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gene_id: Nprl2
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gene_info: Name=Nprl2 {ECO:0000312|FlyBase:FBgn0030800}; ORFNames=CG9104 {ECO:0000312|FlyBase:FBgn0030800};
organism_full: Drosophila melanogaster (Fruit fly).
protein_family: Belongs to the NPR2 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: Q9VXA0
• Protein Description: RecName: Full=GATOR complex protein NPRL2 {ECO:0000305}; AltName: Full=Nitrogen permease regulator 2-like protein {ECO:0000312|FlyBase:FBgn0030800};
• Gene Information: Name=Nprl2 {ECO:0000312|FlyBase:FBgn0030800}; ORFNames=CG9104 {ECO:0000312|FlyBase:FBgn0030800};
• Organism (full): Drosophila melanogaster (Fruit fly).
• Protein Family: Belongs to the NPR2 family. .
• Key Domains: NPR2-like. (IPR009348); NPR2 (PF06218)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Nprl2" 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 'Nprl2' 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 Nprl2 (gene ID: Nprl2, UniProt: Q9VXA0) 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: Q9VXA0
• Protein Description: RecName: Full=GATOR complex protein NPRL2 {ECO:0000305}; AltName: Full=Nitrogen permease regulator 2-like protein {ECO:0000312|FlyBase:FBgn0030800};
• Gene Information: Name=Nprl2 {ECO:0000312|FlyBase:FBgn0030800}; ORFNames=CG9104 {ECO:0000312|FlyBase:FBgn0030800};
• Organism (full): Drosophila melanogaster (Fruit fly).
• Protein Family: Belongs to the NPR2 family. .
• Key Domains: NPR2-like. (IPR009348); NPR2 (PF06218)

MANDATORY VERIFICATION STEPS:

1. Check if the gene symbol "Nprl2" 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 'Nprl2' 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 Nprl2 (gene ID: Nprl2, UniProt: Q9VXA0) 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 overview
- Verified identity: Nprl2 (CG9104; FBgn0030800) in Drosophila melanogaster encodes a conserved GATOR1 subunit (UniProt Q9VXA0), belonging to the NPR2/NPRL2-like family. No symbol ambiguity was detected within D. melanogaster. (context verification)
- Evidence focus: primary Drosophila experiments on GATOR1/Nprl2 in oogenesis and DNA damage response; conserved mechanistic reviews of Rag–mTORC1 signaling; 2023 advances linking NPRL2 post‑translational regulation to methionine/SAM sensing; mammalian NPRL2 studies for localization and mTORC1‑independent roles.

Gene/protein identity verification
- Target matches UniProt Q9VXA0: Drosophila melanogaster Nprl2 (CG9104) annotated as GATOR complex protein NPRL2/Nitrogen permease regulator 2‑like; family/domain annotations concordant with NPR2/NPRL2‑like. No conflicting gene symbol usage in fly was found. (context verification)

1) Key concepts and definitions (current understanding)
- Complex membership and pathway role: Nprl2 is one of three core subunits of GATOR1 (with Iml1/DEPDC5 and Nprl3). GATOR1 is the Rag GTPase-activating protein (GAP) complex that inhibits TORC1/mTORC1 in response to amino‑acid limitation; within GATOR1, NPRL2 contains a catalytic arginine (“arginine finger”) that stimulates RagA/B GTP hydrolysis to turn off mTORC1 signaling. In metazoans, GATOR1 opposes GATOR2, which relays amino‑acid sensors to relieve GATOR1 and promote TORC1 activation when nutrients are sufficient. (lamasherpa2023 review, doi:10.1042/bst20210038, Mar 2023; URL: https://doi.org/10.1042/bst20210038) (lamasherpa2023regulationofmtorc1 pages 2-4, lamasherpa2023regulationofmtorc1 pages 8-9)
- Drosophila functional context: In fly oogenesis, GATOR1 (Iml1/Nprl2/Nprl3) downregulates TORC1 when meiotic double-strand breaks (DSBs) arise; restraining TORC1 via GATOR1 and TSC promotes timely DSB repair and prevents excessive p53 activation. GATOR2 (Mio) antagonizes this inhibition to enable growth later in oogenesis. (Wei et al., eLife, Oct 2019; doi:10.7554/eLife.42149; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 1-3, wei2019thegatorcomplex pages 3-4)

