focused.md
template_variables:
organism: worm
gene_id: epg-5
gene_symbol: epg-5
uniprot_accession: Q18892
protein_description: 'RecName: Full=Ectopic P granules protein 5;'
gene_info: Name=epg-5 {ECO:0000312|WormBase:C56C10.12}; ORFNames=C56C10.12 {ECO:0000312|WormBase:C56C10.12};
organism_full: Caenorhabditis elegans.
protein_family: Belongs to the EPG5 family. .
protein_domains: Autophagy-related_EPG5. (IPR051436)
provider_config:
timeout: 600
max_retries: 3
parameters:
allowed_domains: []
temperature: 0.1
citation_count: 12

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: Q18892
• Protein Description: RecName: Full=Ectopic P granules protein 5;
• Gene Information: Name=epg-5 {ECO:0000312|WormBase:C56C10.12}; ORFNames=C56C10.12 {ECO:0000312|WormBase:C56C10.12};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the EPG5 family. .
• Key Domains: Autophagy-related_EPG5. (IPR051436)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "epg-5" 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 'epg-5' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene epg-5 (gene ID: epg-5, UniProt: Q18892) 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: Q18892
• Protein Description: RecName: Full=Ectopic P granules protein 5;
• Gene Information: Name=epg-5 {ECO:0000312|WormBase:C56C10.12}; ORFNames=C56C10.12 {ECO:0000312|WormBase:C56C10.12};
• Organism (full): Caenorhabditis elegans.
• Protein Family: Belongs to the EPG5 family. .
• Key Domains: Autophagy-related_EPG5. (IPR051436)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "epg-5" 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 'epg-5' is ambiguous or literature is limited for this specific protein"
- Explain what you found (e.g., "Found extensive literature on a different gene with the same symbol in a different organism")
- Describe the protein based ONLY on the UniProt information provided above
- Suggest that the protein function can be inferred from domain/family information

Research Target:

Please provide a comprehensive research report on the gene epg-5 (gene ID: epg-5, UniProt: Q18892) 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 overview: We verified identity and domain/family alignment for C. elegans epg-5 (UniProt Q18892) and gathered recent primary and review literature emphasizing mechanistic function, localization, phenotypes, pathway context, and translational links. We synthesized experimental evidence from C. elegans and conserved human studies, prioritized 2023–2024 sources where available, and compiled quantitative data and assay implementations in worms. All claims below are supported by specific citations.

Comprehensive research report on C. elegans epg-5 (EPG-5)

1) Key concepts, definitions, and current understanding
- Identity and family: epg-5 encodes Ectopic P granules protein 5 (EPG-5), a metazoan-specific autophagy tethering factor in the EPG5 family that functions at the terminal step of autophagy to enforce fusion specificity between autophagosomes and late endosomes/lysosomes (autolysosome formation) (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021) (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 1-3).
- Molecular role: EPG-5 is a Rab7 effector that binds late endosomes/lysosomes. It also engages autophagosomal Atg8/LC3 ortholog LGG-1 via conserved LIR motifs, and coordinates the STX17–SNAP29–VAMP7/8 trans-SNARE machinery to specify and promote autophagosome–lysosome fusion (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021) (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 1-3, wang2016thevicisyndrome pages 6-9).
- Step in autophagy: EPG-5 acts after autophagosome completion, at the docking/fusion stage with late endosomes/lysosomes. Loss of epg-5 causes accumulation of non-degradative hybrid vesicles and non-functional autolysosomes containing both autophagosomal and endosomal markers (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021; Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 1-3, wang2019therbg1–rbg2complex pages 4-7).

