ArticleProceedings of the National Academy of Sciences of the United States of America2024
Chemical mapping of the surface interactome of PIEZO1 identifies CADM1 as a modulator of channel inactivation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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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
18 citing papers in PubMed.
- Piezo1 in Peripheral and Central Sensitisation: Implications for Chronic Pain.Bioengineering (Basel, Switzerland) · 2026Review
- Lipid flip-flop in biological membranes: through the lens of TMEM16F.Physiological reviews · 2026Review
- Piezo ion channels in the digestive system: Mechanotransduction pathways and therapeutic targeting strategies.Genes & diseases · 2026Review
- State-dependent binding of the wedge domain controls inactivation of the mechanosensitive ion channel PIEZO1.Nature communications · 2026Article
- Piezo1 channel: structure, mechanogating mechanism, functions, diseases and therapeutic strategy.Molecular biomedicine · 2026Review
- The Role of Piezo Ion Channels in Pulmonary Hypertension.Pulmonary circulation · 2026Review
- The Piezo1-Ca2+-PI3k/Akt signaling axis as a context-dependent mechanotransduction node during skin wound healing.iScience · 2026Review
- Yoda molecules agonize PIEZO2.bioRxiv : the preprint server for biology · 2026Article
- MDFIC2 is a sensory neuron-specific PIEZO channel auxiliary subunit.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Piezo1 in intestinal smooth muscle cells: Emerging perspectives.The Journal of physiology · 2026Review
- PIPProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mechanotransduction mechanisms in human erythrocytes: Fundamental physiology and clinical significance.Channels (Austin, Tex.) · 2025Review
- Targeting PIEZO1-TMEM16F Coupling to Mitigate Sickle Cell Disease Complications.American journal of hematology · 2025Article
- PIEZO Force Sensing in Vascular Biology: An Explosion of New Knowledge, Concepts and Opportunity.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Insulin facilitates entry of calcium ions into human and murine erythrocytes via Piezo1: a newly identified mechanism with implications for type 2 diabetes.The FEBS journal · 2025Article
- Review
- PIEZO channels as multimodal mechanotransducers.Biochemical Society transactions · 2025Review
- The Mechanobiological Hypothesis of Piezo Family-Mediated Exercise Intervention in Spinal Cord Injury Recovery.Neural plasticity · 2025Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The propeller-shaped blades of the PIEZO1 and PIEZO2 ion channels partition into the plasma membrane and respond to indentation or stretching of the lipid bilayer, thus converting mechanical forces into signals that can be interpreted by cells, in the form of calcium flux and changes in membrane potential. While PIEZO channels participate in diverse physiological processes, from sensing the shear stress of blood flow in the vasculature to detecting touch through mechanoreceptors in the skin, the molecular details that enable these mechanosensors to tune their responses over a vast dynamic range of forces remain largely uncharacterized. To survey the molecular landscape surrounding PIEZO channels at the cell surface, we employed a mass spectrometry-based proteomic approach to capture and identify extracellularly exposed proteins in the vicinity of PIEZO1. This PIEZO1-proximal interactome was enriched in surface proteins localized to cell junctions and signaling hubs within the plasma membrane. Functional screening of these interaction candidates by calcium imaging and electrophysiology in an overexpression system identified the adhesion molecule CADM1/SynCAM that slows the inactivation kinetics of PIEZO1 with little effect on PIEZO2. Conversely, we found that CADM1 knockdown accelerates inactivation of endogenous PIEZO1 in Neuro-2a cells. Systematic deletion of CADM1 domains indicates that the transmembrane region is critical for the observed effects on PIEZO1, suggesting that modulation of inactivation is mediated by interactions in or near the lipid bilayer.
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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.