2) Recent developments and latest research (prioritize 2023–2024)
- Post‑translational regulation of NPRL2 links methionine/SAM to GATOR1: PRMT1 cooperates with the SAM sensor SAMTOR to control mTORC1 methionine sensing by arginine methylation of NPRL2. PRMT1 selectively methylates NPRL2 (not DEPDC5/NPRL3), with asymmetric dimethylation at R6 and R78; R78 is a major functional site. SAMTOR and PRMT1 bind GATOR1 in a mutually exclusive, SAM‑responsive manner. Methionine increases lysosomal PRMT1 and mTOR localization and elevates lysosomal ADMA signals; PRMT1 activity is required for methionine/SAM‑induced mTORC1 activation and lysosomal mTORC1 colocalization. Mechanistically, methylation of NPRL2 suppresses GATOR1 GAP activity, facilitating mTORC1 activation. (Jiang et al., Cell Metabolism, Dec 2023; doi:10.1016/j.cmet.2023.11.001; URL: https://doi.org/10.1016/j.cmet.2023.11.001) (jiang2023prmt1orchestrateswith pages 1-3, jiang2023prmt1orchestrateswith pages 5-6, jiang2023prmt1orchestrateswith pages 6-8, jiang2023prmt1orchestrateswith pages 26-30)
- Consolidated 2023 perspective on Rag–lysosome control of mTORC1: Reviews reaffirm GATOR1 as RagA/B GAP, Ragulator as Rag GEF/lysosomal scaffold, and the lysosome as the mTORC1 control hub integrating amino‑acid sensors (CASTORs, Sestrins, SAMTOR) and transporters (e.g., SLC38A9). These updates refine isoform/tissue‑specific nuances and stress‑dependent lysosomal targeting of TSC2. (Biochemical Society Transactions review, Mar 2023; doi:10.1042/bst20210038; URL: https://doi.org/10.1042/bst20210038) (lamasherpa2023regulationofmtorc1 pages 2-4, lamasherpa2023regulationofmtorc1 pages 8-9)

3) Molecular function, localization, and pathway placement
- Molecular function: Nprl2 is a GATOR1 catalytic subunit contributing the arginine finger essential for GAP activity toward RagA/B, thereby inhibiting TORC1 during amino‑acid starvation or damage responses. In Drosophila, loss of any GATOR1 subunit elevates TORC1 activity and blunts starvation‑induced autophagy. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 1-3, wei2019thegatorcomplex pages 7-9)
- Subcellular localization relevant to function: The GATOR1–Rag–Ragulator axis operates at lysosomes; Ragulator tethers Rags to lysosomes and enables mTORC1 recruitment for activation in nutrient‑replete states, whereas GATOR1’s GAP activity on Rags disengages mTORC1 when nutrients are limiting. KICSTOR recruits GATOR1 to lysosomes under stress, coordinating with Ragulator/Rags. (Lama‑Sherpa et al., 2023; URL: https://doi.org/10.1042/bst20210038) (lamasherpa2023regulationofmtorc1 pages 2-4, lamasherpa2023regulationofmtorc1 pages 8-9); (Jiang et al., 2023; URL: https://doi.org/10.1016/j.cmet.2023.11.001) (jiang2023prmt1orchestrateswith pages 19-20)
- Potential nuclear roles and mTORC1‑independent activities (conserved insights): In human cells, NPRL2 can accumulate in the nucleus upon proteasome inhibition and its overexpression induces NOX2‑dependent ROS, DNA damage signaling, and cell‑cycle arrest, indicating functions beyond canonical mTORC1 regulation. These data suggest possible conserved non‑lysosomal roles that merit evaluation in Drosophila. (Ma et al., Sci Rep, Nov 2017; doi:10.1038/s41598-017-15497-0; URL: https://doi.org/10.1038/s41598-017-15497-0) (ma2017tumorsuppressornprl2 pages 2-4, ma2017tumorsuppressornprl2 pages 13-13)
- Placement relative to GATOR2/Mio: In the fly germline, GATOR2 (via Mio) antagonizes GATOR1/TSC to prevent prolonged TORC1 suppression after DSB‑triggered checkpoint activation, thereby permitting oocyte growth. Loss of Mio causes constitutive TORC1 downregulation and growth defects that are suppressed by reducing GATOR1 activity or preventing meiotic DSBs. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 3-4, wei2019thegatorcomplex pages 1-3)

