4rax

From Proteopedia

(Difference between revisions)

Revision as of 06:48, 2 March 2023

A regulatory domain of an ion channel

Structural highlights

4rax is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PIEZ1_MOUSE Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Piezo proteins are evolutionarily conserved and functionally diverse mechanosensitive cation channels. However, the overall structural architecture and gating mechanisms of Piezo channels have remained unknown. Here we determine the cryo-electron microscopy structure of the full-length (2,547 amino acids) mouse Piezo1 (Piezo1) at a resolution of 4.8 A. Piezo1 forms a trimeric propeller-like structure (about 900 kilodalton), with the extracellular domains resembling three distal blades and a central cap. The transmembrane region has 14 apparently resolved segments per subunit. These segments form three peripheral wings and a central pore module that encloses a potential ion-conducting pore. The rather flexible extracellular blade domains are connected to the central intracellular domain by three long beam-like structures. This trimeric architecture suggests that Piezo1 may use its peripheral regions as force sensors to gate the central ion-conducting pore.

Architecture of the mammalian mechanosensitive Piezo1 channel.,Ge J, Li W, Zhao Q, Li N, Chen M, Zhi P, Li R, Gao N, Xiao B, Yang M Nature. 2015 Nov 5;527(7576):64-9. doi: 10.1038/nature15247. Epub 2015 Sep 21. PMID:26390154^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Coste B, Mathur J, Schmidt M, Earley TJ, Ranade S, Petrus MJ, Dubin AE, Patapoutian A. Piezo1 and Piezo2 are essential components of distinct mechanically activated cation channels. Science. 2010 Oct 1;330(6000):55-60. doi: 10.1126/science.1193270. Epub 2010 Sep , 2. PMID:20813920 doi:http://dx.doi.org/10.1126/science.1193270
↑ Coste B, Xiao B, Santos JS, Syeda R, Grandl J, Spencer KS, Kim SE, Schmidt M, Mathur J, Dubin AE, Montal M, Patapoutian A. Piezo proteins are pore-forming subunits of mechanically activated channels. Nature. 2012 Feb 19;483(7388):176-81. doi: 10.1038/nature10812. PMID:22343900 doi:http://dx.doi.org/10.1038/nature10812
↑ Peyronnet R, Martins JR, Duprat F, Demolombe S, Arhatte M, Jodar M, Tauc M, Duranton C, Paulais M, Teulon J, Honore E, Patel A. Piezo1-dependent stretch-activated channels are inhibited by Polycystin-2 in renal tubular epithelial cells. EMBO Rep. 2013 Dec;14(12):1143-8. doi: 10.1038/embor.2013.170. Epub 2013 Oct 25. PMID:24157948 doi:http://dx.doi.org/10.1038/embor.2013.170
↑ Ranade SS, Qiu Z, Woo SH, Hur SS, Murthy SE, Cahalan SM, Xu J, Mathur J, Bandell M, Coste B, Li YS, Chien S, Patapoutian A. Piezo1, a mechanically activated ion channel, is required for vascular development in mice. Proc Natl Acad Sci U S A. 2014 Jul 15;111(28):10347-52. doi:, 10.1073/pnas.1409233111. Epub 2014 Jun 23. PMID:24958852 doi:http://dx.doi.org/10.1073/pnas.1409233111
↑ 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
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rax"

Categories: Large Structures | Mus musculus | Ge J | Yang M

@@ Line 1: / Line 1: @@
 ==A regulatory domain of an ion channel==
-<StructureSection load='4rax' size='340' side='right' caption='[[4rax]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
+<StructureSection load='4rax' size='340' side='right'caption='[[4rax]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4rax]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RAX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RAX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4rax]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RAX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RAX FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Piezo1, Fam38a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rax OCA], [https://pdbe.org/4rax PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rax RCSB], [https://www.ebi.ac.uk/pdbsum/4rax PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rax ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rax FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rax OCA], [http://pdbe.org/4rax PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rax RCSB], [http://www.ebi.ac.uk/pdbsum/4rax PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rax ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PIEZ1_MOUSE PIEZ1_MOUSE]] Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology.<ref>PMID:20813920</ref> <ref>PMID:22343900</ref> <ref>PMID:24157948</ref> <ref>PMID:24958852</ref> <ref>PMID:25119035</ref>
+[https://www.uniprot.org/uniprot/PIEZ1_MOUSE PIEZ1_MOUSE] Pore-forming subunit of a mechanosensitive non-specific cation channel. Generates currents characterized by a linear current-voltage relationship that are sensitive to ruthenium red and gadolinium. Plays a key role in epithelial cell adhesion by maintaining integrin activation through R-Ras recruitment to the ER, most probably in its activated state, and subsequent stimulation of calpain signaling. In the kidney, may contribute to the detection of intraluminal pressure changes and to urine flow sensing. Acts as shear-stress sensor that promotes endothelial cell organization and alignment in the direction of blood flow through calpain activation. Plays a key role in blood vessel formation and vascular structure in both development and adult physiology.<ref>PMID:20813920</ref> <ref>PMID:22343900</ref> <ref>PMID:24157948</ref> <ref>PMID:24958852</ref> <ref>PMID:25119035</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Ge, J]]
+[[Category: Mus musculus]]
-[[Category: Yang, M]]
+[[Category: Ge J]]
-[[Category: Extra-cellular]]
+[[Category: Yang M]]
-[[Category: Novel structure]]
-[[Category: Regulatory]]
-[[Category: Regulatory domain]]
-[[Category: Sandwich fold]]
-[[Category: Structural protein]]

4rax

From Proteopedia

Revision as of 06:48, 2 March 2023

A regulatory domain of an ion channel

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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