TRPC5

Last updated
TRPC5
Identifiers
Aliases TRPC5 , PPP1R159, TRP5, transient receptor potential cation channel subfamily C member 5
External IDs OMIM: 300334 MGI: 109524 HomoloGene: 74915 GeneCards: TRPC5
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012471

NM_009428

RefSeq (protein)

NP_036603

NP_033454

Location (UCSC) Chr X: 111.77 – 112.08 Mb Chr X: 143.16 – 143.47 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

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. [5] [6] [7] TrpC5 is subtype of the TRPC family of mammalian transient receptor potential ion channels.

Contents

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). [5]

TRPC4 and TRPC5 have been implicated in the mechanism of mercury toxicity [8] and neurological behavior. [9] It was established in 2021 that TRPC5 is a component of the dental cold sensing system. [10]

Activation

Homomultimeric TRPC5 and heteromultimeric TRPC5-TRPC1 channels are activated by extracellular reduced thioredoxin. [11] This channel has also been found to be involved in the action of anaesthetics such as chloroform, halothane and propofol. [12]

Interactions

TRPC5 has been shown to interact with STMN3, [13] TRPC1, [14] [15] and TRPC4. [15]

See also

Related Research Articles

Transient receptor potential channels are a group of ion channels located mostly on the plasma membrane of numerous animal cell types. Most of these are grouped into two broad groups: Group 1 includes TRPC, TRPV, TRPVL, TRPM, TRPS, TRPN, and TRPA. Group 2 consists of TRPP and TRPML. Other less-well categorized TRP channels exist, including yeast channels and a number of Group 1 and Group 2 channels present in non-animals. Many of these channels mediate a variety of sensations such as pain, temperature, different kinds of tastes, pressure, and vision. In the body, some TRP channels are thought to behave like microscopic thermometers and used in animals to sense hot or cold. Some TRP channels are activated by molecules found in spices like garlic (allicin), chili pepper (capsaicin), wasabi ; others are activated by menthol, camphor, peppermint, and cooling agents; yet others are activated by molecules found in cannabis or stevia. Some act as sensors of osmotic pressure, volume, stretch, and vibration. Most of the channels are activated or inhibited by signaling lipids and contribute to a family of lipid-gated ion channels.

TRPC is a family of transient receptor potential cation channels in animals.

<span class="mw-page-title-main">TRPV</span> Subgroup of TRP cation channels named after the vanilloid receptor

TRPV is a family of transient receptor potential cation channels in animals. All TRPVs are highly calcium selective.

TRPM is a family of transient receptor potential ion channels (M standing for wikt:melastatin). Functional TRPM channels are believed to form tetramers. The TRPM family consists of eight different channels, TRPM1–TRPM8.

<span class="mw-page-title-main">MCOLN1</span> Protein-coding gene in the species Homo sapiens

Mucolipin-1 also known as TRPML1 is a protein that in humans is encoded by the MCOLN1 gene. It is a member of the small family of the TRPML channels, a subgroup of the large protein family of TRP ion channels.

<span class="mw-page-title-main">TRPC6</span> Protein and coding gene in humans

Transient receptor potential cation channel, subfamily C, member 6, also known as TRPC6, is a human gene encoding a protein of the same name. TRPC6 is a transient receptor potential channel of the classical TRPC subfamily. It has been associated with depression and anxiety, as well as with focal segmental glomerulosclerosis (FSGS).

<span class="mw-page-title-main">TRPC1</span> Protein and coding gene in humans

Transient receptor potential canonical 1 (TRPC1) is a protein that in humans is encoded by the TRPC1 gene.

<span class="mw-page-title-main">TRPC2</span> Pseudogene in the species Homo sapiens

Transient receptor potential cation channel, subfamily C, member 2, also known as TRPC2, is a protein that in humans is encoded by the TRPC2 pseudogene. This protein is not expressed in humans but is in certain other species such as mouse.