4) Drosophila experimental phenotypes and precise roles
- Meiotic DSB response and p53 activation: GATOR1 mutants (including nprl2 and nprl3 nulls) show elevated TORC1 and delayed repair of meiotic DSBs. In GATOR1 mutants, TORC1 activity in ovaries is ~3× wild type, DSBs persist into later stages, and p53 is hyperactivated. Quantitatively, whereas <5% of region 3 cysts exhibit p53‑GFPnls signal in wild type, nearly 80% do so in GATOR1 mutants, indicating checkpoint stress. Genetic reduction of S6K dosage suppresses excess DSBs in iml1-depleted germlines, implicating TORC1→S6K in the repair delay. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 15-17, wei2019thegatorcomplex pages 7-9)
- Autophagy and starvation response: GATOR1 mutants fail to induce autophagy appropriately upon starvation, consistent with GATOR1’s role as a TORC1 inhibitor in amino‑acid limitation. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 7-9)
- Retrotransposon control: In nprl3 mutants, retrotransposon transcripts are elevated by qRT‑PCR; increases are largely suppressed when meiotic DSB formation is blocked (mei‑P22) and are additive with loss of p53, indicating that GATOR1 and p53 act in parallel to restrain transposons during DSB episodes. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 13-15)
- DNA damage sensitivity: GATOR1 mutants show reduced survival after low‑dose γ‑irradiation, consistent with compromised DNA damage responses when TORC1 is hyperactive. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 15-17)

5) Current applications and real‑world implementations
- Nutrient‑sensing therapeutics and metabolic modulation: The PRMT1–SAMTOR–GATOR1 axis offers a druggable interface connecting methionine/SAM levels to mTORC1 via NPRL2 methylation. PRMT1 inhibition or SAM lowering blunts methionine‑induced mTORC1 activation and lysosomal recruitment, suggesting strategies to modulate mTORC1 through NPRL2 PTMs. While demonstrated in mammalian systems, the conservation of GATOR1 architecture argues for translational relevance and testable hypotheses in Drosophila. (Jiang et al., 2023; URL: https://doi.org/10.1016/j.cmet.2023.11.001) (jiang2023prmt1orchestrateswith pages 26-30, jiang2023prmt1orchestrateswith pages 5-6)
- Disease relevance of GATOR1 components: Human literature continues to link DEPDC5/NPRL2/NPRL3 variants to neurological phenotypes, including epilepsy, emphasizing GATOR1’s clinical significance as a lysosomal mTORC1 checkpoint. (Review overview, Int J Mol Sci, Feb 2023; doi:10.3390/ijms24044223; URL: https://doi.org/10.3390/ijms24044223) (jiang2023prmt1orchestrateswith pages 20-21)

6) Expert opinions and authoritative perspectives
- Consensus models: Recent reviews and perspectives converge on a lysosome‑centric model where Ragulator (lysosomal scaffold/GEF) and GATOR1 (Rag GAP) integrate amino‑acid sensors to govern mTORC1 translocation and activation; TSC/Rheb integrates growth factor and stress cues at the same compartment. These models frame Nprl2 as a catalytic inhibitory node whose regulation (including arginine methylation) tunes nutrient decisions. (Biochemical Society Transactions, Mar 2023; URL: https://doi.org/10.1042/bst20210038) (lamasherpa2023regulationofmtorc1 pages 2-4, lamasherpa2023regulationofmtorc1 pages 8-9)
- Fly germline checkpoint logic: Expert work in eLife (2019) positions GATOR1 as a key mediator of a meiotic DSB‑triggered metabolic checkpoint, with GATOR2/Mio relieving inhibition to allow growth—an elegant in vivo illustration of how nutrient and genome integrity signals intersect via TORC1 control. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 3-4, wei2019thegatorcomplex pages 1-3)

