Short transient receptor potential channel 4 (TRPC4), also known as Trp-related protein 4, is encoded by the TRPC4 gene. TRPC4 belongs to the canonical subfamily of transient receptor potential cation channels. Mutation in this gene may be involved in generalized epilepsy with photosensitivity. TRPC4 contains 6 transmembrane regions, a pore region, a caveolin-binding domain and a PDZ domain binding region at the C terminus. TRPC4 is widely expressed in heart, pancreas, placenta, brain, and kidney, especially in the cortico-limbic regions of the brain with high abundance. In addition, TRPC4 is also present in midbrain dopaminergic neurons in the ventral tegmental area and the substantia nigra.
|Basic Information of TRPC4|
|Protein Name||Short transient receptor potential channel 4|
|Aliases||Trp-related protein 4|
|Organism||Homo sapiens (Human)|
TRPC4 can form a nonspecific calcium-permeable cation channel that may play a role in many biological processes including vasodilation, endothelial permeability, gamma-aminobutyric acid secretion, oligodendrocyte differentiation, regulation of cytosolic calcium ion concentration, cell proliferation and neurotransmitter release. It is possibly controlled by a phosphatidylinositol second messenger system activated by Gαi-coupled receptors, Gαq-coupled receptors and tyrosine kinases. For another, it may also be activated by depletion of intracellular calcium. As an ion channel, it has an enhanced permeability to barium over calcium, and its translocation to the plasma membrane is associated with the interaction with spectrin. There is no experiment structure available for human TRPC4, but we can take a zebrafish TRPC4 structure (PDB: 6G1K) from the reference (Fig.1).
Fig.1 Electron cryo-microscopy structure of the canonical TRPC4 ion channel. (Vinayagam, 2018)
This article confirms the existence of harmful reaction to Englerin A in mice, suggesting that it depends on a combination of TRPC4 and TRPC5 which therefore overlaps partially with TRPC4-dependent cancer cell cytotoxicity.
This article suggests that ML204, a potent TRPC4 channel blocker, might exhibit antagonistic actions on M₂ and M₃ muscarinic receptors. Additionally, the inhibitory effects of ML204 against electrical field stimulation-induced cholinergic contractions might be ascribed to this receptor antagonism rather than the suppression of TRPC4 channel activity.
This article demonstrates that TRPC4 channels are associated with cholinergic-mediated and spontaneous contractions of the murine detrusor. Additionally, expression of TRPC5 is up-regulated in TRPC4-/- detrusor strips, suggesting TRPC5 may to some extent compensate for the lack of TRPC4 channels.
This article reports the electron cryo-microscopy structure of zebrafish TRPC4 in its apo, closed state at an overall resolution of 3.6 Å.
This article demonstrates that TRPC4-TRPC6 hetero-multimerization linked depletion of Ca2+ store and STIM1 accumulation with Na+/Ca2+ exchange reversal in proliferative vascular smooth muscle cells.
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