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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
ILT1 corresponds to the systematic ORF name YDR090C in Saccharomyces cerevisiae (strain ATCC 204508 / S288c), encoding a 310-amino-acid uncharacterized membrane protein (UniProt accession Q03193). The protein is annotated with PQ-loop repeat domains (InterPro IPR006603; Pfam PF04193) and an LAAT-1 domain (InterPro IPR051415), placing it within the lysosomal cystine transporter (LCT) family of the Transporter-Opsin-G protein coupled receptor (TOG) superfamily (saudek2012cystinosinmpdu1sweets pages 3-5). A comprehensive bioinformatic survey by Saudek (2012) explicitly listed YDR090C (Q03193) as one of eight PQ-loop family proteins in S. cerevisiae, designating it as an "uncharacterized membrane protein" (saudek2012cystinosinmpdu1sweets pages 3-5). YDR090C also appears in the phylogenetic tree of yeast and human PQ-loop proteins constructed by Jézégou et al. (2012) (jezegou2012heptahelicalproteinpqlc2 pages 4-5).
Importantly, YDR090C is distinct from the three best-characterized yeast PQ-loop proteins — Ypq1 (YOL092W), Ypq2 (YDR352W), and Ypq3 (YBR147W/RTC2) — which have been functionally characterized as vacuolar basic amino acid transporters (jezegou2012heptahelicalproteinpqlc2 pages 3-4). The following table provides a comprehensive overview of the PQ-loop family in yeast:
| UniProt ID | Systematic name | Gene name(s) | Length (aa) | PQ-loop family status in S. cerevisiae | Known / inferred function |
|---|---|---|---|---|---|
| Q03193 | YDR090C | ILT1, YDR090C | 310 | PQ-loop family member; distinct from Ypq1–3 (saudek2012cystinosinmpdu1sweets pages 3-5, jezegou2012heptahelicalproteinpqlc2 pages 3-4) | Uncharacterized membrane protein. No direct biochemical function established in the retrieved literature. Based on PQ-loop/LAAT-1 domains and family context, it is most plausibly a 7-TM vacuolar/lysosomal transporter-like protein involved in small-solute, likely amino-acid-related, transport or homeostasis, but this remains inference rather than direct evidence (saudek2012cystinosinmpdu1sweets pages 3-5, guo2022structureandmechanism pages 3-5, bianchi2019regulationofamino pages 15-17, liu2012laat1isthe pages 3-4). |
| Q12010 | YOL092W | YPQ1, YOL092W | 308 | PQ-loop family member; one of the three best-characterized yeast Ypq proteins (llinares2015theap3adaptor pages 1-2, jezegou2012heptahelicalproteinpqlc2 pages 3-4) | Vacuolar membrane basic amino acid transporter implicated in cationic amino acid homeostasis; reported as a vacuolar lysine/arginine transporter/exporter in different experimental contexts and strongly linked to lysine-responsive vacuolar membrane quality control and degradation (kawanokawada2018transportofamino pages 2-3, jezegou2012heptahelicalproteinpqlc2 pages 4-5, jezegou2012heptahelicalproteinpqlc2 pages 9-10). |
| Q06328 | YDR352W | YPQ2, YDR352W | 317 | PQ-loop family member; one of the three best-characterized yeast Ypq proteins (llinares2015theap3adaptor pages 1-2, jezegou2012heptahelicalproteinpqlc2 pages 3-4) | Vacuolar membrane basic amino acid transporter; functional ortholog of mammalian PQLC2. Best evidence supports arginine export from the vacuole during nitrogen starvation and broader cationic amino acid homeostasis (llinares2015theap3adaptor pages 1-2, cools2020nitrogencoordinatedimport pages 28-29, cools2020nitrogencoordinatedimport pages 21-22). |
| P38279 | YBR147W | RTC2, YPQ3, YBR147W | 296 | PQ-loop family member; grouped with Ypq1/2 in yeast vacuolar PQ-loop proteins (jezegou2012heptahelicalproteinpqlc2 pages 3-4, saudek2012cystinosinmpdu1sweets pages 3-5) | Vacuolar membrane basic amino acid transporter implicated in cationic amino acid homeostasis; evidence suggests a role particularly in histidine and/or lysine-related vacuolar transport, though less directly characterized than Ypq1/2 (kawanokawada2018transportofamino pages 2-3, jezegou2012heptahelicalproteinpqlc2 pages 4-5). |