<span class="mw-page-title-main">TRPC3</span> Protein and coding gene in humans

Short transient receptor potential channel 3 (TrpC3) also known as transient receptor protein 3 (TRP-3) is a protein that in humans is encoded by the TRPC3 gene. The TRPC3/6/7 subfamily are implicated in the regulation of vascular tone, cell growth, proliferation and pathological hypertrophy. These are diacylglycerol-sensitive cation channels known to regulate intracellular calcium via activation of the phospholipase C (PLC) pathway and/or by sensing Ca2+ store depletion. Together, their role in calcium homeostasis has made them potential therapeutic targets for a variety of central and peripheral pathologies.

<span class="mw-page-title-main">TRPC4</span> Protein and coding gene in humans

The short transient receptor potential channel 4 (TrpC4), also known as Trp-related protein 4, is a protein that in humans is encoded by the TRPC4 gene.

<span class="mw-page-title-main">TRPM5</span> Protein-coding gene in the species Homo sapiens

Transient receptor potential cation channel subfamily M member 5 (TRPM5), also known as long transient receptor potential channel 5 is a protein that in humans is encoded by the TRPM5 gene.

<span class="mw-page-title-main">TRPM4</span> Protein-coding gene in the species Homo sapiens

Transient receptor potential cation channel subfamily M member 4 (hTRPM4), also known as melastatin-4, is a protein that in humans is encoded by the TRPM4 gene.

<span class="mw-page-title-main">TRPC7</span> Protein-coding gene in the species Homo sapiens

Transient receptor potential cation channel, subfamily C, member 7, also known as TRPC7, is a human gene encoding a protein of the same name.

<span class="mw-page-title-main">TRPV4</span> Protein-coding gene in the species Homo sapiens

Transient receptor potential cation channel subfamily V member 4 is an ion channel protein that in humans is encoded by the TRPV4 gene.

<span class="mw-page-title-main">TRPM8</span> Protein-coding gene in the species Homo sapiens

Transient receptor potential cation channel subfamily M (melastatin) member 8 (TRPM8), also known as the cold and menthol receptor 1 (CMR1), is a protein that in humans is encoded by the TRPM8 gene. The TRPM8 channel is the primary molecular transducer of cold somatosensation in humans. In addition, mints can desensitize a region through the activation of TRPM8 receptors.

<span class="mw-page-title-main">TRPM3</span> Protein-coding gene in the species Homo sapiens

Transient receptor potential cation channel subfamily M member 3 is a protein that in humans is encoded by the TRPM3 gene.

<span class="mw-page-title-main">TRPM7</span> Protein-coding gene in the species Homo sapiens

Transient receptor potential cation channel, subfamily M, member 7, also known as TRPM7, is a human gene encoding a protein of the same name.

<span class="mw-page-title-main">Enkurin</span> Protein-coding gene in the species Homo sapiens

Enkurin is a protein that in humans is encoded by the ENKUR gene.

<span class="mw-page-title-main">RNF24</span> Protein-coding gene in the species Homo sapiens

Ring finger protein 24 is a protein that in humans is encoded by the RNF24 gene.

The transient receptor potential Ca2+ channel (TRP-CC) family (TC# 1.A.4) is a member of the voltage-gated ion channel (VIC) superfamily and consists of cation channels conserved from worms to humans. The TRP-CC family also consists of seven subfamilies (TRPC, TRPV, TRPM, TRPN, TRPA, TRPP, and TRPML) based on their amino acid sequence homology:

