ArticleProceedings of the National Academy of Sciences of the United States of America2003
The mouse C-type transient receptor potential 2 (TRPC2) channel: alternative splicing and calmodulin binding to its N terminus.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 65 citations in OpenAlex.
- The Molecular Biology of Placental Transport of Calcium to the Human Foetus.International journal of molecular sciences · 2025Review
- Vascular mechanotransduction.Physiological reviews · 2023Review
- Transient Receptor Potential Channels and Endothelial Cell Calcium Signaling.Comprehensive Physiology · 2019Review
- Review
- Type 3 inositol 1,4,5-trisphosphate receptor is dispensable for sensory activation of the mammalian vomeronasal organ.Scientific reports · 2017Article
- Smooth Muscle Ion Channels and Regulation of Vascular Tone in Resistance Arteries and Arterioles.Comprehensive Physiology · 2017Review
- Transient receptor potential channels in the vasculature.Physiological reviews · 2015Review
- Canonical transient receptor potential channel 2 (TRPC2): old name-new games. Importance in regulating of rat thyroid cell physiology.Pflugers Archiv : European journal of physiology · 2014Review
- Identification of a splice variant of mouse TRPA1 that regulates TRPA1 activity.Nature communications · 2013Article
- Molecular mechanism of TRP channels.Comprehensive Physiology · 2013Review
- Canonical transient receptor potential channel 2 (TRPC2) as a major regulator of calcium homeostasis in rat thyroid FRTL-5 cells: importance of protein kinase C δ (PKCδ) and stromal interaction molecule 2 (STIM2).The Journal of biological chemistry · 2012Article
- Ca2+ -calmodulin feedback mediates sensory adaptation and inhibits pheromone-sensitive ion channels in the vomeronasal organ.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Physiology and pathophysiology of canonical transient receptor potential channels.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2009Review
- Organization and function of TRPC channelosomes.Pflugers Archiv : European journal of physiology · 2007Review
- Orai proteins interact with TRPC channels and confer responsiveness to store depletion.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Neurobiology of TRPC2: from gene to behavior.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
- Mutually exclusive glomerular innervation by two distinct types of olfactory sensory neurons revealed in transgenic zebrafish.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005Article
- Transcriptional regulation and processing increase the functional variability of TRPM channels.Naunyn-Schmiedeberg's archives of pharmacology · 2005Review
- The TRPC2 ion channel and pheromone sensing in the accessory olfactory system.Naunyn-Schmiedeberg's archives of pharmacology · 2005Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Channels of the C-type transient receptor potential (TRPC) are involved in agonist-stimulated and capacitative calcium entry. There are seven TRPCs, all of which have a Ca(2+)-dependent calmodulin (CaM)-binding domain in their C termini. We now tested binding of CaM to TRPC N termini and show that only that of TRPC2 binds CaM in a Ca(2+)-dependent manner. Four TRPC2 cDNAs have been reported: a (also clone 14), b (also clone 17), alpha, and beta. Sequences responsible for CaM binding in TRPC2 a and b are absent from the alpha and beta isoforms. The alpha and beta cDNAs of TRPC2 were reported as alternative forms, when recloning of TRPC2 a and b proved impossible. Here we analyzed total RNA samples from brain and testis for presence of TRPC2 a and b and describe the splicing patterns responsible for their formation, as well as those leading to the alpha and beta forms of TRPC2. We re-assert existence of RNA encoding the TRPC2 a and b, encoded in 21 exons with an initiator ATG in exon 2 for TRPC2a and in exon 4 for TRCP2b. The analysis of alpha and beta TRPC2 cDNAs indicates that although the TRPC2 beta mRNA may exist, the TRPC2 alpha cDNA is derived from an incompletely processed TRPC2a mRNA: It includes in its presumed 5'-untranslated sequence, 713 nt of TRPC2a cDNA fused to 291 nt of an incompletely excised intron. While encoding an active channel in the mouse, the human TRPC2 appears to be a pseudogene. We searched for the human gene in the data bank and located approximately one-half of it in a chromosomal region syntenic to that of the mouse, with similar intron-exon structure. We conclude that the human TRPC2 gene may never have been an active gene because of incomplete ancestral duplication or, if it was complete at one point, that it became inactive upon loss of chromosomal sequences.
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