7) Relevant statistics and quantitative data from recent studies
- Drosophila oogenesis (GATOR1 mutants): TORC1 activity ~3× higher than wild type in mutant ovaries; p53 activation in region 3 cysts rises from <5% (WT) to ~80% (GATOR1 mutants); S6K dose reduction suppresses elevated DSB numbers in iml1‑depleted germlines; atg1 or 4E‑BP loss does not recapitulate the DSB phenotype, arguing for a TORC1→S6K‑specific mechanism. (Wei et al., 2019; URL: https://doi.org/10.7554/eLife.42149) (wei2019thegatorcomplex pages 15-17, wei2019thegatorcomplex pages 7-9)
- NPRL2 methylation kinetics and SAM sensitivity (mammalian cells): NPRL2 R78 asymmetric dimethylation responds to SAM availability (Km for PRMT1 on NPRL2 ~5 μM SAM); SAMTOR binds SAM with Kd ~7 μM, PRMT1 with Kd ~26 μM; methionine promotes PRMT1 and mTOR lysosomal localization and increases lysosomal ADMA signal; PRMT1 loss reduces mTOR–LAMP2 colocalization (Pearson correlation quantitation) and impairs methionine‑induced mTORC1 activation. (Jiang et al., 2023; URL: https://doi.org/10.1016/j.cmet.2023.11.001) (jiang2023prmt1orchestrateswith pages 5-6, jiang2023prmt1orchestrateswith pages 6-8, jiang2023prmt1orchestrateswith pages 26-30)

Functional annotation summary for Drosophila Nprl2 (Q9VXA0)
- Primary molecular role: Catalytic subunit of the GATOR1 complex, acting as a RagA/B GAP to inhibit TORC1 during amino‑acid starvation and in response to meiotic DSBs. (lamasherpa2023regulationofmtorc1 pages 2-4, lamasherpa2023regulationofmtorc1 pages 8-9, wei2019thegatorcomplex pages 3-4)
- Cellular localization where function is executed: Functions at the lysosomal signaling hub through the Ragulator–Rag–GATOR1 axis; Drosophila phenotypes support pathway activity in the germline during oogenesis. (lamasherpa2023regulationofmtorc1 pages 2-4, lamasherpa2023regulationofmtorc1 pages 8-9, wei2019thegatorcomplex pages 1-3)
- Pathway wiring: Upstream amino‑acid sensors signal via GATOR2 to modulate GATOR1; KICSTOR recruits GATOR1 to lysosomes; downstream TORC1 effectors (e.g., S6K) mediate impacts on DSB repair timing and checkpoint signaling. (jiang2023prmt1orchestrateswith pages 19-20, wei2019thegatorcomplex pages 15-17, wei2019thegatorcomplex pages 3-4)
- Phenotypic consequences of loss: Elevated TORC1, impaired starvation‑induced autophagy, delayed meiotic DSB repair, strong p53 hyperactivation, increased retrotransposon expression, and reduced survival to γ‑irradiation. (wei2019thegatorcomplex pages 7-9, wei2019thegatorcomplex pages 15-17, wei2019thegatorcomplex pages 13-15)
- Regulatory innovation (2023): Methionine/SAM‑dependent PRMT1‑mediated methylation of NPRL2 R78 attenuates GATOR1 GAP activity, providing a tunable nutrient‑sensing PTM rheostat for mTORC1 control that likely generalizes across metazoans. (jiang2023prmt1orchestrateswith pages 1-3, jiang2023prmt1orchestrateswith pages 6-8)

Notes on ambiguity
- The symbol “Nprl2/NPRL2” is used across species. All Drosophila-specific functional claims above are supported by fly studies (Wei et al., 2019). Mammalian studies (Ma 2017; Jiang 2023) are invoked to clarify conserved mechanisms (lysosomal Rag regulation; NPRL2 post‑translational control and nuclear roles) and are clearly identified as non‑fly when relevant. (wei2019thegatorcomplex pages 1-3, ma2017tumorsuppressornprl2 pages 2-4, jiang2023prmt1orchestrateswith pages 1-3)