  1. the canonical or classic TRPs,
  2. the vanilloid receptor TRPs,
  3. the melastatin or long TRPs,
  4. ankyrin (whose only member is the transmembrane protein 1 [TRPA1])
  5. TRPN after the nonmechanoreceptor potential C (nonpC), and the more distant cousins,
  6. the polycystins
  7. and mucolipins.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000072315 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000041710 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. 1 2 "Entrez Gene: transient receptor potential cation channel".
  6. Sossey-Alaoui K, Lyon JA, Jones L, Abidi FE, Hartung AJ, Hane B, Schwartz CE, Stevenson RE, Srivastava AK (September 1999). "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. doi:10.1006/geno.1999.5924. PMID   10493832.
  7. Clapham DE, Julius D, Montell C, Schultz G (December 2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. doi:10.1124/pr.57.4.6. PMID   16382100. S2CID   17936350.
  8. Xu SZ, Zeng B, Daskoulidou N, Chen GL, Atkin SL, Lukhele B (January 2012). "Activation of TRPC cationic channels by mercurial compounds confers the cytotoxicity of mercury exposure". Toxicol. Sci. 125 (1): 56–68. doi: 10.1093/toxsci/kfr268 . PMID   21984481.
  9. Riccio A, Li Y, Moon J, Kim KS, Smith KS, Rudolph U, Gapon S, Yao GL, Tsvetkov E, Rodig SJ, Van't Veer A, Meloni EG, Carlezon WA, Bolshakov VY, Clapham DE (May 15, 2009). "Essential role for TRPC5 in amygdala function and fear-related behavior". Cell. 137 (4): 761–72. doi:10.1016/j.cell.2009.03.039. PMC   2719954 . PMID   19450521.
  10. Bernal, Laura; Sotelo-Hitschfeld, Pamela; König, Christine; Sinica, Viktor; Wyatt, Amanda; Winter, Zoltan; Hein, Alexander; Touska, Filip; Reinhardt, Susanne; Tragl, Aaron; Kusuda, Ricardo; Wartenberg, Philipp; Sclaroff, Allen; Pfeifer, John D.; Ectors, Fabien; Dahl, Andreas; Freichel, Marc; Vlachova, Viktorie; Brauchi, Sebastian; Roza, Carolina; Boehm, Ulrich; Clapham, David E.; Lennerz, Jochen K.; Zimmermann, Katharina (2021). "Odontoblast TRPC5 channels signal cold pain in teeth". Science Advances. 7 (13): eabf5567. doi:10.1126/sciadv.abf5567. PMC   7997515 . PMID   33771873.
  11. Xu SZ, Sukumar P, Zeng F, Li J, Jairaman A, English A, Naylor J, Ciurtin C, Majeed Y, Milligan CJ, Bahnasi YM, Al-Shawaf E, Porter KE, Jiang LH, Emery P, Sivaprasadarao A, Beech DJ (January 2008). "TRPC channel activation by extracellular thioredoxin". Nature. 451 (7174): 69–72. doi:10.1038/nature06414. PMC   2645077 . PMID   18172497.
  12. Bahnasi YM, Wright HM, Milligan CJ, Dedman AM, Zeng F, Hopkins PM, Bateson AN, Beech DJ (April 2008). "Modulation of TRPC5 cation channels by halothane, chloroform and propofol". Br. J. Pharmacol. 153 (7): 1505–12. doi:10.1038/sj.bjp.0707689. PMC   2437913 . PMID   18204473.
  13. Greka A, Navarro B, Oancea E, Duggan A, Clapham DE (August 2003). "TRPC5 is a regulator of hippocampal neurite length and growth cone morphology". Nat. Neurosci. 6 (8): 837–45. doi:10.1038/nn1092. PMID   12858178. S2CID   7523946.
  14. Strübing C, Krapivinsky G, Krapivinsky L, Clapham DE (October 2003). "Formation of novel TRPC channels by complex subunit interactions in embryonic brain". J. Biol. Chem. 278 (40): 39014–9. doi: 10.1074/jbc.M306705200 . PMID   12857742.
  15. 1 2 Hofmann T, Schaefer M, Schultz G, Gudermann T (May 2002). "Subunit composition of mammalian transient receptor potential channels in living cells". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7461–6. doi: 10.1073/pnas.102596199 . PMC   124253 . PMID   12032305.

Further reading

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