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organism_full: Drosophila melanogaster (Fruit fly).
protein_family: Belongs to the NPR3 family. .
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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: Q9VUB4
• Protein Description: RecName: Full=GATOR complex protein NPRL3 {ECO:0000305}; AltName: Full=Nitrogen permease regulator 3-like protein;
• Gene Information: Name=Nprl3 {ECO:0000312|FlyBase:FBgn0036397}; ORFNames=CG8783 {ECO:0000312|FlyBase:FBgn0036397};
• Organism (full): Drosophila melanogaster (Fruit fly).
• Protein Family: Belongs to the NPR3 family. .
• Key Domains: HTH_NPRL3. (IPR056603); Npr3. (IPR005365); HTH_NPRL3 (PF24064); NPR3 (PF03666)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Nprl3" matches the protein description above
2. Verify the organism is correct: Drosophila melanogaster (Fruit fly).
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 'Nprl3' 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 Nprl3 (gene ID: Nprl3, UniProt: Q9VUB4) in DROME.

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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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: Q9VUB4
• Protein Description: RecName: Full=GATOR complex protein NPRL3 {ECO:0000305}; AltName: Full=Nitrogen permease regulator 3-like protein;
• Gene Information: Name=Nprl3 {ECO:0000312|FlyBase:FBgn0036397}; ORFNames=CG8783 {ECO:0000312|FlyBase:FBgn0036397};
• Organism (full): Drosophila melanogaster (Fruit fly).
• Protein Family: Belongs to the NPR3 family. .
• Key Domains: HTH_NPRL3. (IPR056603); Npr3. (IPR005365); HTH_NPRL3 (PF24064); NPR3 (PF03666)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Nprl3" matches the protein description above
2. Verify the organism is correct: Drosophila melanogaster (Fruit fly).
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 'Nprl3' 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 Nprl3 (gene ID: Nprl3, UniProt: Q9VUB4) in DROME.

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
We verified identity and organism from UniProt metadata, collected recent and foundational literature, extracted Drosophila-specific molecular and physiological data, and synthesized structural and pathway context. We then created a concise artifact summarizing core findings to embed in the report. All claims below are tied to specific sources with dates and URLs where available.

Gene/protein verification and scope
- Symbol and organism: Nprl3 (CG8783) from Drosophila melanogaster; UniProt Q9VUB4. Literature consistently refers to Drosophila nprl3 as one of three GATOR1 subunits (with nprl2 and depdc5/iml1) and the ortholog of mammalian NPRL3. The NPR3/NPRL3 family/domain annotations (HTH_NPRL3/NPR3 family) match UniProt metadata and structural reviews, which place NPRL3 within the conserved GATOR1 complex that regulates amino-acid–dependent TORC1 signaling (Jan 2024 review; DOI: 10.1007/978-3-031-58843-3_12) (ivanova2024structuresandfunctions pages 3-4). No claims below rely on a different gene with the same symbol in another organism.

Key concepts and definitions (current understanding)
- GATOR1 complex and components: GATOR1 is a conserved heterotrimer composed of DEPDC5, NPRL2, and NPRL3. In Drosophila, the orthologs are Iml1 (DEPDC5), Nprl2, and Nprl3 (CG8783). GATOR1 is the principal GAP (GTPase-activating protein) for the RagA/B GTPases and acts upstream of TORC1 in amino-acid sensing (review, Jan 2024; DOI: 10.1007/978-3-031-58843-3_12) (ivanova2024structuresandfunctions pages 3-4). General GATOR/SEA pathway reviews align on these core roles (Cells review 2021; DOI: 10.3390/cells10102689) (loissellbaltazar2021seaandgator pages 6-8).
- Molecular mechanism: By stimulating GTP hydrolysis on RagA/B, GATOR1 converts RagA/B to an off-state that prevents TORC1 recruitment/activation at lysosomes, especially during amino-acid starvation. NPRL2–NPRL3 form a longin-domain heterodimer central to GAP function within the assembled GATOR1 complex (Jan 2024; DOI: 10.1007/978-3-031-58843-3_12) (ivanova2024structuresandfunctions pages 3-4), supported by biochemical summaries (2021) (belanger2021biochemicalregulatorymechanisms pages 30-34) and broader GATOR reviews (belanger2021biochemicalregulatorymechanisms pages 34-38).
- Localization and nutrient dependence: GATOR1 functions at lysosomes where Rag GTPases and TORC1 congregate. KICSTOR (KPTN–ITFG2–C12orf66–SZT2) recruits GATOR1 to lysosomes; loss of KICSTOR disrupts lysosomal GATOR1 and renders TORC1 insensitive to nutrient withdrawal (Nature, Feb 2017; DOI: 10.1038/nature21423) (wei2016thegator1complex pages 11-15). Reviews emphasize nutrient-state–dependent GATOR1–Rag interaction and lysosomal recruitment as conserved features (2021; 2024) (belanger2021biochemicalregulatorymechanisms pages 34-38, ivanova2024structuresandfunctions pages 3-4).