Selected sources with URLs and dates
- Wei et al., 2019, eLife, Oct 2019. The GATOR complex regulates an essential response to meiotic double-stranded breaks in Drosophila. https://doi.org/10.7554/eLife.42149 (wei2019thegatorcomplex pages 1-3, wei2019thegatorcomplex pages 7-9, wei2019thegatorcomplex pages 15-17, wei2019thegatorcomplex pages 13-15, wei2019thegatorcomplex pages 3-4)
- Lama‑Sherpa et al., 2023, Biochemical Society Transactions, Mar 2023. Regulation of mTORC1 by the Rag GTPases. https://doi.org/10.1042/bst20210038 (lamasherpa2023regulationofmtorc1 pages 2-4, lamasherpa2023regulationofmtorc1 pages 8-9)
- Jiang et al., 2023, Cell Metabolism, Dec 2023. PRMT1 orchestrates with SAMTOR to govern mTORC1 methionine sensing via Arg‑methylation of NPRL2. https://doi.org/10.1016/j.cmet.2023.11.001 (jiang2023prmt1orchestrateswith pages 1-3, jiang2023prmt1orchestrateswith pages 5-6, jiang2023prmt1orchestrateswith pages 6-8, jiang2023prmt1orchestrateswith pages 26-30, jiang2023prmt1orchestrateswith pages 19-20)
- Ma et al., 2017, Scientific Reports, Nov 2017. Tumor suppressor NPRL2 induces ROS production and DNA damage response. https://doi.org/10.1038/s41598-017-15497-0 (ma2017tumorsuppressornprl2 pages 2-4, ma2017tumorsuppressornprl2 pages 13-13)
- Sun and Wang, 2023, Int J Mol Sci, Feb 2023. Clocking Epilepsies: A Chronomodulated Strategy‑Based Therapy for Rhythmic Seizures. https://doi.org/10.3390/ijms24044223 (jiang2023prmt1orchestrateswith pages 20-21)

Conclusion
Drosophila Nprl2 is the conserved catalytic subunit of GATOR1 that suppresses TORC1 by acting as a Rag GAP at lysosomes. In vivo, Nprl2/GATOR1 enforces a meiotic DSB‑responsive metabolic checkpoint in the germline, ensuring timely DNA repair and restraining p53 and transposon activation; GATOR2/Mio relieves this inhibition to resume growth. Recent work reveals that NPRL2 is subject to methionine/SAM‑sensitive arginine methylation by PRMT1, establishing a tunable post‑translational control over GATOR1 activity that connects one‑carbon metabolism to mTORC1. Together, these findings refine Nprl2’s placement as a central inhibitory node in nutrient and genome‑integrity signaling, with emerging therapeutic implications through modulation of NPRL2 methylation and GATOR1–lysosome interactions. (wei2019thegatorcomplex pages 3-4, wei2019thegatorcomplex pages 7-9, lamasherpa2023regulationofmtorc1 pages 2-4, jiang2023prmt1orchestrateswith pages 6-8)

References

1. (lamasherpa2023regulationofmtorc1 pages 2-4): Tshering D. Lama-Sherpa, Mi-Hyeon Jeong, and Jenna L. Jewell. Regulation of mtorc1 by the rag gtpases. Biochemical Society Transactions, 51:655-664, Mar 2023. URL: https://doi.org/10.1042/bst20210038, doi:10.1042/bst20210038. This article has 48 citations and is from a peer-reviewed journal.

2. (lamasherpa2023regulationofmtorc1 pages 8-9): Tshering D. Lama-Sherpa, Mi-Hyeon Jeong, and Jenna L. Jewell. Regulation of mtorc1 by the rag gtpases. Biochemical Society Transactions, 51:655-664, Mar 2023. URL: https://doi.org/10.1042/bst20210038, doi:10.1042/bst20210038. This article has 48 citations and is from a peer-reviewed journal.