| P17261 | YCR075C | ERS1, YCR075C | 260 | PQ-loop family member; yeast homolog of cystinosin (jezegou2012heptahelicalproteinpqlc2 pages 3-4) | Functional homolog of human cystinosin by complementation evidence, but native yeast biochemical activity remains incompletely resolved. Reported to localize to vacuole/endosome and proposed to participate in lysosome/vacuole-related transport or trafficking functions (jezegou2012heptahelicalproteinpqlc2 pages 3-4, saudek2012cystinosinmpdu1sweets pages 3-5). |
| P18414 | YBL040C | ERD2, YBL040C | 219 | PQ-loop family member in broad family classifications (saudek2012cystinosinmpdu1sweets pages 3-5) | ER lumen protein-retaining receptor (HDEL receptor); a well-established retrieval receptor rather than a vacuolar basic amino acid transporter. Included here because it falls within the broader PQ-loop-related family classification used in comparative analyses (saudek2012cystinosinmpdu1sweets pages 3-5). |
| P25565 | YCL002C | YCL002C, YCL2C | 251 | PQ-loop family member in broad family classifications (saudek2012cystinosinmpdu1sweets pages 3-5) | Putative uncharacterized PQ-loop membrane protein; no direct function established in the retrieved literature (saudek2012cystinosinmpdu1sweets pages 3-5). |
| Q03687 | YMR010W | YMR010W | 405 | PQ-loop family member in broad family classifications (saudek2012cystinosinmpdu1sweets pages 3-5) | Uncharacterized membrane protein; no direct biochemical function established in the retrieved literature (saudek2012cystinosinmpdu1sweets pages 3-5). |
Table: This table summarizes the PQ-loop family proteins reported in Saccharomyces cerevisiae, combining broad family listings with functional evidence where available. It is especially useful for distinguishing the uncharacterized YDR090C/ILT1 protein from the better-studied Ypq1–Ypq3 vacuolar amino acid transporters.
YDR090C possesses the hallmark domains of PQ-loop family proteins: two internal PQ-loop repeats (containing conserved proline-glutamine dipeptides) and predicted seven-transmembrane (7-TM) helical topology (bianchi2019regulationofamino pages 15-17, jezegou2012heptahelicalproteinpqlc2 pages 2-3, kawanokawada2018transportofamino pages 2-3). Structural studies on the closely related family member cystinosin have revealed that PQ-loop proteins adopt a characteristic 3+1+3 architecture, in which two related three-transmembrane-helix bundles (TMs 1–3 and TMs 5–7) are connected by an inversion linker helix (TM4), forming a central substrate binding cavity at the interface of the two bundles (guo2022structureandmechanism pages 3-5, bianchi2019regulationofamino pages 15-17). The conserved PQ motifs are actually located within transmembrane helices TM1 and TM5, rather than in loop regions as originally supposed, and they play essential roles in conformational transitions during the transport cycle (guo2022structureandmechanism pages 9-11).
PQ-loop transporters operate via an alternating access mechanism, oscillating between lumen-open (outward-open) and cytosol-open (inward-open) conformations. This involves rigid-body movements of the two three-helix bundles around the central substrate binding site. Conserved salt bridges on either side of the binding site serve as gates that control access from the luminal and cytosolic sides of the membrane (guo2022structureandmechanism pages 3-5, lobel2022structuralbasisfor pages 6-7, guo2022structureandmechanism pages 9-11). The structural resolution of cystinosin from both Arabidopsis thaliana and humans has firmly established this mechanistic framework for the entire PQ-loop family (guo2022structureandmechanism pages 3-5, lobel2022structuralbasisfor pages 6-7, lobel2022structuralbasisfor pages 3-4).