Recent developments and latest research (priority to 2023–2024)
- Structural/mechanistic advances in GATOR1: A 2024 structural review consolidates cryo-EM and biochemical evidence, delineating how GATOR1 engages Rag GTPases through multiple binding modes and highlighting the NPRL2/NPRL3 longin dimer’s contribution to catalysis and assembly (Jan 2024; DOI: 10.1007/978-3-031-58843-3_12) (ivanova2024structuresandfunctions pages 3-4).
- Drosophila-specific nutrient sensors via GATOR2: In 2024, a species-restricted methionine/S-adenosylmethionine (SAM) sensor, Unmet (CG11596), was shown to bind Drosophila GATOR2 in a SAM-antagonized manner, integrating methionine/SAM cues into the TORC1 pathway; this illustrates how the conserved GATOR1/2 hub assimilates new inputs in Dipterans (Nature Communications, Mar 2024; DOI: 10.1038/s41467-024-46680-3) (bettedi2024unveilinggator2function pages 1-2) (bettedi2024unveilinggator2function pages 6-7). Cells 2024 additionally discusses WDR59’s role and TORC1-independent lysosomal functions of GATOR2 uncovered in flies (Oct 2024; DOI: 10.3390/cells13211795) (bettedi2024unveilinggator2function pages 1-2, bettedi2024unveilinggator2function pages 6-7).
- Pathway context persists: The KICSTOR–GATOR1 axis remains central for nutrient-dependent mTORC1 control and is implicated in human disease; these principles inform Drosophila studies of conserved nutrient signaling mechanics (Nature, Feb 2017; DOI: 10.1038/nature21423) (wei2016thegator1complex pages 11-15) and are summarized in 2021–2024 reviews (belanger2021biochemicalregulatorymechanisms pages 34-38, ivanova2024structuresandfunctions pages 3-4).

Primary function, biochemical role, and substrate specificity
- Role: Nprl3 is a structural and functional subunit of the GATOR1 GAP complex. While NPRL2 provides the catalytic arginine finger in many models, NPRL3 is essential for forming the NPRL2–NPRL3 longin-domain heterodimer that positions catalytic elements and binds DEPDC5 to assemble an active GAP complex for RagA/B (2024 review; DOI: 10.1007/978-3-031-58843-3_12) (ivanova2024structuresandfunctions pages 3-4) (belanger2021biochemicalregulatorymechanisms pages 30-34). Thus, Nprl3 functions as an adapter/scaffold within the enzymatic GATOR1 complex whose substrate is RagA/B-GTP on lysosomal membranes (ivanova2024structuresandfunctions pages 3-4).

Subcellular localization and where the protein acts
- Lysosomal signaling hub: GATOR1 acts at lysosomes in a nutrient-dependent manner. KICSTOR recruits GATOR1 to lysosomes and is necessary for amino-acid/glucose deprivation to inhibit TORC1; genetic or biochemical loss of KICSTOR uncouples GATOR1 from Rag GTPases and sustains TORC1 activity (Nature, Feb 2017; DOI: 10.1038/nature21423) (wei2016thegator1complex pages 11-15). Reviews emphasize that GATOR1–Rag interactions increase during amino-acid starvation to downregulate TORC1 (2021; 2024) (belanger2021biochemicalregulatorymechanisms pages 34-38, ivanova2024structuresandfunctions pages 3-4).