2) Recent developments and latest research (emphasis 2023–2024)
- Expanded pathway connections to endocytic recycling and signaling: New work shows EPG-5 modulates retrograde endocytic trafficking in C. elegans development, impacting TGF-β (SMA-6 receptor) and WNT (WLS/MIG-14) pathways. In epg-5 mutants, SMA-6 and MIG-14 are trapped in hybrid endosomal structures co-localizing with SNX-1 or SNX-3; defects in RAB-5→RAB-7 and RAB-5→RAB-10 conversion generate hybrid vesicles. Notably, HOPS knockdown ameliorates trafficking and autophagy defects, linking EPG-5 to endosome maturation machinery (Apr 2025; https://doi.org/10.1080/15548627.2025.2485420) (yuan2025epg5regulatestgfbtgfβ pages 1-2).
- Disease spectrum and translational genetics: A 2024 multicenter cohort analysis (n=200 individuals with recessive EPG5 variants) extends the spectrum of EPG5-related disorders from classic Vici syndrome to milder neurodevelopmental/neurodegenerative phenotypes, including epilepsy, dystonia, and early-onset parkinsonism; genotype–phenotype patterns suggest residual expression correlates with severity (Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (dafsari2024mutationsinepg5 pages 9-12, dafsari2024mutationsinepg5 pages 24-27).

3) Primary function, localization, pathways, and worm phenotypes
- Molecular interactions and mechanism:
- Rab GTPase and SNARE interface: EPG-5 binds RAB-7 and the R-SNARE VAMP7/8 on late endosomes/lysosomes, and associates with the Qabc SNARE complex STX17–SNAP29 assembled on autophagosomes. In reconstituted liposome systems, EPG-5 promotes STX17–SNAP29–VAMP7/8 fusion, defining its role as a fusion-tethering factor. Depletion alters SNARE pairing (e.g., increased STX17–SNAP25–VAMP8) indicating a role in fusion specificity (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021) (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 1-3).
- ATG8-family binding: EPG-5 directly binds LGG-1 through conserved LIR motifs (two canonical motifs within residues 500–530). Mutation or deletion of this region abolishes LGG-1 binding, supporting EPG-5’s engagement with autophagosomal membranes (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021) (wang2016thevicisyndrome pages 6-9).
- Subcellular localization: In worms, EPG-5 localizes to late endosomes/lysosomes via RAB-7, and to sites of autophagosome–lysosome interaction; epg-5 mutants accumulate enlarged vesicles co-labeled by autophagy (LGG-1) and endosomal/lysosomal markers (RAB-7, RAB-10, NUC-1 reporters), reflecting hybrid non-degradative autolysosomes (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021; Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2016thevicisyndrome pages 3-5, wang2019therbg1–rbg2complex pages 4-7).
- Pathway context and genetic interactions:
- epg-5 functions downstream in the autophagy pathway, at maturation/fusion, interfacing with RAB-7 and HOPS-dependent endolysosomal machinery; loss of rbg-1 (component of the RBG-1–RBG-2 complex) genetically suppresses epg-5 phenotypes by promoting lysosomal biogenesis and restoring acidification and flux, partly via modulating RAB-7 dynamics (Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2019therbg1–rbg2complex pages 1-2, wang2019therbg1–rbg2complex pages 4-7).
- epg-5 intersects with endocytic recycling and retrograde transport (RAB-5→RAB-7, RAB-5→RAB-10 conversion), impacting TGF-β and WNT receptor trafficking and hence developmental outcomes (Apr 2025; https://doi.org/10.1080/15548627.2025.2485420) (yuan2025epg5regulatestgfbtgfβ pages 1-2).
- Worm phenotypes:
- Autophagy defects: epg-5 mutants accumulate GFP::LGG-1 puncta and non-acidic enlarged hybrid vesicles bearing autophagosomal and endosomal markers; lysosomal acidification and degradation reporters (e.g., NUC-1 tandem reporters) indicate impaired delivery/acidification; FRAP shows reduced RAB-7 mobility on late endosomes/lysosomes (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021; Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2016thevicisyndrome pages 3-5, wang2019therbg1–rbg2complex pages 4-7).
- Mitophagy and neuro-motor phenotypes: epg-5 knockdown in worms increases LGG-1 autophagosome puncta and DCT-1 mitophagy puncta, consistent with impaired clearance; locomotor defects were quantified in RNAi-fed animals (methods: three biological replicates of 10 day-1 adults per replicate) (Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (dafsari2024mutationsinepg5 pages 24-27).

