Biology:TRPC5

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Short transient receptor potential channel 5 (TrpC5) also known as transient receptor protein 5 (TRP-5) is a protein that in humans is encoded by the TRPC5 gene.[1][2][3] TrpC5 is subtype of the TRPC family of mammalian transient receptor potential ion channels.

Function

TrpC5 is one of the seven mammalian TRPC (transient receptor potential canonical) proteins. TrpC5 is a multi-pass membrane protein and is thought to form a receptor-activated non-selective calcium permeant cation channel. The protein is active alone or as a heteromultimeric assembly with TRPC1, TRPC3, and TRPC4. It also interacts with multiple proteins including calmodulin, CABP1, enkurin, Na+–H+ exchange regulatory factor (NHERF), interferon-induced GTP-binding protein (MX1), ring finger protein 24 (RNF24), and SEC14 domain and spectrin repeat-containing protein 1 (SESTD1).[1]

TRPC4 and TRPC5 have been implicated in the mechanism of mercury toxicity[4] and neurological behavior.[5] It was established in 2021 that TRPC5 is a component of the dental cold sensing system.[6]

Activation

Homomultimeric TRPC5 and heteromultimeric TRPC5-TRPC1 channels are activated by extracellular reduced thioredoxin.[7] This channel has also been found to be involved in the action of anaesthetics such as chloroform, halothane and propofol.[8]

Interactions

TRPC5 has been shown to interact with STMN3,[9] TRPC1,[10][11] and TRPC4.[11]

See also

References

  1. 1.0 1.1 "Entrez Gene: transient receptor potential cation channel". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7224. 
  2. "Molecular cloning and characterization of TRPC5 (HTRP5), the human homologue of a mouse brain receptor-activated capacitative Ca2+ entry channel". Genomics 60 (3): 330–40. September 1999. doi:10.1006/geno.1999.5924. PMID 10493832. 
  3. "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. December 2005. doi:10.1124/pr.57.4.6. PMID 16382100. 
  4. "Activation of TRPC cationic channels by mercurial compounds confers the cytotoxicity of mercury exposure". Toxicol. Sci. 125 (1): 56–68. January 2012. doi:10.1093/toxsci/kfr268. PMID 21984481. 
  5. "Essential role for TRPC5 in amygdala function and fear-related behavior". Cell 137 (4): 761–72. May 15, 2009. doi:10.1016/j.cell.2009.03.039. PMID 19450521. 
  6. Bernal, Laura; Sotelo-Hitschfeld, Pamela; König, Christine; Sinica, Viktor; Wyatt, Amanda; Winter, Zoltan; Hein, Alexander; Touska, Filip et al. (2021). "Odontoblast TRPC5 channels signal cold pain in teeth". Science Advances 7 (13): eabf5567. doi:10.1126/sciadv.abf5567. PMID 33771873. 
  7. "TRPC channel activation by extracellular thioredoxin". Nature 451 (7174): 69–72. January 2008. doi:10.1038/nature06414. PMID 18172497. 
  8. "Modulation of TRPC5 cation channels by halothane, chloroform and propofol". Br. J. Pharmacol. 153 (7): 1505–12. April 2008. doi:10.1038/sj.bjp.0707689. PMID 18204473. 
  9. "TRPC5 is a regulator of hippocampal neurite length and growth cone morphology". Nat. Neurosci. 6 (8): 837–45. August 2003. doi:10.1038/nn1092. PMID 12858178. 
  10. "Formation of novel TRPC channels by complex subunit interactions in embryonic brain". J. Biol. Chem. 278 (40): 39014–9. October 2003. doi:10.1074/jbc.M306705200. PMID 12857742. 
  11. 11.0 11.1 "Subunit composition of mammalian transient receptor potential channels in living cells". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7461–6. May 2002. doi:10.1073/pnas.102596199. PMID 12032305. Bibcode2002PNAS...99.7461H. 

Further reading

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.