ArticleThe Biochemical journal2001
The transient receptor potential, TRP4, cation channel is a novel member of the family of calmodulin binding proteins.
Article in The Biochemical journal, 2001. 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, 75 citations in OpenAlex.
- Drafting the calmodulation playbook: Emerging structural insights into transient receptor potential channel regulation by calmodulin.The Journal of physiology · 2026Review
- Recent advancement of sonogenetics: A promising noninvasive cellular manipulation by ultrasound.Genes & diseases · 2024Review
- TRPC channels: Structure, function, regulation and recent advances in small molecular probes.Pharmacology & therapeutics · 2020Review
- A CaScientific reports · 2019Article
- Article
- Intracellular spermine blocks TRPC4 channel via electrostatic interaction with C-terminal negative amino acids.Pflugers Archiv : European journal of physiology · 2016Article
- Canonical transient receptor potential 4 and its small molecule modulators.Science China. Life sciences · 2015Review
- Trans-activation response (TAR) RNA-binding protein 2 is a novel modulator of transient receptor potential canonical 4 (TRPC4) protein.The Journal of biological chemistry · 2014Article
- The serine-threonine phosphatase calcineurin is a regulator of endothelial store-operated calcium entry.Pulmonary circulation · 2014Article
- Ca2+-dependent desensitization of TRPV2 channels is mediated by hydrolysis of phosphatidylinositol 4,5-bisphosphate.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Ca2+-calmodulin-dependent myosin light chain kinase is essential for activation of TRPC5 channels expressed in HEK293 cells.The Journal of physiology · 2006Article
- Specific detection and semi-quantitative analysis of TRPC4 protein expression by antibodies.Pflugers Archiv : European journal of physiology · 2005Review
- Multiple roles of calmodulin and other Ca(2+)-binding proteins in the functional regulation of TRP channels.Pflugers Archiv : European journal of physiology · 2005Review
- Receptor-operated cation channels formed by TRPC4 and TRPC5.Naunyn-Schmiedeberg's archives of pharmacology · 2005Review
- The epithelial calcium channels TRPV5 and TRPV6: regulation and implications for disease.Naunyn-Schmiedeberg's archives of pharmacology · 2005Review
- Calmidazolium and arachidonate activate a calcium entry pathway that is distinct from store-operated calcium influx in HeLa cells.The Biochemical journal · 2004Article
- Structural determinant of TRPV1 desensitization interacts with calmodulin.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Characterization of a pathogen-induced calmodulin-binding protein: mapping of four Ca2+-dependent calmodulin-binding domains.Plant molecular biology · 2003Article
- Alpha 1-adrenoceptor-activated cation currents in neurones acutely isolated from rat cardiac parasympathetic ganglia.The Journal of physiology · 2003Article
- The mouse C-type transient receptor potential 2 (TRPC2) channel: alternative splicing and calmodulin binding to its N terminus.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mammalian gene products, transient receptor potential (trp)1 to trp7, are related to the Drosophila TRP and TRP-like ion channels, and are candidate proteins underlying agonist-activated Ca(2+)-permeable ion channels. Recently, the TRP4 protein has been shown to be part of native store-operated Ca(2+)-permeable channels. These channels, most likely, are composed of other proteins in addition to TRP4. In the present paper we report the direct interaction of TRP4 and calmodulin (CaM) by: (1) retention of in vitro translated TRP4 and of TRP4 protein solubilized from bovine adrenal cortex by CaM-Sepharose in the presence of Ca(2+), and (2) TRP4-glutathione S-transferase pull-down experiments. Two domains of TRP4, amino acid residues 688-759 and 786-848, were identified as being able to interact with CaM. The binding of CaM to both domains occurred only in the presence of Ca(2+) concentrations above 10 microM, with half maximal binding occurring at 16.6 microM (domain 1) and 27.9 microM Ca(2+) (domain 2). Synthetic peptides, encompassing the two putative CaM binding sites within these domains and covering amino acid residues 694-728 and 829-853, interacted directly with dansyl-CaM with apparent K(d) values of 94-189 nM. These results indicate that TRP4/Ca(2+)-CaM are parts of a signalling complex involved in agonist-induced Ca(2+) entry.
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