4) Expert opinions and analyses from authoritative sources
- Canonical fusion-tether model: The Mol Cell study (2016) provides the authoritative mechanistic framework placing EPG-5 as a Rab7-dependent tether that ensures correct SNARE pairing for autophagosome–lysosome fusion, preventing mistargeted fusion with other compartments (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021) (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 1-3).
- Autophagy-endocytosis crosstalk and disease implications: New data emphasize EPG-5’s role in endocytic retrograde trafficking and receptor recycling, mechanistically connecting autophagy defects to developmental signaling alterations and suggesting convergence with HOPS-dependent lysosomal fusion. This provides a unifying explanation for epg-5 pleiotropy and informs ALS/Vici syndrome pathogenesis (Apr 2025; https://doi.org/10.1080/15548627.2025.2485420) (yuan2025epg5regulatestgfbtgfβ pages 1-2).
- Genetic modifiers of EPG5 deficiency: The RBG-1–RBG-2 complex modulates lysosomal biogenesis/function and RAB-7 dynamics to suppress epg-5 defects, highlighting lysosome-centered therapeutic angles for EPG5-related disease (Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2019therbg1–rbg2complex pages 1-2, wang2019therbg1–rbg2complex pages 4-7).

5) Relevant statistics, data, and assays
- Human cohort statistics: 200 individuals with recessive EPG5 variants were compiled, delineating a spectrum from classic Vici syndrome to milder neurodevelopmental/neurodegenerative presentations, with genotype–phenotype correlations suggesting residual expression modifies severity (Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (dafsari2024mutationsinepg5 pages 9-12).
- C. elegans experimental numbers and quantitation:
- RNAi locomotion and mitophagy assays: three biological replicates of n=10 day‑1 adults each per condition were used to quantify locomotor phenotypes and mitophagy/autophagy puncta (Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (dafsari2024mutationsinepg5 pages 24-27).
- Lysosome function and RAB-7 dynamics: quantitative imaging of NUC-1 tandem reporters and pH-sensitive probes, volumes/intensity of lysosomal structures (n≈10 animals/condition, mean±s.e.m.), FRAP of GFP–RAB-7 mobility, and GST–RILP pulldown for GTP-RAB-7 were used to define suppression of epg-5 defects by rbg-1 loss (Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2019therbg1–rbg2complex pages 4-7).
- Core worm assays used to define epg-5 function:
- Autophagosome markers: GFP::LGG-1 puncta quantification and colocalization with RAB-7-labeled late endosomes (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021) (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 6-9).
- Lysosomal delivery/acidification reporters: NUC-1::sfGFP::mCherry (tandem pH-insensitive/sensitive), NUC-1::pHTomato, indicating impaired acidification in epg-5 mutants (Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2019therbg1–rbg2complex pages 4-7).
- Endosomal/recycling markers and conversions: RAB-5, RAB-7, RAB-10 conversions and SNX-1/SNX-3 colocalization to define hybrid vesicles; suppression by HOPS KD (Apr 2025; https://doi.org/10.1080/15548627.2025.2485420) (yuan2025epg5regulatestgfbtgfβ pages 1-2).
- Selective autophagy/mitophagy: DCT-1 (BNIP3 homolog) mitophagy puncta and LGG‑1 reporters to quantify impaired mitophagic clearance upon epg-5 perturbation (Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (dafsari2024mutationsinepg5 pages 24-27).

