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== Structure of TRPV1 ==
== Structure of TRPV1 ==
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The TRPV1 receptor is a transmembrane protein receptor. It is made up of '''839 amino acids'''. It’s molecular weight is '''94 938Da'''.<ref>« Structure of the TRPV1 ion channel determined by electron cryo-microscopy | Nature ». https://www.nature.com/articles/nature12822#Fig3 (consulté le déc. 28, 2020)</ref>. TRPV1 exists in two states : the open state and the closed state.<ref> T. Rosenbaum et S. A. Simon, « TRPV1 Receptors and Signal Transduction », in TRP Ion Channel Function in Sensory Transduction and Cellular Signaling Cascades, W. B. Liedtke et S. Heller, Éd. Boca Raton (FL): CRC Press/Taylor & Francis, 2007</ref>
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The TRPV1 receptor is a transmembrane protein receptor. It is made up of '''839 amino acids'''. It’s molecular weight is '''94 938Da'''.<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy">Liao, M., Cao, E., Julius, D., & Cheng, Y. (2013b). Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature, 504(7478), 107‑112. https://doi.org/10.1038/nature12822(consulté le déc. 28, 2020)</ref> TRPV1 exists in two states : the open state and the closed state.<ref> T. Rosenbaum et S. A. Simon, « TRPV1 Receptors and Signal Transduction », in TRP Ion Channel Function in Sensory Transduction and Cellular Signaling Cascades, W. B. Liedtke et S. Heller, Éd. Boca Raton (FL): CRC Press/Taylor & Francis, 2007</ref>
TRPV1 are '''tetrameric''' channel type receptors. The four subunits from a symmetry plane around a pore allowing the passage of ions.
TRPV1 are '''tetrameric''' channel type receptors. The four subunits from a symmetry plane around a pore allowing the passage of ions.
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Each TRPV1 subunits are made of one '''N-terminal tail''', one '''transmembrane region''', a'' C-terminal tail'' preceded by a '''TRP domain'''. The N-terminal and C-terminal region are intracellular. N and C terminal region are responsible of 70% of the total mass of TRPV1.<ref>« Structure of the TRPV1 ion channel determined by electron cryo-microscopy | Nature ». https://www.nature.com/articles/nature12822#Fig3 (consulté le déc. 28, 2020)</ref>
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Each TRPV1 subunits are made of one '''N-terminal tail''', one '''transmembrane region''', a'' C-terminal tail'' preceded by a '''TRP domain'''. The N-terminal and C-terminal region are intracellular. N and C terminal region are responsible of 70% of the total mass of TRPV1.<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/>
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The N-terminal region has 6 repeats of [https://en.wikipedia.org/wiki/Ankyrin ankyrin].<ref>« Structure of the TRPV1 ion channel determined by electron cryo-microscopy | Nature ».https://www.nature.com/articles/nature12822#Fig3 (consulté le déc. 28, 2020)</ref><ref>G. Smutzer et R. K. Devassy, « Integrating TRPV1 Receptor Function with Capsaicin Psychophysics », Advances in Pharmacological Sciences, janv. 14, 2016</ref>
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The N-terminal region has 6 repeats of [https://en.wikipedia.org/wiki/Ankyrin ankyrin].<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/><ref name="Integrating TRPV1 Receptor Function with Capsaicin Psychophysics">G. Smutzer et R. K. Devassy, « Integrating TRPV1 Receptor Function with Capsaicin Psychophysics », Advances in Pharmacological Sciences, janv. 14, 2016</ref>
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The transmembrane region is composed of '''six transmembrane a helices''' (S1-S6). S1,S2 and S3 helices contain aromatic side chain (S1 : Y441,Y444,Y555 S2: F488 S3 : F516).<ref>« Structure of the TRPV1 ion channel determined by electron cryo-microscopy | Nature ». https://www.nature.com/articles/nature12822#Fig3 (consulté le déc. 28, 2020)</ref>. A small hydrophobic domain beetween S5 and S6 with a re-entrant loop constitutes the pore allowing the passage of ions through the TRPV1 receptor.<ref name="TRPV1"/>