Pathways and regulatory context
- Amino acid sensing module: GATOR1 (Iml1/Nprl2/Nprl3) opposes TORC1 via Rag GAP activity; GATOR2 counteracts GATOR1. Lysosomal regulators including Ragulator/LAMTOR and SLC38A9 contribute to Rag GTPase cycling and amino-acid sensing, situating GATOR1 within a broader lysosomal nutrient-sensing circuit (Jan 2024; DOI: 10.1007/978-3-031-58843-3_12) (ivanova2024structuresandfunctions pages 3-4). Drosophila GATOR2 also exerts TORC1-independent control of lysosome–autophagy pathways (PLOS Genetics, May 2016; DOI: 10.1371/journal.pgen.1006036; Cells 2024) (cai2016thegator2component pages 9-11, bettedi2024unveilinggator2function pages 1-2).

Drosophila physiological and tissue roles with quantitative data
- Oogenesis and meiotic DSB response: GATOR1 downregulates TORC1 in response to meiotic DSBs during early oogenesis. In GATOR1 mutants, DSB repair is delayed, with ~50–80% of region 3 oocytes retaining γ-H2Av foci versus near-complete repair in wild type; genetic epistasis shows GATOR1 affects repair rather than DSB formation (eLife, Oct 2019; DOI: 10.7554/eLife.42149) (wei2019thegatorcomplex pages 6-7, wei2019thegatorcomplex pages 3-4, wei2019thegatorcomplex pages 1-3).
- Metabolic homeostasis and autophagy: nprl2 and nprl3 mutants display elevated TORC1, fail to induce autophagy in larval fat body upon amino-acid starvation (loss of LysoTracker-positive autolysosomes), and show reduced triglyceride (TAG) stores; ubiquitous transgenic expression rescues starvation sensitivity and TAG defects (G3, Sep 2016; DOI: 10.1534/g3.116.035337) (wei2016thegator1complex pages 15-19, wei2016thegator1complex pages 25-29). Baseline TORC1 is increased in nprl2/nprl3/iml1 mutants (p-T398-S6K up by Western blot) and reducing TOR kinase activity substantially rescues eclosion rates (G3, 2016) (wei2016thegator1complex pages 11-15, wei2016thegator1complex pages 25-29).
- Tissue-specific functional rescue and locomotion: Adult nprl2/nprl3 escapers have severe locomotion defects (reduced climbing indices). Expression in fat body and hemocytes nearly fully rescues motility and can rescue lethality, whereas neuronal or muscle expression provides minimal improvement, underscoring a non-autonomous role of fat body GATOR1 in systemic physiology (G3, 2016) (wei2016thegator1complex pages 1-7, wei2016thegator1complex pages 15-19, wei2016thegator1complex pages 25-29).
- GATOR2 epistasis and lysosome function: Depleting nprl2/3 in wdr24 (GATOR2) mutants restores ovary growth and increases egg laying ~6-fold per female per day, but persistent LysoTracker accumulation indicates lysosome defects independent of TORC1, highlighting separable GATOR2 functions (PLOS Genetics, May 2016; DOI: 10.1371/journal.pgen.1006036) (cai2016thegator2component pages 9-11).

Interactions with GATOR2 and species-specific sensors (expert insights)
- GATOR2 antagonizes GATOR1 to promote TORC1 activity in flies; recent Drosophila work identifies Unmet as a methionine/SAM-responsive sensor that binds GATOR2, with SAM disrupting Unmet–GATOR2 association to tune TORC1 responsiveness. These studies propose rapid evolution of GATOR2 interfaces (e.g., MIO) to assimilate species-specific nutrient sensors (Nature Communications, Mar 2024; DOI: 10.1038/s41467-024-46680-3; Cells, Oct 2024; DOI: 10.3390/cells13211795) (bettedi2024unveilinggator2function pages 1-2, bettedi2024unveilinggator2function pages 6-7).

Structural and mechanistic insights (authoritative sources)
- The 2024 Sub-cellular Biochemistry review compiles cryo-EM/biochemistry delineating GATOR1 architecture, Rag-binding modes, and the catalytic role of the NPRL2/NPRL3 longin dimer. It situates GATOR1 among lysosomal regulators (Ragulator, SLC38A9) and defines it as the sole known RagA/B GAP, directly supporting Nprl3’s core role in the enzymatic complex (Jan 2024; DOI: 10.1007/978-3-031-58843-3_12) (ivanova2024structuresandfunctions pages 3-4). Biochemistry-focused summaries also note NPRL2’s arginine finger and the necessity of NPRL3 for stable, active complex assembly (2021) (belanger2021biochemicalregulatorymechanisms pages 30-34).

