Formation of a new receptor-operated channel by heteromeric assembly of TRPP2 and TRPC1 subunits
| العنوان: | Formation of a new receptor-operated channel by heteromeric assembly of TRPP2 and TRPC1 subunits |
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| المؤلفون: | Aurélie Giamarchi, Lise Rodat-Despoix, Leonidas Tsiokas, Françoise Padilla, Patrick Delmas, Chang Xi Bai, Tamyra Downs |
| المساهمون: | Laboratoire de neurophysiologie cellulaire (LNPC), Université de la Méditerranée - Aix-Marseille 2-Centre National de la Recherche Scientifique (CNRS) |
| المصدر: | EMBO Reports EMBO Reports, 2008, epub ahead of print. ⟨10.1038/embor.2008.29⟩ |
| بيانات النشر: | Nature Publishing Group, 2008. |
| سنة النشر: | 2008 |
| مصطلحات موضوعية: | TRPP Cation Channels, Swine, Protein subunit, Scientific Report, Muscarinic Agonists, Kidney, Biochemistry, Lanthanoid Series Elements, Ion Channels, Cell Line, Receptors, G-Protein-Coupled, TRPC1, Amiloride, Transient receptor potential channel, Mice, Genetics, medicine, Animals, Cilia, Receptor, Molecular Biology, Ion channel, Cells, Cultured, Neurons, Mechanosensation, Chemistry, Oxotremorine, Colocalization, Rats, Protein Subunits, Biophysics, LLC-PK1 Cells, [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC], medicine.drug, Sodium Channel Blockers |
| الوصف: | Although several protein-protein interactions have been reported between transient receptor potential (TRP) channels, they are all known to occur exclusively between members of the same group. The only intergroup interaction described so far is that of TRPP2 and TRPC1; however, the significance of this interaction is unknown. Here, we show that TRPP2 and TRPC1 assemble to form a channel with a unique constellation of new and TRPP2/TRPC1-specific properties. TRPP2/TRPC1 is activated in response to G-protein-coupled receptor activation and shows a pattern of single-channel conductance, amiloride sensitivity and ion permeability distinct from that of TRPP2 or TRPC1 alone. Native TRPP2/TRPC1 activity is shown in kidney cells by complementary gain-of-function and loss-of-function experiments, and its existence under physiological conditions is supported by colocalization at the primary cilium and by co-immunoprecipitation from kidney membranes. Identification of the heteromultimeric TRPP2/TRPC1 channel has implications in mechanosensation and cilium-based Ca(2+) signalling. |
| اللغة: | English |
| تدمد: | 1469-221X 1469-3178 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::410d86b287b86995a96c9e79def9a92eTest https://europepmc.org/articles/PMC2373364Test/ |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....410d86b287b86995a96c9e79def9a92e |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 1469221X 14693178 |
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