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The transmembrane region is composed of '''six transmembrane a helices''' (S1-S6). S1,S2 and S3 helices contain aromatic side chain (S1 : Y441,Y444,Y555 S2: F488 S3 : F516).<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> A small hydrophobic domain beetween S5 and S6 with a re-entrant loop constitutes the pore allowing the passage of ions through the TRPV1 receptor.<ref name="TRPV1"/><ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/>
'''Threonin''' residu (T550) and '''tyrosin''' residu (Y511) located on the fifth and the third transmembrane helices are very conserved. Threonin 550 and tyrosin 511 are implicated in TRPV1 activation by [https://en.wikipedia.org/wiki/Vanilloids vanilloids] and in pain sensation.<ref>R. Kumar, A. Hazan, A. Basu, N. Zalcman, H. Matzner, et A. Priel, « Tyrosine Residue in the TRPV1 Vanilloid Binding Pocket Regulates Deactivation Kinetics », J. Biol. Chem., vol. 291, no 26, p. 13855‑13863, juin 2016, doi: 10.1074/jbc.M116.726372.</ref>
'''Threonin''' residu (T550) and '''tyrosin''' residu (Y511) located on the fifth and the third transmembrane helices are very conserved. Threonin 550 and tyrosin 511 are implicated in TRPV1 activation by [https://en.wikipedia.org/wiki/Vanilloids vanilloids] and in pain sensation.<ref>R. Kumar, A. Hazan, A. Basu, N. Zalcman, H. Matzner, et A. Priel, « Tyrosine Residue in the TRPV1 Vanilloid Binding Pocket Regulates Deactivation Kinetics », J. Biol. Chem., vol. 291, no 26, p. 13855‑13863, juin 2016, doi: 10.1074/jbc.M116.726372.</ref>
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The S6 domain links the receptor to the C-terminal domain of TRPV1. The C-terminal is made of 150 amino acids and it contains '''TRP domain'''.<ref>G. Smutzer et R. K. Devassy, « Integrating TRPV1 Receptor Function with Capsaicin Psychophysics », Advances in Pharmacological Sciences, janv. 14, 2016.</ref>.The TRP domain is made of 23-25 aminoacids with a alpha helical structure, it is found in many TRP family members.<ref>« Structure of the TRPV1 ion channel determined by electron cryo-microscopy | Nature ». https://www.nature.com/articles/nature12822#Fig3 (consulté le déc. 28, 2020)</ref>.TRP domain is necessary for the formation of tetrameric TRPV1.
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The S6 domain links the receptor to the C-terminal domain of TRPV1. The C-terminal is made of 150 amino acids and it contains '''TRP domain'''.<ref name="Integrating TRPV1 Receptor Function with Capsaicin Psychophysics"/>.The TRP domain is made of 23-25 aminoacids with a alpha helical structure, it is found in many TRP family members.<ref name="Structure of the TRPV1 ion channel determined by electron cryo-microscopy"/> TRP domain is necessary for the formation of tetrameric TRPV1.
Many amino-acids of the C-terminal domain are the target of post-translationnal modifications by [https://en.wikipedia.org/wiki/Kinase kinases] and [https://en.wikipedia.org/wiki/Phosphatase phosphatases].<ref>X. Yao, H.-Y. Kwan, et Y. Huang, « Regulation of TRP Channels by Phosphorylation », Neurosignals, vol. 14, no 6, p. 273‑280, 2005, doi: 10.1159/000093042</ref>
Many amino-acids of the C-terminal domain are the target of post-translationnal modifications by [https://en.wikipedia.org/wiki/Kinase kinases] and [https://en.wikipedia.org/wiki/Phosphatase phosphatases].<ref>X. Yao, H.-Y. Kwan, et Y. Huang, « Regulation of TRP Channels by Phosphorylation », Neurosignals, vol. 14, no 6, p. 273‑280, 2005, doi: 10.1159/000093042</ref>

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The Transient Receptor Potential cation channel subfamily V member 1 TRPV1

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References

  1. ↑ 1.0 1.1 1.2 Wikipedia contributors. (2020b, décembre 21). TRPV1. Wikipedia. https://en.wikipedia.org/wiki/TRPV1 (Consulté le: déc. 28, 2020). [En ligne].