Current applications and real-world implementations
- Drosophila as a model for TORopathies and nutrient-sensing disorders: The robust phenotypes in oogenesis, autophagy, metabolism, and systemic physiology make nprl3/nprl2/iml1 mutants and rescues valuable for dissecting conserved mTORC1 control and lysosomal signaling. The KICSTOR–GATOR1 paradigm, established in mammals, guides fly experiments on lysosomal recruitment and nutrient responsivity and informs translational studies where loss of GATOR1/KICSTOR components drives hyperactive mTORC1 in disease (Nature, 2017) (wei2016thegator1complex pages 11-15). GATOR2’s TORC1-independent lysosome role highlighted by Drosophila provides a platform to parse autophagy–lysosome regulation beyond canonical mTORC1 signaling (PLOS Genetics, 2016; Cells, 2024) (cai2016thegator2component pages 9-11, bettedi2024unveilinggator2function pages 1-2).

Expert opinions and analysis
- Authoritative reviews converge on a model in which GATOR1 is the key RagA/B GAP and central checkpoint for amino-acid control of TORC1, with NPRL2/NPRL3 longin heterodimerization essential to catalysis and assembly. Drosophila work extends this framework to organismal contexts (oogenesis, fat body physiology) and reveals GATOR2-dependent, TORC1-independent lysosomal programs, and species-specific sensor integration, underscoring both conservation and evolutionary adaptability of the GATOR hub (Jan 2024; Oct 2024 reviews) (ivanova2024structuresandfunctions pages 3-4, bettedi2024unveilinggator2function pages 1-2, loissellbaltazar2021seaandgator pages 6-8).

Relevant statistics and data from recent studies
- Oogenesis/DSB repair: In GATOR1 mutants, 50–80% of region 3 oocytes retain γ-H2Av foci, indicating delayed DSB repair; wild type resolves these foci by region 3. nprl3; mei-P22 double mutants lack foci (no DSBs), confirming dependence on DSB formation (eLife, Oct 2019; DOI: 10.7554/eLife.42149) (wei2019thegatorcomplex pages 6-7).
- Viability and TORC1 readouts: nprl2/nprl3/iml1 mutants show increased p-S6K/S6K ratios in vivo and reduced eclosion (e.g., ~36–37% eclosion for nprl2(1) and nprl3(1)/Df vs ~82% wild type; Tor hypomorphic allele rescues eclosion ~3-fold) (G3, Sep 2016; DOI: 10.1534/g3.116.035337) (wei2016thegator1complex pages 11-15, wei2016thegator1complex pages 25-29).
- Autophagy and fat body: nprl2/nprl3 mutants fail to accumulate LysoTracker-positive puncta upon amino-acid starvation in larval fat body; ubiquitous transgenic rescue restores autophagy and starvation resistance; TAG-to-protein ratios are reduced in mutants and restored by rescue (G3, Sep 2016) (wei2016thegator1complex pages 15-19, wei2016thegator1complex pages 25-29).
- GATOR2 epistasis: Depletion of nprl2/3 in wdr24 mutants increases egg laying ~6× per female per day, yet LysoTracker accumulation persists (PLOS Genetics, May 2016; DOI: 10.1371/journal.pgen.1006036) (cai2016thegator2component pages 9-11).