Although YDR090C/ILT1 itself has not been directly characterized biochemically, strong functional predictions can be made based on its domain architecture and the experimentally established functions of its yeast paralogs and orthologs in other organisms.
The three closest yeast paralogs of YDR090C — Ypq1, Ypq2, and Ypq3 — are all vacuolar membrane proteins that function as cationic (basic) amino acid transporters. Ypq1 mediates ATP-dependent uptake of lysine and arginine into vacuolar membrane vesicles (kawanokawada2018transportofamino pages 2-3). Ypq2 functions as an exporter of intravacuolar arginine under nitrogen starvation conditions and has been demonstrated to be a functional ortholog of mammalian PQLC2 (llinares2015theap3adaptor pages 1-2, cools2020nitrogencoordinatedimport pages 21-22). Ypq3 has been implicated in histidine uptake into vacuoles and may also export lysine from the vacuole to the cytosol; its expression is under the control of the Lys14 transcription factor and is repressed by excess lysine (kawanokawada2018transportofamino pages 2-3, jezegou2012heptahelicalproteinpqlc2 pages 4-5). A quadruple mutant lacking all three Ypq proteins plus Avt1 completely lost basic amino acid uptake activity at the vacuolar membrane (kawanokawada2018transportofamino pages 2-3).
The mammalian PQ-loop protein PQLC2 localizes to lysosomes and catalyzes a robust, electrogenic transport selective for cationic amino acids including lysine, arginine, and histidine, and is strongly activated at low extracytosolic pH (jezegou2012heptahelicalproteinpqlc2 pages 2-3, jezegou2012heptahelicalproteinpqlc2 pages 4-5). In Caenorhabditis elegans, the PQ-loop family member LAAT-1 (lysosomal amino acid transporter-1) functions as a lysosomal lysine/arginine transporter essential for amino acid homeostasis: laat-1 mutant lysosomes accumulate lysine and arginine at 16-fold and 8-fold higher levels than wild-type, respectively, while cystine levels remain normal (liu2012laat1isthe pages 3-4).
Another well-characterized PQ-loop family member is cystinosin (encoded by CTNS in humans, with the yeast homolog being Ers1/YCR075C). Cystinosin is a proton-coupled cystine symporter that exports cystine from the lysosomal lumen; mutations cause cystinosis, a lysosomal storage disease (ruivo2012mechanismofprotonsubstrate pages 1-2). This demonstrates that while most characterized PQ-loop proteins transport basic amino acids, the family can accommodate divergent substrate specificities.
The following blockquote summarizes the functional inference for YDR090C:
YDR090C/ILT1 is best interpreted as a PQ-loop family membrane protein in Saccharomyces cerevisiae, not as one of the experimentally characterized Ypq transporters themselves. It carries the defining PQ-loop/LAAT-1-type architecture associated with seven transmembrane helices and membership in the lysosomal cystine transporter/PQ-loop family, but the specific substrate and physiological role of YDR090C have not yet been established directly in the available primary literature (saudek2012cystinosinmpdu1sweets pages 3-5, jezegou2012heptahelicalproteinpqlc2 pages 3-4).
Functional inference comes from better-characterized fungal and metazoan relatives. In budding yeast, the closest characterized paralogs Ypq1/YOL092W, Ypq2/YDR352W, and Ypq3/YBR147W are vacuolar PQ-loop proteins involved in cationic/basic amino-acid homeostasis, while mammalian PQLC2 and C. elegans LAAT-1 mediate lysosomal export of basic amino acids such as lysine and arginine; the family founder cystinosin instead transports cystine, showing that PQ-loop proteins are transporter-like but can differ in substrate specificity (llinares2015theap3adaptor pages 1-2, jezegou2012heptahelicalproteinpqlc2 pages 4-5, jezegou2012heptahelicalproteinpqlc2 pages 9-10, jezegou2012heptahelicalproteinpqlc2 pages 2-3, liu2012laat1isthe pages 3-4).
