6lqi
From Proteopedia
(Difference between revisions)
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<SX load='6lqi' size='340' side='right' viewer='molstar' caption='[[6lqi]], [[Resolution|resolution]] 4.50Å' scene=''> | <SX load='6lqi' size='340' side='right' viewer='molstar' caption='[[6lqi]], [[Resolution|resolution]] 4.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6lqi]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LQI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6lqi]] is a 3 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=6LQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6LQI FirstGlance]. <br> |
| - | </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=6lqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lqi OCA], [http://pdbe.org/6lqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lqi RCSB], [http://www.ebi.ac.uk/pdbsum/6lqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lqi ProSAT]</span></td></tr> | + | </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> |
| + | <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=6lqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lqi OCA], [http://pdbe.org/6lqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lqi RCSB], [http://www.ebi.ac.uk/pdbsum/6lqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lqi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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> | [[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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The mechanosensitive Piezo1 and Piezo2 channels convert mechanical force into cation permeation. However, their precise mechanogating and regulatory mechanisms remain elusive. Here, we report that Piezo1 utilizes three lateral ion-conducting portals equipped with physical gates for cooperative gating and splicing regulation. Mutating residues lining the portal converts Piezo1 into an anion-selective channel, demonstrating the portal-based cation-permeating pathway. Intriguingly, the portal is physically blocked with a plug domain, which undergoes alternative splicing in both Piezo1 and Piezo2. The Piezo1 isoform has local openings of the portals, enlarged single-channel conductance and sensitized mechanosensitivity. Remarkably, the three plugs are strategically latched onto the central axis for coordinated gating of the three portals. Disrupting the latching induces three quantal sub-conductance states in Piezo1, but not in the isoform. Together, we propose that Piezo utilizes an elegant plug-and-latch mechanism to physically and coordinately gate the lateral portals through the spliceable plug gates. | ||
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| + | A Plug-and-Latch Mechanism for Gating the Mechanosensitive Piezo Channel.,Geng J, Liu W, Zhou H, Zhang T, Wang L, Zhang M, Li Y, Shen B, Li X, Xiao B Neuron. 2020 Mar 5. pii: S0896-6273(20)30109-4. doi:, 10.1016/j.neuron.2020.02.010. PMID:32142647<ref>PMID:32142647</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6lqi" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</SX> | </SX> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Lk3 transgenic mice]] | ||
[[Category: Geng, J]] | [[Category: Geng, J]] | ||
[[Category: Li, X]] | [[Category: Li, X]] | ||
Revision as of 10:19, 18 March 2020
Cryo-EM structure of the mouse Piezo1 isoform Piezo1.1
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Categories: Large Structures | Lk3 transgenic mice | Geng, J | Li, X | Liu, W | Shen, B | Wang, L | Xiao, B | Zhang, M | Zhang, T | Zhou, H | Isoform | Mechanogating | Mechanotransduction channel | Membrane protein | Piezo1 1