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 Liao, M., Cao, E., Julius, D., & Cheng, Y. (2013b). Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature, 504(7478), 107‑112. https://doi.org/10.1038/nature12822(consulté le déc. 28, 2020)
  3. ↑ T. Rosenbaum et S. A. Simon, « TRPV1 Receptors and Signal Transduction », in TRP Ion Channel Function in Sensory Transduction and Cellular Signaling Cascades, W. B. Liedtke et S. Heller, Éd. Boca Raton (FL): CRC Press/Taylor & Francis, 2007
  4. ↑ 4.0 4.1 G. Smutzer et R. K. Devassy, « Integrating TRPV1 Receptor Function with Capsaicin Psychophysics », Advances in Pharmacological Sciences, janv. 14, 2016
  5. ↑ R. Kumar, A. Hazan, A. Basu, N. Zalcman, H. Matzner, et A. Priel, « Tyrosine Residue in the TRPV1 Vanilloid Binding Pocket Regulates Deactivation Kinetics », J. Biol. Chem., vol. 291, no 26, p. 13855‑13863, juin 2016, doi: 10.1074/jbc.M116.726372.
  6. ↑ X. Yao, H.-Y. Kwan, et Y. Huang, « Regulation of TRP Channels by Phosphorylation », Neurosignals, vol. 14, no 6, p. 273‑280, 2005, doi: 10.1159/000093042
  7. ↑ F. Yang et J. Zheng, « Understand spiciness: mechanism of TRPV1 channel activation by capsaicin », Protein Cell, vol. 8, no 3, p. 169‑177, mars 2017, doi: 10.1007/s13238-016-0353-7.
  8. ↑ F. Yang et al., « Structural mechanism underlying capsaicin binding and activation of the TRPV1 ion channel », Nat. Chem. Biol., vol. 11, no 7, Art. no 7, juill. 2015, doi: 10.1038/nchembio.1835.
  9. ↑ G. Smutzer et R. K. Devassy, « Integrating TRPV1 Receptor Function with Capsaicin Psychophysics », Advances in Pharmacological Sciences, janv. 14, 2016.
  10. ↑ F. Yang et al., « The conformational wave in capsaicin activation of transient receptor potential vanilloid 1 ion channel », Nat. Commun., vol. 9, no 1, Art. no 1, juill. 2018, doi: 10.1038/s41467-018-05339-6.
  11. ↑ K. Elokely et al., « Understanding TRPV1 activation by ligands: Insights from the binding modes of capsaicin and resiniferatoxin », Proc. Natl. Acad. Sci., vol. 113, no 2, p. E137‑E145, janv. 2016, doi:10.1073/pnas.1517288113.
  12. ↑ K. W. Ho, N. J. Ward, et D. J. Calkins, « TRPV1: a stress response protein in the central nervous system », Am. J. Neurodegener. Dis., vol. 1, no 1, p. 1‑14, avr. 2012.
  13. ↑ G. Smutzer et R. K. Devassy, « Integrating TRPV1 Receptor Function with Capsaicin Psychophysics », Advances in Pharmacological Sciences, janv. 14, 2016.
  14. ↑ K. W. Ho, N. J. Ward, et D. J. Calkins, « TRPV1: a stress response protein in the central nervous system », Am. J. Neurodegener. Dis., vol. 1, no 1, p. 1‑14, avr. 2012.
  15. ↑ G. Bhave et al., « Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1) », Proc. Natl. Acad. Sci., vol. 100, no 21, p. 12480‑12485, oct. 2003, doi: 10.1073/pnas.2032100100.
  16. ↑ A. Danigo, L. Magy, et C. Demiot, « TRPV1 dans les neuropathies douloureuses - Des modèles animaux aux perspectives thérapeutiques », médecine/sciences, vol. 29, no 6‑7, Art. no 6‑7, juin 2013, doi: 10.1051/medsci/2013296012.
  17. ↑ A. Danigo, L. Magy, et C. Demiot, « TRPV1 dans les neuropathies douloureuses - Des modèles animaux aux perspectives thérapeutiques », médecine/sciences, vol. 29, no 6‑7, Art. no 6‑7, juin 2013, doi: 10.1051/medsci/2013296012.
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