6) Biological inference and pathway integration in C. elegans
- Primary role and substrate specificity: EPG-5 is not an enzyme or transporter; it is a vesicle tethering/scaffolding factor that enforces fidelity of autophagosome–lysosome fusion. Its “substrates” are membrane-bound fusion intermediates: it recognizes Rab7-positive late endosomes/lysosomes and LC3/LGG-1-decorated autophagosomes, stabilizing STX17–SNAP29–VAMP7/8 to drive correct fusion and prevent aberrant SNARE pairing (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021) (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 1-3, wang2016thevicisyndrome pages 6-9).
- Cellular site of action: Cytosolic peripheral localization at late endosome/lysosome membranes and autophagosome–lysosome contact sites characterized by RAB-7 and VAMP7/8 presence (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021; Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2016thevicisyndrome pages 3-5, wang2019therbg1–rbg2complex pages 4-7).
- Pathway crosstalk: EPG-5 bridges autophagy and the endocytic/recycling routes. In worms, epg-5 ensures proper retrograde trafficking of SMA-6 and MIG-14, thereby modulating TGF-β-dependent body size and WNT-dependent cell migration; HOPS dependency emphasizes its role at the endosome–lysosome interface (Apr 2025; https://doi.org/10.1080/15548627.2025.2485420) (yuan2025epg5regulatestgfbtgfβ pages 1-2).

7) Conservation to human EPG5 and disease relevance
- Mechanistic conservation: The Rab7-effector, LC3/Atg8-binding, and SNARE-fusion roles are conserved features of EPG5 orthologs; mutations in human EPG5 cause Vici syndrome and broader EPG5-related disorders, aligning with the fusion-defect model established in C. elegans (Sep 2016; https://doi.org/10.1016/j.molcel.2016.08.021; Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (wang2016thevicisyndrome pages 3-5, dafsari2024mutationsinepg5 pages 9-12).
- Clinical spectrum and quantitative data: A 2024 cohort of 200 patients delineates a continuum from severe, classic Vici syndrome to milder neurodevelopmental/neurodegenerative disease; functional studies in patient fibroblasts demonstrate impaired PINK1/PRKN mitophagy, mirroring worm epg-5 mitophagy/autophagy defects (Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (dafsari2024mutationsinepg5 pages 9-12, dafsari2024mutationsinepg5 pages 24-27).

8) Current applications and real-world implementations (C. elegans)
- Flux and cargo assays: LGG-1 puncta and tandem reporters (e.g., NUC-1::sfGFP::mCherry; NUC-1::pHTomato) quantify delivery and acidification defects in epg-5 mutants; FRAP of GFP–RAB-7 and GST–RILP pulldown quantify RAB-7 dynamics/state (Oct 2019; https://doi.org/10.1242/jcs.234195) (wang2019therbg1–rbg2complex pages 4-7).
- Endosomal trafficking readouts: RAB-5/RAB-7/RAB-10 conversion analyses and SNX-1/SNX-3 colocalization identify hybrid vesicles; HOPS RNAi epistasis tests mechanistic positions (Apr 2025; https://doi.org/10.1080/15548627.2025.2485420) (yuan2025epg5regulatestgfbtgfβ pages 1-2).
- Selective autophagy/mitophagy reporter usage in vivo: DCT-1 mitophagy puncta with LGG-1 and locomotion assays to quantify functional consequences of epg-5 knockdown (Jun 2024; https://doi.org/10.1101/2024.06.12.24308722) (dafsari2024mutationsinepg5 pages 24-27).

Conclusions
EPG-5/epg-5 is a conserved metazoan autophagy tether that specifies and promotes the fusion of autophagosomes with late endosomes/lysosomes through coordinated Rab7/Atg8 and SNARE interactions. In C. elegans, epg-5 loss yields hybrid, non-degradative autolysosomes, impaired acidification, and stalled selective autophagy (including mitophagy). Recent work highlights epg-5’s broader role in retrograde endocytic trafficking that modulates TGF-β and WNT signaling, providing a mechanistic bridge between autophagy and developmental signaling. Human genetics consolidates the fusion-defect model and expands the EPG5-related disease spectrum, with quantitative cohorts and functional patient-cell phenotypes mirroring nematode biology (wang2016thevicisyndrome pages 3-5, wang2016thevicisyndrome pages 1-3, wang2016thevicisyndrome pages 6-9, wang2019therbg1–rbg2complex pages 4-7, yuan2025epg5regulatestgfbtgfβ pages 1-2, dafsari2024mutationsinepg5 pages 9-12, dafsari2024mutationsinepg5 pages 24-27).