On that basis, the most defensible current model is that YDR090C/ILT1 is a vacuolar/lysosomal membrane transporter-like protein, likely participating in amino-acid efflux or compartmental amino-acid homeostasis, with basic amino acids being a plausible candidate substrate class by analogy to Ypq1-3, PQLC2, and LAAT-1. However, this remains a prediction from homology and domain architecture, not an experimentally proven annotation for YDR090C itself (bianchi2019regulationofamino pages 15-17, liu2012laat1isthe pages 3-4, jezegou2012heptahelicalproteinpqlc2 pages 4-5, cools2020nitrogencoordinatedimport pages 21-22).
Structural work on PQ-loop proteins provides a mechanistic rationale for this inference: these proteins share a 3+1+3 topology, in which two related 3-transmembrane bundles form the transport core and move by an alternating-access mechanism to expose a central substrate-binding cavity to opposite sides of the membrane. This framework, resolved for cystinosin and generalized across PQ-loop transporters, strongly supports interpreting YDR090C as a small-solute transporter rather than a soluble regulatory protein, even though its precise transported substrate remains unknown (guo2022structureandmechanism pages 3-5, lobel2022structuralbasisfor pages 6-7, guo2022structureandmechanism pages 9-11, bianchi2019regulationofamino pages 15-17).
Blockquote: This blockquote summarizes the strongest current inference for YDR090C/ILT1 based on PQ-loop family membership, domain architecture, and comparison with characterized paralogs and orthologs. It is useful because direct experimental data on YDR090C are sparse, so function must be inferred cautiously from structural and evolutionary evidence.
No direct experimental localization data for YDR090C/ILT1 was identified in the primary literature. However, its localization can be inferred from family context. All three yeast Ypq proteins (Ypq1–3) localize to the vacuolar membrane and are delivered there via the AP-3 adaptor complex-dependent alkaline phosphatase (ALP) trafficking pathway, utilizing an acidic dileucine motif in their second cytosolic loop (llinares2015theap3adaptor pages 1-2). Similarly, Ers1 (the yeast cystinosin homolog) localizes to the vacuole and endosomes (saudek2012cystinosinmpdu1sweets pages 3-5). In metazoans, PQLC2 localizes to lysosomes and LAAT-1 localizes to lysosomal membranes via a C-terminal dileucine-based sorting motif (liu2012laat1isthe pages 3-4). Given that YDR090C shares the PQ-loop/LAAT-1 domain architecture with these proteins, it is most likely a vacuolar membrane protein or associated with endomembrane compartments involved in vacuolar trafficking.
The yeast vacuole serves as the primary storage compartment for amino acids, accumulating approximately 50% of total cellular amino acids under nutrient-rich conditions (kawanokawada2018transportofamino pages 1-2). The composition of amino acids differs markedly between the vacuolar lumen and the cytosol, reflecting the coordinated action of multiple vacuolar transporters including the Ypq proteins, Vba importers, Avt family transporters, and Vsb1 (kawanokawada2018transportofamino pages 2-3, cools2020nitrogencoordinatedimport pages 21-22, kawanokawada2018transportofamino pages 1-2). Ypq proteins and Vba proteins work in a coordinated manner: Vba1–3 mediate import of cationic amino acids into the vacuole, while Ypq proteins mediate their export to the cytosol (jezegou2012heptahelicalproteinpqlc2 pages 4-5, jezegou2012heptahelicalproteinpqlc2 pages 9-10).
The activity of vacuolar amino acid transporters is regulated by nitrogen availability. Under nitrogen-replete conditions, arginine is actively imported into the vacuole via Vsb1; upon nitrogen starvation, Vsb1 activity is inhibited and Ypq2 exports stored arginine to the cytosol for biosynthetic recycling (cools2020nitrogencoordinatedimport pages 28-29, cools2020nitrogencoordinatedimport pages 21-22). This inverse regulation by nitrogen status represents a key mechanism for adapting amino acid metabolism to nutrient availability.