3. (wei2019thegatorcomplex pages 1-3): Youheng Wei, Lucia Bettedi, Chun-Yuan Ting, Kuikwon Kim, Yingbiao Zhang, Jiadong Cai, and Mary A Lilly. The gator complex regulates an essential response to meiotic double-stranded breaks in drosophila. eLife, Oct 2019. URL: https://doi.org/10.7554/elife.42149, doi:10.7554/elife.42149. This article has 27 citations and is from a domain leading peer-reviewed journal.

4. (wei2019thegatorcomplex pages 3-4): Youheng Wei, Lucia Bettedi, Chun-Yuan Ting, Kuikwon Kim, Yingbiao Zhang, Jiadong Cai, and Mary A Lilly. The gator complex regulates an essential response to meiotic double-stranded breaks in drosophila. eLife, Oct 2019. URL: https://doi.org/10.7554/elife.42149, doi:10.7554/elife.42149. This article has 27 citations and is from a domain leading peer-reviewed journal.

5. (jiang2023prmt1orchestrateswith pages 1-3): Cong Jiang, Jing Liu, Shaohui He, Wei Xu, Runzhi Huang, Weijuan Pan, Xiaolong Li, Xiaoming Dai, Jianping Guo, Tao Zhang, Hiroyuki Inuzuka, Ping Wang, John M. Asara, Jianru Xiao, and Wenyi Wei. Prmt1 orchestrates with samtor to govern mtorc1 methionine sensing via arg-methylation of nprl2. Cell Metabolism, 35:2183-2199.e7, Dec 2023. URL: https://doi.org/10.1016/j.cmet.2023.11.001, doi:10.1016/j.cmet.2023.11.001. This article has 30 citations and is from a highest quality peer-reviewed journal.

6. (jiang2023prmt1orchestrateswith pages 5-6): Cong Jiang, Jing Liu, Shaohui He, Wei Xu, Runzhi Huang, Weijuan Pan, Xiaolong Li, Xiaoming Dai, Jianping Guo, Tao Zhang, Hiroyuki Inuzuka, Ping Wang, John M. Asara, Jianru Xiao, and Wenyi Wei. Prmt1 orchestrates with samtor to govern mtorc1 methionine sensing via arg-methylation of nprl2. Cell Metabolism, 35:2183-2199.e7, Dec 2023. URL: https://doi.org/10.1016/j.cmet.2023.11.001, doi:10.1016/j.cmet.2023.11.001. This article has 30 citations and is from a highest quality peer-reviewed journal.

7. (jiang2023prmt1orchestrateswith pages 6-8): Cong Jiang, Jing Liu, Shaohui He, Wei Xu, Runzhi Huang, Weijuan Pan, Xiaolong Li, Xiaoming Dai, Jianping Guo, Tao Zhang, Hiroyuki Inuzuka, Ping Wang, John M. Asara, Jianru Xiao, and Wenyi Wei. Prmt1 orchestrates with samtor to govern mtorc1 methionine sensing via arg-methylation of nprl2. Cell Metabolism, 35:2183-2199.e7, Dec 2023. URL: https://doi.org/10.1016/j.cmet.2023.11.001, doi:10.1016/j.cmet.2023.11.001. This article has 30 citations and is from a highest quality peer-reviewed journal.

8. (jiang2023prmt1orchestrateswith pages 26-30): Cong Jiang, Jing Liu, Shaohui He, Wei Xu, Runzhi Huang, Weijuan Pan, Xiaolong Li, Xiaoming Dai, Jianping Guo, Tao Zhang, Hiroyuki Inuzuka, Ping Wang, John M. Asara, Jianru Xiao, and Wenyi Wei. Prmt1 orchestrates with samtor to govern mtorc1 methionine sensing via arg-methylation of nprl2. Cell Metabolism, 35:2183-2199.e7, Dec 2023. URL: https://doi.org/10.1016/j.cmet.2023.11.001, doi:10.1016/j.cmet.2023.11.001. This article has 30 citations and is from a highest quality peer-reviewed journal.

