ArticleScience advances2020
TRPML2 is an osmo/mechanosensitive cation channel in endolysosomal organelles.
Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 59 citations in OpenAlex.
- Mechanically Regulated Secretion: How Physical Forces Instruct the Secretory Pathway and Remodel the Secretome.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- NF-κB-Dependent Transcriptional Regulation of Piezo1 Mediates Bacterial Clearance on Infected Lung Stiffness.American journal of respiratory cell and molecular biology · 2026Article
- Obinutuzumab induces lysosomal destabilization via sphingomyelin-dependent inhibition of TRPML2.Scientific reports · 2026Article
- Microvesicles, exosomes and their combinations with cytoplasmic organelles: from their discovery to their innovative roles in clinical medicine.Biology direct · 2026Review
- Review
- NF-κB-Dependent Transcriptional Regulation of Piezo1 Mediates Bacterial Clearance on Stiffened Lung Matrix.bioRxiv : the preprint server for biology · 2025Article
- Physiological functions and pharmacological targeting of transient receptor potential channels.Pharmacological reviews · 2025Review
- Lysosomal ion channels and pain.Pain reports · 2025Review
- TRPML2 in distinct states reveals the activation and modulation principles of the TRPML family.Nature communications · 2025Article
- The spectrum of lysosomal stress and damage responses: from mechanosensing to inflammation.EMBO reports · 2025Review
- Lysosomal Ion Channels and Transporters: Recent Findings, Therapeutic Potential, and Technical Approaches.Bioelectricity · 2025Review
- SARS-CoV-2 ORF3a accessory protein is a water-permeable channel that induces lysosome swelling.Communications biology · 2025Article
- Lysosomes finely control macrophage inflammatory function via regulating the release of lysosomal FeNature communications · 2025Article
- INPP4B promotes PDAC aggressiveness via PIKfyve and TRPML-1-mediated lysosomal exocytosis.The Journal of cell biology · 2024Article
- Pressure sensing of lysosomes enables control of TFEB responses in macrophages.Nature cell biology · 2024Article
- The ion channels of endomembranes.Physiological reviews · 2024Review
- CaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Drosophila TMEM63 and mouse TMEM63A are lysosomal mechanosensory ion channels.Nature cell biology · 2024Article
- Lysosomal channels sensing forces.Nature cell biology · 2024Article
- Two-pore channel regulators - Who is in control?Frontiers in physiology · 2024Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endolysosomes are dynamic, intracellular compartments, regulating their surface-to-volume ratios to counteract membrane swelling or shrinkage caused by osmotic challenges upon tubulation and vesiculation events. While osmosensitivity has been extensively described on the plasma membrane, the mechanisms underlying endolysosomal surface-to-volume ratio changes and identities of involved ion channels remain elusive. Endolysosomes mediate endocytosis, exocytosis, cargo transport, and sorting of material for recycling or degradation. We demonstrate the endolysosomal cation channel TRPML2 to be hypotonicity/mechanosensitive, a feature crucial to its involvement in fast-recycling processes of immune cells. We demonstrate that the phosphoinositide binding pocket is required for TRPML2 hypotonicity-sensitivity, as substitution of L314 completely abrogates hypotonicity-sensitivity. Last, the hypotonicity-insensitive TRPML2 mutant L314R slows down the fast recycling pathway, corroborating the functional importance of hypotonicity-sensitive TRPML2. Our results highlight TRPML2 as an accelerator of endolysosomal trafficking by virtue of its hypotonicity-sensitivity, with implications in immune cell surveillance and viral trafficking.
Identifiers
What OpenQuestion holds
Registered trials
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.