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The <scene name='86/868186/Ion_conducting_pore/1'>central pore axis</scene> of piezo1 is lined with the <scene name='86/868186/Ced/1'>extracellular cap domain</scene>, inner helix and cytosolic <scene name='86/868186/Ctd/1'>CTD</scene>. The extracellular cations can approach the pore entry “vertically through the internal cavity along the threefold axis of the cap domain”, they can also approach laterally through spaces (gaps) between the flexible linkers which connect the cap with inner and outer helices.<ref name= "ion channel"> DOI 10.1038/nature25453</ref> The <scene name='86/868186/Ion_conducting_pore/1'>ion conduction pathway</scene> is situated below the <scene name='86/868186/Ced/1'>cap</scene>, and is
The <scene name='86/868186/Ion_conducting_pore/1'>central pore axis</scene> of piezo1 is lined with the <scene name='86/868186/Ced/1'>extracellular cap domain</scene>, inner helix and cytosolic <scene name='86/868186/Ctd/1'>CTD</scene>. The extracellular cations can approach the pore entry “vertically through the internal cavity along the threefold axis of the cap domain”, they can also approach laterally through spaces (gaps) between the flexible linkers which connect the cap with inner and outer helices.<ref name= "ion channel"> DOI 10.1038/nature25453</ref> The <scene name='86/868186/Ion_conducting_pore/1'>ion conduction pathway</scene> is situated below the <scene name='86/868186/Ced/1'>cap</scene>, and is
lined by the three inner transmembrane helices. The possible access for lipids or other hydrophobic molecules through the pore could be “two lateral openings between the inner helices separated by a ‘seal’ formed by K2479 and F2480”. These openings are approximately 11 Å wide and 16 Å tall. <ref name= "ion channel">
lined by the three inner transmembrane helices. The possible access for lipids or other hydrophobic molecules through the pore could be “two lateral openings between the inner helices separated by a ‘seal’ formed by K2479 and F2480”. These openings are approximately 11 Å wide and 16 Å tall. <ref name= "ion channel">
 +
==='''CTD and Beam'''===
==='''CTD and Beam'''===

