ArticleCell2023
Structural basis for membrane-proximal proteolysis of substrates by ADAM10.
Article in Cell, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- Cell surface remodeling caused by the loss of the flippase subunit TMEM30A in immune cells.Journal of cell science · 2026Article
- Engineering CAR-T cells to remodel the mucin-rich cancer cell glycocalyx.bioRxiv : the preprint server for biology · 2026Article
- Naturally occurring ACE2 stalk variants are differentially released from the cell.Scientific reports · 2026Article
- A potential mechanism for tetraspanin CD82-mediated regulation of EGFR.Life science alliance · 2026Article
- Transferrin receptor 1 shedding by the pro-inflammatory iRhom-ADAM17 complex and ADAM10 regulates cellular iron uptake and ferroptosis.Experimental & molecular medicine · 2026Article
- Article
- Naturally occurring ACE2 stalk variants are differentially released from the cell.bioRxiv : the preprint server for biology · 2026Article
- Membrane-Based Assembly and Interactions in Immune Receptors.Chemical reviews · 2026Review
- ADAM10-Mediated Proteolytic Remodelling of Signalling and Adhesion Proteins on Brain Cell-Derived Small Extracellular Vesicles.Journal of extracellular biology · 2026Article
- Isolation Defines Identity: Functional Consequences of Extracellular Vesicle Purification Strategies.Advanced healthcare materials · 2026Article
- Lipid-Facilitated Opening of the ADAM10 Sheddase Revealed by Enhanced Sampling Simulations.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Connexin 26 Functions as a Direct Transcriptional Regulator During the Cochlea Development.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Targeted shedding of extracellular membrane proteins by induced protease recruitment.bioRxiv : the preprint server for biology · 2026Article
- Leukocytic ADAM10 and ADAM17 modulate disease severity and systemic outcome in bacterial and viral pneumonia.The European respiratory journal · 2026Article
- Tetraspanin TSP-12 and SUP-17/ADAM10 exhibit cell type-specific codependence for trafficking through the Golgi.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- LECT2 promotes liver regeneration across developmental stages by activating the ADAM10-NOTCH signaling pathway.Hepatology communications · 2025Article
- Structural basis for regulation of Frizzled-4 signaling by the co-receptor Tetraspanin-12.bioRxiv : the preprint server for biology · 2025Article
- Tetraspanin-enriched membrane domains regulate vascular leakage by altering membrane cholesterol accessibility to balance antagonistic GTPases.Nature cardiovascular research · 2025Article
- Structural insights into the activation and inhibition of the ADAM17-iRhom2 complex.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- An in vivo screen identifies diverse domains that can act as force-dependent proteolytic switches for Notch activation.Science signaling · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The endopeptidase ADAM10 is a critical catalyst for the regulated proteolysis of key drivers of mammalian development, physiology, and non-amyloidogenic cleavage of APP as the primary α-secretase. ADAM10 function requires the formation of a complex with a C8-tetraspanin protein, but how tetraspanin binding enables positioning of the enzyme active site for membrane-proximal cleavage remains unknown. We present here a cryo-EM structure of a vFab-ADAM10-Tspan15 complex, which shows that Tspan15 binding relieves ADAM10 autoinhibition and acts as a molecular measuring stick to position the enzyme active site about 20 Å from the plasma membrane for membrane-proximal substrate cleavage. Cell-based assays of N-cadherin shedding establish that the positioning of the active site by the interface between the ADAM10 catalytic domain and the bound tetraspanin influences selection of the preferred cleavage site. Together, these studies reveal the molecular mechanism underlying ADAM10 proteolysis at membrane-proximal sites and offer a roadmap for its modulation in disease.
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