Ypq1 has emerged as a model substrate for studying ubiquitin-dependent quality control of vacuolar membrane proteins. Upon lysine starvation, Ypq1 is ubiquitinated and sorted into the vacuolar lumen for degradation via the ESCRT (endosomal sorting complexes required for transport) machinery, a process termed the vacuolar membrane recycling and degradation (vReD) pathway (jezegou2012heptahelicalproteinpqlc2 pages 4-5, jezegou2012heptahelicalproteinpqlc2 pages 9-10). Whether YDR090C is similarly subject to starvation-induced or condition-dependent degradation remains unknown.
The gene name ILT1 (Ionic Liquid Tolerance 1) for YDR090C appears to originate from studies on yeast tolerance to ionic liquids, which are solvents used in biomass pretreatment. A study by Reed et al. (2019) reported on directed evolution of an ILT1 homolog from Yarrowia lipolytica for improved ionic liquid tolerance in S. cerevisiae. The mechanistic basis for how a PQ-loop membrane protein might contribute to ionic liquid tolerance is not well established, and this phenotypic naming convention should not be conflated with the primary molecular function of the protein, which is more likely related to vacuolar amino acid transport based on domain architecture.
YDR090C/ILT1 remains an experimentally uncharacterized member of the PQ-loop family of membrane transporters in S. cerevisiae. Based on its domain architecture (PQ-loop repeats, LAAT-1 domain, predicted 7-TM topology) and the well-characterized functions of its yeast paralogs (Ypq1–3) and metazoan orthologs (PQLC2, LAAT-1, cystinosin), YDR090C is most plausibly a vacuolar membrane transporter involved in amino acid efflux or compartmental amino acid homeostasis, with basic amino acids being a probable substrate class. However, it should be noted that PQ-loop family members can transport different substrates (e.g., cystine for cystinosin), and the specific substrate of YDR090C cannot be definitively assigned without direct biochemical characterization. Structural studies on cystinosin (guo2022structureandmechanism pages 3-5, lobel2022structuralbasisfor pages 6-7) provide a framework for understanding the likely alternating-access transport mechanism of YDR090C. Future work involving heterologous expression, reconstitution into proteoliposomes, and transport assays would be needed to establish the substrate specificity and transport properties of this protein directly.
References
(saudek2012cystinosinmpdu1sweets pages 3-5): Vladimir Saudek. Cystinosin, mpdu1, sweets and kdelr belong to a well-defined protein family with putative function of cargo receptors involved in vesicle trafficking. PLoS ONE, 7:e30876, Feb 2012. URL: https://doi.org/10.1371/journal.pone.0030876, doi:10.1371/journal.pone.0030876. This article has 63 citations and is from a peer-reviewed journal.
(jezegou2012heptahelicalproteinpqlc2 pages 4-5): Adrien Jézégou, Elisa Llinares, Christine Anne, Sylvie Kieffer-Jaquinod, Seana O’Regan, Joëlle Aupetit, Allel Chabli, Corinne Sagné, Cécile Debacker, Bernadette Chadefaux-Vekemans, Agnès Journet, Bruno André, and Bruno Gasnier. Heptahelical protein pqlc2 is a lysosomal cationic amino acid exporter underlying the action of cysteamine in cystinosis therapy. Proceedings of the National Academy of Sciences, 109:E3434-E3443, Nov 2012. URL: https://doi.org/10.1073/pnas.1211198109, doi:10.1073/pnas.1211198109. This article has 236 citations and is from a highest quality peer-reviewed journal.
(jezegou2012heptahelicalproteinpqlc2 pages 3-4): Adrien Jézégou, Elisa Llinares, Christine Anne, Sylvie Kieffer-Jaquinod, Seana O’Regan, Joëlle Aupetit, Allel Chabli, Corinne Sagné, Cécile Debacker, Bernadette Chadefaux-Vekemans, Agnès Journet, Bruno André, and Bruno Gasnier. Heptahelical protein pqlc2 is a lysosomal cationic amino acid exporter underlying the action of cysteamine in cystinosis therapy. Proceedings of the National Academy of Sciences, 109:E3434-E3443, Nov 2012. URL: https://doi.org/10.1073/pnas.1211198109, doi:10.1073/pnas.1211198109. This article has 236 citations and is from a highest quality peer-reviewed journal.