Revision as of 08:00, 10 January 2021

Piezo 1

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References

  1. 1.0 1.1 1.2 Zhao Q, Wu K, Geng J, Chi S, Wang Y, Zhi P, Zhang M, Xiao B. Ion Permeation and Mechanotransduction Mechanisms of Mechanosensitive Piezo Channels. Neuron. 2016 Mar 16;89(6):1248-1263. doi: 10.1016/j.neuron.2016.01.046. Epub 2016, Feb 25. PMID:26924440 doi:http://dx.doi.org/10.1016/j.neuron.2016.01.046
  2. 2.0 2.1 Parpaite T, Coste B. Piezo channels. Curr Biol. 2017 Apr 3;27(7):R250-R252. doi: 10.1016/j.cub.2017.01.048. PMID:28376327 doi:http://dx.doi.org/10.1016/j.cub.2017.01.048
  3. 3.0 3.1 Wei L, Mousawi F, Li D, Roger S, Li J, Yang X, Jiang LH. Adenosine Triphosphate Release and P2 Receptor Signaling in Piezo1 Channel-Dependent Mechanoregulation. Front Pharmacol. 2019 Nov 6;10:1304. doi: 10.3389/fphar.2019.01304. eCollection, 2019. PMID:31780935 doi:http://dx.doi.org/10.3389/fphar.2019.01304
  4. Lin YC, Guo YR, Miyagi A, Levring J, MacKinnon R, Scheuring S. Force-induced conformational changes in PIEZO1. Nature. 2019 Sep;573(7773):230-234. doi: 10.1038/s41586-019-1499-2. Epub 2019 Aug, 21. PMID:31435018 doi:http://dx.doi.org/10.1038/s41586-019-1499-2
  5. Li J, Hou B, Tumova S, Muraki K, Bruns A, Ludlow MJ, Sedo A, Hyman AJ, McKeown L, Young RS, Yuldasheva NY, Majeed Y, Wilson LA, Rode B, Bailey MA, Kim HR, Fu Z, Carter DA, Bilton J, Imrie H, Ajuh P, Dear TN, Cubbon RM, Kearney MT, Prasad KR, Evans PC, Ainscough JF, Beech DJ. Piezo1 integration of vascular architecture with physiological force. Nature. 2014 Nov 13;515(7526):279-82. doi: 10.1038/nature13701. Epub 2014 Aug 10. PMID:25119035 doi:http://dx.doi.org/10.1038/nature13701
  6. 6.0 6.1 Zhou, Z. (2019). Structural Analysis of Piezo1 Ion Channel Reveals the Relationship between Amino Acid Sequence Mutations and Human Diseases. 139–155. DOI 10.4236/jbm.2019.712012
  7. Zhao Q, Zhou H, Chi S, Wang Y, Wang J, Geng J, Wu K, Liu W, Zhang T, Dong MQ, Wang J, Li X, Xiao B. Structure and mechanogating mechanism of the Piezo1 channel. Nature. 2018 Feb 22;554(7693):487-492. doi: 10.1038/nature25743. Epub 2018 Jan, 22. PMID:29469092 doi:http://dx.doi.org/10.1038/nature25743
  8. 8.0 8.1 8.2 8.3 Liang X, Howard J. Structural Biology: Piezo Senses Tension through Curvature. Curr Biol. 2018 Apr 23;28(8):R357-R359. doi: 10.1016/j.cub.2018.02.078. PMID:29689211 doi:http://dx.doi.org/10.1016/j.cub.2018.02.078
  9. Guo YR, MacKinnon R. Structure-based membrane dome mechanism for Piezo mechanosensitivity. Elife. 2017 Dec 12;6. pii: 33660. doi: 10.7554/eLife.33660. PMID:29231809 doi:http://dx.doi.org/10.7554/eLife.33660
  10. Guo YR, MacKinnon R. Structure-based membrane dome mechanism for Piezo mechanosensitivity. Elife. 2017 Dec 12;6. pii: 33660. doi: 10.7554/eLife.33660. PMID:29231809 doi:http://dx.doi.org/10.7554/eLife.33660
  11. Lin YC, Guo YR, Miyagi A, Levring J, MacKinnon R, Scheuring S. Force-induced conformational changes in PIEZO1. Nature. 2019 Sep;573(7773):230-234. doi: 10.1038/s41586-019-1499-2. Epub 2019 Aug, 21. PMID:31435018 doi:http://dx.doi.org/10.1038/s41586-019-1499-2
  12. 12.0 12.1 Saotome K, Murthy SE, Kefauver JM, Whitwam T, Patapoutian A, Ward AB. Structure of the mechanically activated ion channel Piezo1. Nature. 2017 Dec 20. pii: nature25453. doi: 10.1038/nature25453. PMID:29261642 doi:http://dx.doi.org/10.1038/nature25453
  13. Ge J, Li W, Zhao Q, Li N, Chen M, Zhi P, Li R, Gao N, Xiao B, Yang M. Architecture of the mammalian mechanosensitive Piezo1 channel. Nature. 2015 Nov 5;527(7576):64-9. doi: 10.1038/nature15247. Epub 2015 Sep 21. PMID:26390154 doi:http://dx.doi.org/10.1038/nature15247
  14. Cite error: Invalid <ref> tag; no text was provided for refs named mechanogating
  15. doi: https://dx.doi.org/10.4236/jbm.2019.712012
  16. Ge J, Li W, Zhao Q, Li N, Chen M, Zhi P, Li R, Gao N, Xiao B, Yang M. Architecture of the mammalian mechanosensitive Piezo1 channel. Nature. 2015 Nov 5;527(7576):64-9. doi: 10.1038/nature15247. Epub 2015 Sep 21. PMID:26390154 doi:http://dx.doi.org/10.1038/nature15247
  17. 17.0 17.1 Albuisson J, Murthy SE, Bandell M, Coste B, Louis-Dit-Picard H, Mathur J, Feneant-Thibault M, Tertian G, de Jaureguiberry JP, Syfuss PY, Cahalan S, Garcon L, Toutain F, Simon Rohrlich P, Delaunay J, Picard V, Jeunemaitre X, Patapoutian A. Dehydrated hereditary stomatocytosis linked to gain-of-function mutations in mechanically activated PIEZO1 ion channels. Nat Commun. 2013;4:1884. doi: 10.1038/ncomms2899. PMID:23695678 doi:http://dx.doi.org/10.1038/ncomms2899
  18. Andolfo I, Alper SL, De Franceschi L, Auriemma C, Russo R, De Falco L, Vallefuoco F, Esposito MR, Vandorpe DH, Shmukler BE, Narayan R, Montanaro D, D'Armiento M, Vetro A, Limongelli I, Zuffardi O, Glader BE, Schrier SL, Brugnara C, Stewart GW, Delaunay J, Iolascon A. Multiple clinical forms of dehydrated hereditary stomatocytosis arise from mutations in PIEZO1. Blood. 2013 May 9;121(19):3925-35, S1-12. doi: 10.1182/blood-2013-02-482489. Epub, 2013 Mar 11. PMID:23479567 doi:http://dx.doi.org/10.1182/blood-2013-02-482489
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