References

1. (wang2016thevicisyndrome pages 3-5): Zheng Wang, Guangyan Miao, Xue-Yi Xue, Xiangyang Guo, Chongzhen Yuan, Zhaoyu Wang, Gangming Zhang, Yingyu Chen, Du Feng, Junjie Hu, and Hong Zhang. The vici syndrome protein epg5 is a rab7 effector that determines the fusion specificity of autophagosomes with late endosomes/lysosomes. Molecular cell, 63 5:781-95, Sep 2016. URL: https://doi.org/10.1016/j.molcel.2016.08.021, doi:10.1016/j.molcel.2016.08.021. This article has 331 citations and is from a highest quality peer-reviewed journal.

2. (wang2016thevicisyndrome pages 1-3): Zheng Wang, Guangyan Miao, Xue-Yi Xue, Xiangyang Guo, Chongzhen Yuan, Zhaoyu Wang, Gangming Zhang, Yingyu Chen, Du Feng, Junjie Hu, and Hong Zhang. The vici syndrome protein epg5 is a rab7 effector that determines the fusion specificity of autophagosomes with late endosomes/lysosomes. Molecular cell, 63 5:781-95, Sep 2016. URL: https://doi.org/10.1016/j.molcel.2016.08.021, doi:10.1016/j.molcel.2016.08.021. This article has 331 citations and is from a highest quality peer-reviewed journal.

3. (wang2016thevicisyndrome pages 6-9): Zheng Wang, Guangyan Miao, Xue-Yi Xue, Xiangyang Guo, Chongzhen Yuan, Zhaoyu Wang, Gangming Zhang, Yingyu Chen, Du Feng, Junjie Hu, and Hong Zhang. The vici syndrome protein epg5 is a rab7 effector that determines the fusion specificity of autophagosomes with late endosomes/lysosomes. Molecular cell, 63 5:781-95, Sep 2016. URL: https://doi.org/10.1016/j.molcel.2016.08.021, doi:10.1016/j.molcel.2016.08.021. This article has 331 citations and is from a highest quality peer-reviewed journal.

4. (wang2019therbg1–rbg2complex pages 4-7): Zhaoyu Wang, Hongyu Zhao, Chongzhen Yuan, Dongfeng Zhao, Yanan Sun, Xiaochen Wang, and Hong Zhang. The rbg-1–rbg-2 complex modulates autophagy activity by regulating lysosomal biogenesis and function in c. elegans. Journal of Cell Science, Oct 2019. URL: https://doi.org/10.1242/jcs.234195, doi:10.1242/jcs.234195. This article has 13 citations and is from a domain leading peer-reviewed journal.

5. (yuan2025epg5regulatestgfbtgfβ pages 1-2): Chongzhen Yuan, Huachuan Dong, Chunyan Wu, Jinyang Liu, Zheng Wang, Xingwei Wang, Haiyan Ren, Zhaoyu Wang, and Qun Lu. Epg-5 regulates tgfb/tgf-β and wnt signalling by modulating retrograde endocytic trafficking. Autophagy, pages 1-14, Apr 2025. URL: https://doi.org/10.1080/15548627.2025.2485420, doi:10.1080/15548627.2025.2485420. This article has 2 citations and is from a domain leading peer-reviewed journal.

