ArticleNature communications2012
Molecular mechanism of the assembly of an acid-sensing receptor ion channel complex.
Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 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
35 citing papers in PubMed, 53 citations in OpenAlex.
- A Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026Review
- Cold-Sensing TRP Channels and Temperature Preference Modulate Ovarian Development in the Model OrganismInternational journal of molecular sciences · 2025Article
- A roadmap to cysteine specific labeling of membrane proteins for single-molecule photobleaching studies.Methods (San Diego, Calif.) · 2025Article
- Article
- Bacterial pathogens deliver water/solute-permeable channels as a virulence strategy.bioRxiv : the preprint server for biology · 2023Article
- TRP (transient receptor potential) ion channel family: structures, biological functions and therapeutic interventions for diseases.Signal transduction and targeted therapy · 2023Review
- A single-molecule method for measuring fluorophore labeling yields for the study of membrane protein oligomerization in membranes.PloS one · 2023Article
- The roles of two extracellular loops in proton sensing and permeation in human Otop1 proton channel.Communications biology · 2022Article
- The GPCR properties of polycystin-1- A new paradigm.Frontiers in molecular biosciences · 2022Review
- Nanchung and Inactive define pore properties of the native auditory transduction channel inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structural basis for CaNature communications · 2021Article
- Distribution and Assembly of TRP Ion Channels.Advances in experimental medicine and biology · 2021Article
- The ion channel function of polycystin-1 in the polycystin-1/polycystin-2 complex.EMBO reports · 2019Article
- A PKD1L3 splice variant in taste buds is not cleaved at the G protein-coupled receptor proteolytic site.Biochemical and biophysical research communications · 2019Article
- Heat activation mechanism of TRPV1: New insights from molecular dynamics simulation.Temperature (Austin, Tex.) · 2019Review
- Global versus local mechanisms of temperature sensing in ion channels.Pflugers Archiv : European journal of physiology · 2018Review
- Cryo-EM structure of the polycystic kidney disease-like channel PKD2L1.Nature communications · 2018Article
- A Calmodulin C-Lobe CaNeuron · 2018Article
- Decrypting the Heat Activation Mechanism of TRPV1 Channel by Molecular Dynamics Simulation.Biophysical journal · 2018Article
- Extracellular Loops Are Essential for the Assembly and Function of Polycystin Receptor-Ion Channel Complexes.The Journal of biological chemistry · 2017Article
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 3 institutions in 2 countries.
Funding
Abstract
Polycystic kidney disease (PKD) family proteins associate with transient receptor potential (TRP) channel family proteins to form functionally important complexes. PKD proteins differ from known ion channel-forming proteins and are generally thought to act as membrane receptors. Here we find that PKD1L3, a PKD protein, functions as a channel-forming subunit in an acid-sensing heteromeric complex formed by PKD1L3 and TRPP3, a TRP channel protein. Single amino-acid mutations in the putative pore region of both proteins alter the channel's ion selectivity. The PKD1L3/TRPP3 complex in the plasma membrane of live cells contains one PKD1L3 and three TRPP3. A TRPP3 C-terminal coiled-coil domain forms a trimer in solution and in crystal, and has a crucial role in the assembly and surface expression of the PKD1L3/TRPP3 complex. These results demonstrate that PKD subunits constitute a new class of channel-forming proteins, enriching our understanding of the function of PKD proteins and PKD/TRPP complexes.
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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.