(guo2022structureandmechanism pages 3-5): Xue Guo, Philip Schmiege, Tufa E. Assafa, Rong Wang, Yan Xu, Linda Donnelly, Michael Fine, Xiaodan Ni, Jiansen Jiang, Glenn Millhauser, Liang Feng, and Xiaochun Li. Structure and mechanism of human cystine exporter cystinosin. Cell, 185:3739-3752.e18, Sep 2022. URL: https://doi.org/10.1016/j.cell.2022.08.020, doi:10.1016/j.cell.2022.08.020. This article has 60 citations and is from a highest quality peer-reviewed journal.
(bianchi2019regulationofamino pages 15-17): Frans Bianchi, Joury S. van’t Klooster, Stephanie J. Ruiz, and Bert Poolman. Regulation of amino acid transport in saccharomyces cerevisiae. Microbiology and Molecular Biology Reviews, Nov 2019. URL: https://doi.org/10.1128/mmbr.00024-19, doi:10.1128/mmbr.00024-19. This article has 171 citations and is from a domain leading peer-reviewed journal.
(liu2012laat1isthe pages 3-4): Bin Liu, Hongwei Du, Rachael Rutkowski, Anton Gartner, and Xiaochen Wang. Laat-1 is the lysosomal lysine/arginine transporter that maintains amino acid homeostasis. Science, 337:351-354, Jul 2012. URL: https://doi.org/10.1126/science.1220281, doi:10.1126/science.1220281. This article has 230 citations and is from a highest quality peer-reviewed journal.
(llinares2015theap3adaptor pages 1-2): Elisa Llinares, Abdoulaye Oury Barry, and Bruno André. The ap-3 adaptor complex mediates sorting of yeast and mammalian pq-loop-family basic amino acid transporters to the vacuolar/lysosomal membrane. Scientific Reports, Nov 2015. URL: https://doi.org/10.1038/srep16665, doi:10.1038/srep16665. This article has 42 citations and is from a peer-reviewed journal.
(kawanokawada2018transportofamino pages 2-3): Miyuki Kawano-Kawada, Yoshimi Kakinuma, and Takayuki Sekito. Transport of amino acids across the vacuolar membrane of yeast: its mechanism and physiological role. Biological & pharmaceutical bulletin, 41 10:1496-1501, Oct 2018. URL: https://doi.org/10.1248/bpb.b18-00165, doi:10.1248/bpb.b18-00165. This article has 42 citations and is from a peer-reviewed journal.
(jezegou2012heptahelicalproteinpqlc2 pages 9-10): Adrien Jézégou, Elisa Llinares, Christine Anne, Sylvie Kieffer-Jaquinod, Seana O’Regan, Joëlle Aupetit, Allel Chabli, Corinne Sagné, Cécile Debacker, Bernadette Chadefaux-Vekemans, Agnès Journet, Bruno André, and Bruno Gasnier. Heptahelical protein pqlc2 is a lysosomal cationic amino acid exporter underlying the action of cysteamine in cystinosis therapy. Proceedings of the National Academy of Sciences, 109:E3434-E3443, Nov 2012. URL: https://doi.org/10.1073/pnas.1211198109, doi:10.1073/pnas.1211198109. This article has 236 citations and is from a highest quality peer-reviewed journal.
(cools2020nitrogencoordinatedimport pages 28-29): Melody Cools, Simon Lissoir, Elisabeth Bodo, Judith Ulloa-Calzonzin, Alexander DeLuna, Isabelle Georis, and Bruno André. Nitrogen coordinated import and export of arginine across the yeast vacuolar membrane. Aug 2020. URL: https://doi.org/10.1371/journal.pgen.1008966, doi:10.1371/journal.pgen.1008966. This article has 29 citations and is from a domain leading peer-reviewed journal.