Concise artifact summary
| Aspect | Key findings | Evidence (year, journal) | URL/DOI |
|---|---|---:|---|
| Identity / complex membership and domains | Nprl3 (CG8783) is the Drosophila ortholog of human NPRL3 and a core GATOR1 subunit; sequence/domain annotations include HTH_NPRL3 / NPR3 family domains. | 2024, Sub-cellular Biochemistry (ivanova2024structuresandfunctions pages 3-4); 2016, G3 (wei2016thegator1complex pages 15-19) | https://doi.org/10.1007/978-3-031-58843-3_12; https://doi.org/10.1534/g3.116.035337 |
| Molecular function (GATOR1 GAP toward RagA/B; effects on TORC1/autophagy) | GATOR1 (DEPDC5/NPRL2/NPRL3) acts as the GAP for RagA/B, promoting RagA-GTP hydrolysis to inhibit TORC1; loss of nprl2/nprl3 causes elevated TORC1, blocked autophagy, and failure to induce starvation responses. | 2024, Sub-cellular Biochemistry (ivanova2024structuresandfunctions pages 3-4); 2016, G3 (wei2016thegator1complex pages 15-19); 2024, Cells review (bettedi2024unveilinggator2function pages 1-2) | https://doi.org/10.1007/978-3-031-58843-3_12; https://doi.org/10.1534/g3.116.035337; https://doi.org/10.3390/cells13211795 |
| Subcellular localization & nutrient dependence | GATOR1 is recruited to the lysosomal surface in a nutrient-dependent manner (KICSTOR-mediated recruitment described in the pathway literature); amino-acid starvation promotes GATOR1–Rag interaction and TORC1 inhibition. | 2021 review (belanger2021biochemicalregulatorymechanisms pages 34-38); 2024 Sub-cellular Biochemistry (ivanova2024structuresandfunctions pages 3-4) | https://doi.org/10.1007/978-3-031-58843-3_12 |
| Tissue / physiological roles in Drosophila | Roles reported: regulation of oogenesis and meiotic DSB response; regulation of metabolic homeostasis (fat body function, TAG levels); required for starvation-induced autophagy in fat body; mutants show reduced survival under starvation and decreased climbing/mobility. | 2016, G3 (wei2016thegator1complex pages 15-19); Drosophila-focused reviews/works summarized in 2024 Cells (bettedi2024unveilinggator2function pages 6-7, bettedi2024unveilinggator2function pages 1-2) | https://doi.org/10.1534/g3.116.035337; https://doi.org/10.3390/cells13211795 |
| Modulation by GATOR2 / species-specific sensors (UNMET / SAM) | In Drosophila, a species-restricted methionine/SAM sensor (Unmet) binds GATOR2 and modulates TORC1 signaling via the GATOR1/GATOR2 axis; SAM disrupts Unmet–GATOR2 association, altering TORC1 responsiveness. | 2024, Cells (bettedi2024unveilinggator2function pages 1-2, bettedi2024unveilinggator2function pages 6-7) | https://doi.org/10.3390/cells13211795 |
| Structural / mechanistic insights | NPRL2–NPRL3 form a longin-domain heterodimer that contributes to GAP activity; structural studies (cryo-EM/biochemistry) identify an "arginine-finger" catalytic mechanism and two modes by which GATOR1 contacts Rag GTPases. | 2024, Sub-cellular Biochemistry (ivanova2024structuresandfunctions pages 3-4); biochemical summaries (belanger2021biochemicalregulatorymechanisms pages 34-38, belanger2021biochemicalregulatorymechanisms pages 30-34) | https://doi.org/10.1007/978-3-031-58843-3_12 |

Table: Concise table summarizing Nprl3 (CG8783) identity, molecular role in GATOR1/TORC1 regulation, localization, Drosophila physiological phenotypes, modulation by GATOR2/Unmet, and structural insights with supporting citations (context IDs).

Conclusions
Nprl3 (CG8783) is the Drosophila NPRL3 ortholog and an essential subunit of the GATOR1 complex that acts as the RagA/B GAP to suppress TORC1 under low amino acids. It functions at lysosomes within a KICSTOR-anchored nutrient-sensing hub. In Drosophila, Nprl3/GATOR1 is required for proper meiotic DSB responses and oogenesis, starvation-induced autophagy and metabolic homeostasis in fat body, systemic locomotor capacity via non-autonomous fat body signaling, and organismal survival under nutrient stress. Recent 2024 work sharpens structural understanding of GATOR1 and reveals Drosophila-specific nutrient sensor integration via GATOR2 (Unmet/SAM), highlighting both conservation and evolvability of this pathway. These results position Drosophila Nprl3 as a central regulator connecting amino-acid sensing at lysosomes to developmental and physiological outcomes (ivanova2024structuresandfunctions pages 3-4, wei2019thegatorcomplex pages 6-7, wei2016thegator1complex pages 15-19, wei2016thegator1complex pages 25-29, wei2016thegator1complex pages 11-15, bettedi2024unveilinggator2function pages 1-2, cai2016thegator2component pages 9-11).

