ArticleJournal of molecular modeling2013
Regulation of the transient receptor potential channel TRPA1 by its N-terminal ankyrin repeat domain.
Article in Journal of molecular modeling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Ion channels of cold transduction and transmission.The Journal of general physiology · 2024Review
- Functions of TRPs in retinal tissue in physiological and pathological conditions.Frontiers in molecular neuroscience · 2024Review
- Dual role of transient receptor potential ankyrin 1 in respiratory and gastrointestinal physiology: From molecular mechanisms to therapeutic targets.Frontiers in physiology · 2024Review
- TRP (transient receptor potential) ion channel family: structures, biological functions and therapeutic interventions for diseases.Signal transduction and targeted therapy · 2023Review
- Transient Receptor Potential Ankyrin 1 (TRPA1) Channel as a Sensor of Oxidative Stress in Cancer Cells.Cells · 2023Review
- Transient Receptor Potential Channel Ankyrin 1: A Unique Regulator of Vascular Function.Cells · 2021Review
- Selenium and Neurological Diseases: Focus on Peripheral Pain and TRP Channels.Current neuropharmacology · 2020Review
- Regulation of vascular tone by transient receptor potential ankyrin 1 channels.Current topics in membranes · 2020Review
- Review
- TRPA1 ankyrin repeat six interacts with a small molecule inhibitor chemotype.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Phosphorylation of the Transient Receptor Potential Ankyrin 1 by Cyclin-dependent Kinase 5 affects Chemo-nociception.Scientific reports · 2018Article
- TRPA1 expression and its functional activation in rodent cortex.Open biology · 2017Article
- Sensitization of TRPA1 by Protein Kinase A.PloS one · 2017Article
- Activation of Transient Receptor Potential Ankyrin-1 by Insoluble Particulate Material and Association with Asthma.American journal of respiratory cell and molecular biology · 2015Article
- Genetic variants affecting human TRPA1 or TRPM8 structure can be classified in vitro as 'well expressed', 'poorly expressed' or 'salvageable'.Bioscience reports · 2015Article
- Article
- Role of TRP channels in the induction of heat shock proteins (Hsps) by heating skin.Biophysics (Nagoya-shi, Japan) · 2015Review
- Potency of irritation by benzylidenemalononitriles in humans correlates with TRPA1 ion channel activation.Royal Society open science · 2015Article
- The transient receptor potential channel TRPA1: from gene to pathophysiology.Pflugers Archiv : European journal of physiology · 2012Review
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transient receptor potential channel A1 (TRPA1) is unique among ion channels of higher vertebrates in that it harbors a large ankyrin repeat domain. The TRPA1 channel is expressed in the inner ear and in nociceptive neurons. It is involved in hearing as well as in the perception of pungent and irritant chemicals. The ankyrin repeat domain has special mechanical properties, which allows it to function as a soft spring that can be extended over a large range while maintaining structural integrity. A calcium-binding site has been experimentally identified within the ankyrin repeats. We built a model of the N-terminal 17 ankyrin repeat structure, including the calcium-binding EF-hand. In our simulations we find the calcium-bound state to be rigid as compared to the calcium-free state. While the end-to-end distance can change by almost 50% in the apo form, these fluctuations are strongly reduced by calcium binding. This increase in stiffness that constraints the end-to-end distance in the holo form is predicted to affect the force acting on the gate of the TRPA1 channel, thereby changing its open probability. Simulations of the transmembrane domain of TRPA1 show that residue N855, which has been associated with familial episodic pain syndrome, forms a strong link between the S4-S5 connecting helix and S1, thereby creating a direct force link between the N-terminus and the gate. The N855S mutation weakens this interaction, thereby reducing the communication between the N-terminus and the transmembrane part of TRPA1.
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Registered trials
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