6. (dafsari2024mutationsinepg5 pages 9-12): Hormos Salimi Dafsari, Celine Deneubourg, Kritarth Singh, Reza Maroofian, Zita Suprenant, Ay Lin Kho, Neil J Ingham, Karen P Steel, Preethi Sheshadri, Franciska Baur, Lea Hentrich, Birgit Gerisch, Mina Zamani, Cesar Alvares, Ata Siddiqui, Haidar S Dafsari, Mehri Salari, Anthony Lang, Michael Harris, Alice Abdelaleem, Saeid Sadeghian, Reza Azizimalamiri, Hamid Galehdari, Gholamreza Shariati, Alireza Sedaghat, Jawaher Zeighami, Daniel Calame, Dana Marafi, Ruizhi Duan, Adrian Boehnke, Carrie Mohila, Dora Steel, Saurabh Chopra, Suvasini Sharma, Nicolai Kohlschmidt, Steffi Patzer, Afshin Saffari, Darius Ebrahimi-Fakhari, Büşra Eser Çavdartepe, Irene J Chang, Erika Beckman, Renate Peters, Andrew Paul Fennell, Bernice Lo, Luisa Averdunk, Felix Distelmaier, Martina Baethmann, Frances Elmslie, Kairit Joost, Sheela Nampoothiri, Dhanya Yesodharan, Hannah Mandel, Amy Kimball, Antonie D. Kline, Cyril Mignot, Boris Keren, Vincent Laugel, Katrin Õunap, Kalpana Devadathan, Frederique M.C. van Berkestijn, Arpana Silwal, Saskia Koene, Sumit Verma, Mohammed Yousuf Karim, Chahynez Boubidi, Majid Aziz, Gehad ElGhazali, Lauren Mattas, Mohammad Miryounesi, Farzad Hashemi-Gorji, Shahryar Alavi, Nayereh Nouri, Mehrdad Noruzinia, Saeedeh Kavousi, Arveen Kamath, Sandeep Jayawant, Russell Saneto, Nourelhoda A. Haridy, Pinar Ozkan Kart, Ali Cansu, Claire Beneteau, Kyra E. Stuurman, Martina Wilke, Tahsin Stefan Barakat, Homa Tajsharghi, Annarita Scardamaglia, Sadeq Vallian, Semra Hız, Ali Shoeibi, Reza Boostani, Narges Hashemi, Meisam Babaei, Norah Saleh Alsaleh, Julie Lander, Tania Attié-Bitach, Pauline Marzin, Dorota Wicher, Jessica I Gold, Mariana H G Monje, Dimitri Krainc, Niccolò Mencacci, Somayeh Bakhtiari, Michael Kruer, Emanuela Argilli, Elliott Sherr, Yalda Jamshidi, Ehsan Ghayoor Karimiani, Yiu Wing Sunny Cheung, Ivan Karin, Wendy K Chung, James R. Lupski, Manju A. Kurian, Jörg Dötsch, Jürgen-Christoph von Kleist-Retzow, Thomas Klopstock, Matias Wagner, Calvin Yip, Andreas Roos, Carlo Dionisi-Vici, Mathias Gautel, Michael R Duchen, Adam Antebi, Henry Houlden, Manolis Fanto, and Heinz Jungbluth. Mutations in epg5 are associated with a wide spectrum of neurodevelopmental and neurodegenerative disorders. MedRxiv, Jun 2024. URL: https://doi.org/10.1101/2024.06.12.24308722, doi:10.1101/2024.06.12.24308722. This article has 3 citations.

