ArticleProceedings of the National Academy of Sciences of the United States of America2021
Receptor-like role for PQLC2 amino acid transporter in the lysosomal sensing of cationic amino acids.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 20 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Cystinosin/Ers1 functions in redox homeostasis in the early secretory pathway.bioRxiv : the preprint server for biology · 2026Article
- Longitudinal plasma proteomics: relation to incident Alzheimer's disease dementia and biomarkers.Alzheimer's & dementia : the journal of the Alzheimer's Association · 2025Article
- Eukaryote-Wide Distribution of a Family of Longin Domain-Containing GAP Complexes for Small GTPases.Traffic (Copenhagen, Denmark) · 2025Article
- BiDAC-dependent degradation of plasma membrane proteins by the endolysosomal system.Nature communications · 2025Article
- ALS-linked C9orf72-SMCR8 complex is a negative regulator of primary ciliogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The role of lysosomes in metabolic and autoimmune diseases.Nature reviews. Nephrology · 2023Review
- Longin domain GAP complexes in nutrient signalling, membrane traffic and neurodegeneration.FEBS letters · 2023Review
- Deciphering genetic causes for sex differences in human health through drug metabolism and transporter genes.Nature communications · 2023Article
- Article
- Structural basis for proton coupled cystine transport by cystinosin.Nature communications · 2022Article
- The progress inSmall GTPases · 2022Review
- Picking the arginine lock on PQLC2 cycling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Arginine-selective modulation of the lysosomal transporter PQLC2 through a gate-tuning mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for the ARF GAP activity and specificity of the C9orf72 complex.Nature communications · 2021Article
- Plug-and-socket mechanisms in nutrient sensing by lysosomal amino acid transporters.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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3 authors at 1 institution in 1 country.
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Abstract
PQLC2, a lysosomal cationic amino acid transporter, also serves as a sensor that responds to scarcity of its substrates by recruiting a protein complex composed of C9orf72, SMCR8, and WDR41 to the surface of lysosomes. This protein complex controls multiple aspects of lysosome function. Although it is known that this response to changes in cationic amino acid availability depends on an interaction between PQLC2 and WDR41, the underlying mechanism for the regulated interaction is not known. In this study, we present evidence that the WDR41-PQLC2 interaction is mediated by a short peptide motif in a flexible loop that extends from the WDR41 β-propeller and inserts into a cavity presented by the inward-facing conformation of PQLC2. The data support a transceptor model wherein conformational changes in PQLC2 related to substrate transport regulate the availability of the WDR41-binding site on PQLC2 and mediate recruitment of the WDR41-SMCR8-C9orf72 complex to the surface of lysosomes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.