(cools2020nitrogencoordinatedimport pages 21-22): Melody Cools, Simon Lissoir, Elisabeth Bodo, Judith Ulloa-Calzonzin, Alexander DeLuna, Isabelle Georis, and Bruno André. Nitrogen coordinated import and export of arginine across the yeast vacuolar membrane. Aug 2020. URL: https://doi.org/10.1371/journal.pgen.1008966, doi:10.1371/journal.pgen.1008966. This article has 29 citations and is from a domain leading peer-reviewed journal.
(jezegou2012heptahelicalproteinpqlc2 pages 2-3): Adrien Jézégou, Elisa Llinares, Christine Anne, Sylvie Kieffer-Jaquinod, Seana O’Regan, Joëlle Aupetit, Allel Chabli, Corinne Sagné, Cécile Debacker, Bernadette Chadefaux-Vekemans, Agnès Journet, Bruno André, and Bruno Gasnier. Heptahelical protein pqlc2 is a lysosomal cationic amino acid exporter underlying the action of cysteamine in cystinosis therapy. Proceedings of the National Academy of Sciences, 109:E3434-E3443, Nov 2012. URL: https://doi.org/10.1073/pnas.1211198109, doi:10.1073/pnas.1211198109. This article has 236 citations and is from a highest quality peer-reviewed journal.
(guo2022structureandmechanism pages 9-11): Xue Guo, Philip Schmiege, Tufa E. Assafa, Rong Wang, Yan Xu, Linda Donnelly, Michael Fine, Xiaodan Ni, Jiansen Jiang, Glenn Millhauser, Liang Feng, and Xiaochun Li. Structure and mechanism of human cystine exporter cystinosin. Cell, 185:3739-3752.e18, Sep 2022. URL: https://doi.org/10.1016/j.cell.2022.08.020, doi:10.1016/j.cell.2022.08.020. This article has 60 citations and is from a highest quality peer-reviewed journal.
(lobel2022structuralbasisfor pages 6-7): Mark Löbel, Sacha P. Salphati, Kamel El Omari, Armin Wagner, Stephen J. Tucker, Joanne L. Parker, and Simon Newstead. Structural basis for proton coupled cystine transport by cystinosin. Nature Communications, Aug 2022. URL: https://doi.org/10.1038/s41467-022-32589-2, doi:10.1038/s41467-022-32589-2. This article has 38 citations and is from a highest quality peer-reviewed journal.
(lobel2022structuralbasisfor pages 3-4): Mark Löbel, Sacha P. Salphati, Kamel El Omari, Armin Wagner, Stephen J. Tucker, Joanne L. Parker, and Simon Newstead. Structural basis for proton coupled cystine transport by cystinosin. Nature Communications, Aug 2022. URL: https://doi.org/10.1038/s41467-022-32589-2, doi:10.1038/s41467-022-32589-2. This article has 38 citations and is from a highest quality peer-reviewed journal.
(ruivo2012mechanismofprotonsubstrate pages 1-2): Raquel Ruivo, Gian Carlo Bellenchi, Xiong Chen, Giovanni Zifarelli, Corinne Sagné, Cécile Debacker, Michael Pusch, Stéphane Supplisson, and Bruno Gasnier. Mechanism of proton/substrate coupling in the heptahelical lysosomal transporter cystinosin. Proceedings of the National Academy of Sciences, 109:E210-E217, Jan 2012. URL: https://doi.org/10.1073/pnas.1115581109, doi:10.1073/pnas.1115581109. This article has 68 citations and is from a highest quality peer-reviewed journal.
(kawanokawada2018transportofamino pages 1-2): Miyuki Kawano-Kawada, Yoshimi Kakinuma, and Takayuki Sekito. Transport of amino acids across the vacuolar membrane of yeast: its mechanism and physiological role. Biological & pharmaceutical bulletin, 41 10:1496-1501, Oct 2018. URL: https://doi.org/10.1248/bpb.b18-00165, doi:10.1248/bpb.b18-00165. This article has 42 citations and is from a peer-reviewed journal.