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== Structure ==
== Structure ==
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==='''[https://en.wikipedia.org/wiki/Gating_(electrophysiology) Gating mechanism]'''===
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==='''Blade'''===
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Piezo 1 has a central domain which is composed of <scene name='86/868186/Cedohihctd/1'>one CTD, one cap (or CED), 3 inner helice (IH) and 3 outer helice (OH).</scene>
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This central domain is surrounded by 3 extended arms called <scene name='86/868186/Blade/1'>blades</scene> extending out from the central pore in a rotatory manner <ref name ="Alexandra"> 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 </ref>.
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Each of these blade, deflecting at an angle of 100° perpendicular to the membrane, contains 6 tandems transmembranar helical unites (THUs) constitute
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of 4 transmembrane domains <ref name= "Article six"> DOI 10.1038/nature25743</ref> <ref name="Alexandra"/>. These blades are not planar: instead, they lie on a spherically curved surface with the membrane bulging into the cytoplasm <ref name= "Piezo Senses Tension "> DOI 10.1016/j.cub.2018.02.078</ref>
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These blades flexibles are inside the membrane and force the membrane to curve. That why, they are considered as mechanotransduction modules, force sensors and transducers to gate the central pore. These 3 blades propeller architecture is mechanically interesting because 3 blades are the minimum
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for omnidirectional sensitivity <ref name="Piezo Senses Tension "/> <ref> DOI 10.7554/eLife.33660 </ref>
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==='''[Gating mechanism]'''===
Piezo 1 possesses delicate force sensing and mechanotransduction mechanisms. Here, we explain how Piezo channels sense and transduce mechanical force
Piezo 1 possesses delicate force sensing and mechanotransduction mechanisms. Here, we explain how Piezo channels sense and transduce mechanical force
to gate the central ion-conducting pore.
to gate the central ion-conducting pore.
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Indeed, mPiezo trimer is non-planar conformation inside lipid bilayer, it produces a local dome-shaped deformation of the membrane. In cells, this membrane curvature project towards the cytoplasm and some electrostatics interactions stabilize the trimeric assembly in its curved conformation.
Indeed, mPiezo trimer is non-planar conformation inside lipid bilayer, it produces a local dome-shaped deformation of the membrane. In cells, this membrane curvature project towards the cytoplasm and some electrostatics interactions stabilize the trimeric assembly in its curved conformation.
<ref name = "nv article"> DOI 10.7554/eLife.33660</ref>
<ref name = "nv article"> DOI 10.7554/eLife.33660</ref>
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The structure of Piezo1 offers a plausible explanation for the origin of its tension gating. Indeed, if the semi-spherical dome becomes flatter when Piezo opens, then the channel membrane system will expand thanks to the flexibility of the blades.
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The structure of Piezo1 offers a plausible explanation for the origin of its tension [https://en.wikipedia.org/wiki/Gating_(electrophysiology)gating]. Indeed, if the semi-spherical dome becomes flatter when Piezo opens, then the channel membrane system will expand thanks to the flexibility of the blades.
However, because flattening does not constrain the pore to open wide, expansion and pore diameter are decoupled such that Piezo can exhibit is small conductance and cation selecticity, properties that are essential to its function.<ref name ="Piezo Senses Tension"/> <ref name="Fanny"> DOI 10.1038/s41586-019-1499-2</ref>
However, because flattening does not constrain the pore to open wide, expansion and pore diameter are decoupled such that Piezo can exhibit is small conductance and cation selecticity, properties that are essential to its function.<ref name ="Piezo Senses Tension"/> <ref name="Fanny"> DOI 10.1038/s41586-019-1499-2</ref>
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The lever-like mechanotransduction apparatus constituted by the beam is possible because of its uneven movement. It displays large motion at the distal beam while subtle movement at the proximal end. It enables Piezo channels to effectively convert a large conformational change of the distal blades to a relatively slight opening of the central pore, allowing cation-selective permeation. The L1342 and L1345 residues of the beam act as a pivot to form the lever-like apparatus.<ref name="mechanogating"/>
The lever-like mechanotransduction apparatus constituted by the beam is possible because of its uneven movement. It displays large motion at the distal beam while subtle movement at the proximal end. It enables Piezo channels to effectively convert a large conformational change of the distal blades to a relatively slight opening of the central pore, allowing cation-selective permeation. The L1342 and L1345 residues of the beam act as a pivot to form the lever-like apparatus.<ref name="mechanogating"/>
-
==='''Blade'''===
 
- 
-
Piezo 1 has a central domain which is composed of <scene name='86/868186/Cedohihctd/1'>one CTD, one cap (or CED), 3 inner helice (IH) and 3 outer helice (OH).</scene>
 
-
This central domain is surrounded by 3 extended arms called <scene name='86/868186/Blade/1'>blades</scene> extending out from the central pore in a rotatory manner <ref name ="Alexandra"> 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 </ref>.
 
-
Each of these blade, deflecting at an angle of 100° perpendicular to the membrane, contains 6 tandems transmembranar helical unites (THUs) constitute
 
-
of 4 transmembrane domains <ref name= "Article six"> DOI 10.1038/nature25743</ref> <ref name="Alexandra"/>. These blades are not planar: instead, they lie on a spherically curved surface with the membrane bulging into the cytoplasm <ref name= "Piezo Senses Tension "> DOI 10.1016/j.cub.2018.02.078</ref>
 
-
These blades flexibles are inside the membrane and force the membrane to curve. That why, they are considered as mechanotransduction modules, force sensors and transducers to gate the central pore. These 3 blades propeller architecture is mechanically interesting because 3 blades are the minimum
 
-
for omnidirectional sensitivity <ref name="Piezo Senses Tension "/> <ref> DOI 10.7554/eLife.33660 </ref>
 

Revision as of 09:25, 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. 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
  13. 13.0 13.1 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
  14. Cite error: Invalid <ref> tag; no text was provided for refs named architecture
  15. 15.0 15.1 15.2 15.3 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
  16. doi: https://dx.doi.org/10.4236/jbm.2019.712012
  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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