7. (dafsari2024mutationsinepg5 pages 24-27): Hormos Salimi Dafsari, Celine Deneubourg, Kritarth Singh, Reza Maroofian, Zita Suprenant, Ay Lin Kho, Neil J Ingham, Karen P Steel, Preethi Sheshadri, Franciska Baur, Lea Hentrich, Birgit Gerisch, Mina Zamani, Cesar Alvares, Ata Siddiqui, Haidar S Dafsari, Mehri Salari, Anthony Lang, Michael Harris, Alice Abdelaleem, Saeid Sadeghian, Reza Azizimalamiri, Hamid Galehdari, Gholamreza Shariati, Alireza Sedaghat, Jawaher Zeighami, Daniel Calame, Dana Marafi, Ruizhi Duan, Adrian Boehnke, Carrie Mohila, Dora Steel, Saurabh Chopra, Suvasini Sharma, Nicolai Kohlschmidt, Steffi Patzer, Afshin Saffari, Darius Ebrahimi-Fakhari, Büşra Eser Çavdartepe, Irene J Chang, Erika Beckman, Renate Peters, Andrew Paul Fennell, Bernice Lo, Luisa Averdunk, Felix Distelmaier, Martina Baethmann, Frances Elmslie, Kairit Joost, Sheela Nampoothiri, Dhanya Yesodharan, Hannah Mandel, Amy Kimball, Antonie D. Kline, Cyril Mignot, Boris Keren, Vincent Laugel, Katrin Õunap, Kalpana Devadathan, Frederique M.C. van Berkestijn, Arpana Silwal, Saskia Koene, Sumit Verma, Mohammed Yousuf Karim, Chahynez Boubidi, Majid Aziz, Gehad ElGhazali, Lauren Mattas, Mohammad Miryounesi, Farzad Hashemi-Gorji, Shahryar Alavi, Nayereh Nouri, Mehrdad Noruzinia, Saeedeh Kavousi, Arveen Kamath, Sandeep Jayawant, Russell Saneto, Nourelhoda A. Haridy, Pinar Ozkan Kart, Ali Cansu, Claire Beneteau, Kyra E. Stuurman, Martina Wilke, Tahsin Stefan Barakat, Homa Tajsharghi, Annarita Scardamaglia, Sadeq Vallian, Semra Hız, Ali Shoeibi, Reza Boostani, Narges Hashemi, Meisam Babaei, Norah Saleh Alsaleh, Julie Lander, Tania Attié-Bitach, Pauline Marzin, Dorota Wicher, Jessica I Gold, Mariana H G Monje, Dimitri Krainc, Niccolò Mencacci, Somayeh Bakhtiari, Michael Kruer, Emanuela Argilli, Elliott Sherr, Yalda Jamshidi, Ehsan Ghayoor Karimiani, Yiu Wing Sunny Cheung, Ivan Karin, Wendy K Chung, James R. Lupski, Manju A. Kurian, Jörg Dötsch, Jürgen-Christoph von Kleist-Retzow, Thomas Klopstock, Matias Wagner, Calvin Yip, Andreas Roos, Carlo Dionisi-Vici, Mathias Gautel, Michael R Duchen, Adam Antebi, Henry Houlden, Manolis Fanto, and Heinz Jungbluth. Mutations in epg5 are associated with a wide spectrum of neurodevelopmental and neurodegenerative disorders. MedRxiv, Jun 2024. URL: https://doi.org/10.1101/2024.06.12.24308722, doi:10.1101/2024.06.12.24308722. This article has 3 citations.

8. (wang2019therbg1–rbg2complex pages 1-2): Zhaoyu Wang, Hongyu Zhao, Chongzhen Yuan, Dongfeng Zhao, Yanan Sun, Xiaochen Wang, and Hong Zhang. The rbg-1–rbg-2 complex modulates autophagy activity by regulating lysosomal biogenesis and function in c. elegans. Journal of Cell Science, Oct 2019. URL: https://doi.org/10.1242/jcs.234195, doi:10.1242/jcs.234195. This article has 13 citations and is from a domain leading peer-reviewed journal.

Citations

1. wang2016thevicisyndrome pages 6-9
2. wang2016thevicisyndrome pages 3-5
3. wang2016thevicisyndrome pages 1-3
4. https://doi.org/10.1016/j.molcel.2016.08.021
5. https://doi.org/10.1016/j.molcel.2016.08.021;
6. https://doi.org/10.1242/jcs.234195
7. https://doi.org/10.1080/15548627.2025.2485420
8. https://doi.org/10.1101/2024.06.12.24308722
9. https://doi.org/10.1016/j.molcel.2016.08.021,
10. https://doi.org/10.1242/jcs.234195,
11. https://doi.org/10.1080/15548627.2025.2485420,
12. https://doi.org/10.1101/2024.06.12.24308722,