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Transient receptor potential cation channel, subfamily C, member 4
This gene encodes a member of the canonical subfamily of transient receptor potential cation channels. The encoded protein forms a non-selective calcium-permeable cation channel that is activated by Gq-coupled receptors and tyrosine kinases, and plays a role in multiple processes including endothelial permeability, vasodilation, neurotransmitter release and cell proliferation. Single nucleotide polymorphisms in this gene may be associated with generalized epilepsy with photosensitivity. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Aug 2011] (from
Zhu et al., Homburg, Germany. In Proc Natl Acad Sci U S A, Feb 2016
Although TRPC3/C6/C7 can be directly activated by diacylglycerols produced by PLC breakdown of phosphatidylinositol 4,5-bisphosphate (PIP2), the mechanism by which the PLC pathway activates TRPC4/C5 remains unclear.
Renaud et al., Ottawa, Canada. In Neuroscience, Jan 2016
Collectively, the data imply that activation of TRH receptors in these midline thalamic neurons engages novel signaling pathways that include postsynaptic intracellular CB1 and CB2 receptors in the activation of TRPC4/5-like channels.
Yin et al., Nantong, China. In Mol Cell Biochem, Nov 2015
EP2 deficiency in these MCs augmented the coupling of TGF-β1 to ER stress-associated proteins [chaperone glucose-regulated protein 78 (GRP78), transient receptor potential channel 1 (TRPC1), and transient receptor potential channel 4 (TRPC4)], and upregulation of EP2 showed no significant change of GRP78, but augmented the expression of TRPC1, while TRPC4 expression was downregulated in comparison to normal MCs.
Such store-operated Ca2+ entry comprises organization of a Ca2+ signal complex at the local subplasmalemmal domain involving TRPC4, caveolin1, and STIM1, a Ca2+ sensor protein for intracellular Ca2+ stores.
Zhu et al., Hefei, China. In Sci China Life Sci, 2015
Canonical transient receptor potential 4 (TRPC4) forms non-selective cation channels that contribute to phospholipase C-dependent Ca(2+) entry into cells following stimulation of G protein coupled receptors and receptor tyrosine kinases.
Stevens et al., Mobile, United States. In Circ Res, 2012
Orai1 interacts with TRPC4 in the endogenous channel complex, where it controls TRPC1/4 activation and channel permeation characteristics, including calcium selectivity, important for control of endothelial cell barrier function.
Egger et al., Homburg, Germany. In J Neurosci, 2012
This study concluded that TRPC4 can be activated downstream of NMDA receptor activation and contribute to slow synaptic transmission in the olfactory bulb, including the calcium dynamics required for asynchronous release from the granule cell spine.
Zheng et al., Little Rock, United States. In Mol Pharmacol, 2012
report that the large depolarizing plateau potential that underlies the epileptiform burst firing induced by metabotropic glutamate receptor agonists in lateral septal neurons was completely abolished in TRPC1/4 double-knockout mice