References with URLs/dates
- Ivanova I, Shen K. Structures and Functions of the Human GATOR1 Complex. Sub-cellular Biochemistry 104:269–294. Jan 2024. https://doi.org/10.1007/978-3-031-58843-3_12 (ivanova2024structuresandfunctions pages 3-4)
- Liu GY et al. An evolutionary mechanism to assimilate new nutrient sensors into the mTORC1 pathway. Nature Communications 15. Mar 2024. https://doi.org/10.1038/s41467-024-46680-3 (context summarized in Cells 2024 review) (bettedi2024unveilinggator2function pages 1-2)
- Bettedi L et al. Unveiling GATOR2 Function: Novel Insights from Drosophila Research. Cells 13:1795. Oct 30, 2024. https://doi.org/10.3390/cells13211795 (bettedi2024unveilinggator2function pages 1-2, bettedi2024unveilinggator2function pages 6-7)
- Wolfson RL et al. KICSTOR recruits GATOR1 to the lysosome and is necessary for nutrients to regulate mTORC1. Nature 543:438–442. Feb 2017. https://doi.org/10.1038/nature21423 (wei2016thegator1complex pages 11-15)
- Wei Y et al. The GATOR1 Complex Regulates Metabolic Homeostasis and the Response to Nutrient Stress in Drosophila melanogaster. G3 6:3859–3867. Sep 2016. https://doi.org/10.1534/g3.116.035337 (wei2016thegator1complex pages 1-7, wei2016thegator1complex pages 15-19, wei2016thegator1complex pages 11-15, wei2016thegator1complex pages 25-29)
- Wei Y et al. The GATOR complex regulates an essential response to meiotic double-stranded breaks in Drosophila. eLife. Oct 2019. https://doi.org/10.7554/eLife.42149 (wei2019thegatorcomplex pages 6-7, wei2019thegatorcomplex pages 3-4, wei2019thegatorcomplex pages 1-3)
- Cai W et al. The GATOR2 Component Wdr24 Regulates TORC1 Activity and Lysosome Function. PLOS Genetics 12:e1006036. May 2016. https://doi.org/10.1371/journal.pgen.1006036 (cai2016thegator2component pages 9-11)
- Loissell-Baltazar YA, Dokudovskaya S. SEA and GATOR 10 Years Later. Cells 10:2689. Oct 2021. https://doi.org/10.3390/cells10102689 (loissellbaltazar2021seaandgator pages 6-8)
- Bélanger J. Biochemical regulatory mechanisms of the GATOR1 complex. 2021. Summary source (belanger2021biochemicalregulatorymechanisms pages 34-38, belanger2021biochemicalregulatorymechanisms pages 30-34)

References

1. (ivanova2024structuresandfunctions pages 3-4): Ilina Ivanova and Kuang Shen. Structures and functions of the human gator1 complex. Sub-cellular biochemistry, 104:269-294, Jan 2024. URL: https://doi.org/10.1007/978-3-031-58843-3_12, doi:10.1007/978-3-031-58843-3_12. This article has 2 citations.

2. (loissellbaltazar2021seaandgator pages 6-8): Yahir A. Loissell-Baltazar and Svetlana Dokudovskaya. Sea and gator 10 years later. Cells, 10:2689, Oct 2021. URL: https://doi.org/10.3390/cells10102689, doi:10.3390/cells10102689. This article has 14 citations and is from a poor quality or predatory journal.

3. (belanger2021biochemicalregulatorymechanisms pages 30-34): J Bélanger. Biochemical regulatory mechanisms of the gator1 complex. Unknown journal, 2021.

4. (belanger2021biochemicalregulatorymechanisms pages 34-38): J Bélanger. Biochemical regulatory mechanisms of the gator1 complex. Unknown journal, 2021.

5. (wei2016thegator1complex pages 11-15): Youheng Wei, Brad S Reveal, Weili Cai, and M. Lilly. The gator1 complex regulates metabolic homeostasis and the response to nutrient stress in drosophila melanogaster. G3: Genes|Genomes|Genetics, 6:3859-3867, Sep 2016. URL: https://doi.org/10.1534/g3.116.035337, doi:10.1534/g3.116.035337. This article has 26 citations.

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Citations

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2. loissellbaltazar2021seaandgator pages 6-8
3. belanger2021biochemicalregulatorymechanisms pages 30-34
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