9. (wei2019thegatorcomplex pages 7-9): Youheng Wei, Lucia Bettedi, Chun-Yuan Ting, Kuikwon Kim, Yingbiao Zhang, Jiadong Cai, and Mary A Lilly. The gator complex regulates an essential response to meiotic double-stranded breaks in drosophila. eLife, Oct 2019. URL: https://doi.org/10.7554/elife.42149, doi:10.7554/elife.42149. This article has 27 citations and is from a domain leading peer-reviewed journal.

10. (jiang2023prmt1orchestrateswith pages 19-20): Cong Jiang, Jing Liu, Shaohui He, Wei Xu, Runzhi Huang, Weijuan Pan, Xiaolong Li, Xiaoming Dai, Jianping Guo, Tao Zhang, Hiroyuki Inuzuka, Ping Wang, John M. Asara, Jianru Xiao, and Wenyi Wei. Prmt1 orchestrates with samtor to govern mtorc1 methionine sensing via arg-methylation of nprl2. Cell Metabolism, 35:2183-2199.e7, Dec 2023. URL: https://doi.org/10.1016/j.cmet.2023.11.001, doi:10.1016/j.cmet.2023.11.001. This article has 30 citations and is from a highest quality peer-reviewed journal.

11. (ma2017tumorsuppressornprl2 pages 2-4): Yinxing Ma, Licia Silveri, John LaCava, and Svetlana Dokudovskaya. Tumor suppressor nprl2 induces ros production and dna damage response. Scientific Reports, Nov 2017. URL: https://doi.org/10.1038/s41598-017-15497-0, doi:10.1038/s41598-017-15497-0. This article has 29 citations and is from a peer-reviewed journal.

12. (ma2017tumorsuppressornprl2 pages 13-13): Yinxing Ma, Licia Silveri, John LaCava, and Svetlana Dokudovskaya. Tumor suppressor nprl2 induces ros production and dna damage response. Scientific Reports, Nov 2017. URL: https://doi.org/10.1038/s41598-017-15497-0, doi:10.1038/s41598-017-15497-0. This article has 29 citations and is from a peer-reviewed journal.

13. (wei2019thegatorcomplex pages 15-17): Youheng Wei, Lucia Bettedi, Chun-Yuan Ting, Kuikwon Kim, Yingbiao Zhang, Jiadong Cai, and Mary A Lilly. The gator complex regulates an essential response to meiotic double-stranded breaks in drosophila. eLife, Oct 2019. URL: https://doi.org/10.7554/elife.42149, doi:10.7554/elife.42149. This article has 27 citations and is from a domain leading peer-reviewed journal.

14. (wei2019thegatorcomplex pages 13-15): Youheng Wei, Lucia Bettedi, Chun-Yuan Ting, Kuikwon Kim, Yingbiao Zhang, Jiadong Cai, and Mary A Lilly. The gator complex regulates an essential response to meiotic double-stranded breaks in drosophila. eLife, Oct 2019. URL: https://doi.org/10.7554/elife.42149, doi:10.7554/elife.42149. This article has 27 citations and is from a domain leading peer-reviewed journal.

15. (jiang2023prmt1orchestrateswith pages 20-21): Cong Jiang, Jing Liu, Shaohui He, Wei Xu, Runzhi Huang, Weijuan Pan, Xiaolong Li, Xiaoming Dai, Jianping Guo, Tao Zhang, Hiroyuki Inuzuka, Ping Wang, John M. Asara, Jianru Xiao, and Wenyi Wei. Prmt1 orchestrates with samtor to govern mtorc1 methionine sensing via arg-methylation of nprl2. Cell Metabolism, 35:2183-2199.e7, Dec 2023. URL: https://doi.org/10.1016/j.cmet.2023.11.001, doi:10.1016/j.cmet.2023.11.001. This article has 30 citations and is from a highest quality peer-reviewed journal.

Citations

1. wei2019thegatorcomplex pages 7-9
2. wei2019thegatorcomplex pages 13-15
3. wei2019thegatorcomplex pages 15-17
4. wei2019thegatorcomplex pages 1-3
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