| Structural highlights
Function
[CSCL5_ARATH] Acts as a hyperosmolarity-gated non-selective cation channel that permeates Ca(2+) ions. Shows the following permeability sequence: K(+) > Ba(2+) = Ca(2+) > Na(+) = Mg(2+) = Cs(+).[1]
Publication Abstract from PubMed
Mechanosensitive ion channels convert mechanical stimuli into a flow of ions. These channels are widely distributed from bacteria to higher plants and humans, and are involved in many crucial physiological processes. Here we show that two members of the OSCA protein family in Arabidopsis thaliana, namely AtOSCA1.1 and AtOSCA3.1, belong to a new class of mechanosensitive ion channels. We solve the structure of the AtOSCA1.1 channel at 3.5-A resolution and AtOSCA3.1 at 4.8-A resolution by cryo-electron microscopy. OSCA channels are symmetric dimers that are mediated by cytosolic inter-subunit interactions. Strikingly, they have structural similarity to the mammalian TMEM16 family proteins. Our structural analysis accompanied with electrophysiological studies identifies the ion permeation pathway within each subunit and suggests a conformational change model for activation.
Structure of the mechanosensitive OSCA channels.,Zhang M, Wang D, Kang Y, Wu JX, Yao F, Pan C, Yan Z, Song C, Chen L Nat Struct Mol Biol. 2018 Sep;25(9):850-858. doi: 10.1038/s41594-018-0117-6. Epub, 2018 Sep 6. PMID:30190597[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yuan F, Yang H, Xue Y, Kong D, Ye R, Li C, Zhang J, Theprungsirikul L, Shrift T, Krichilsky B, Johnson DM, Swift GB, He Y, Siedow JN, Pei ZM. OSCA1 mediates osmotic-stress-evoked Ca2+ increases vital for osmosensing in Arabidopsis. Nature. 2014 Oct 16;514(7522):367-71. doi: 10.1038/nature13593. Epub 2014 Aug 27. PMID:25162526 doi:http://dx.doi.org/10.1038/nature13593
- ↑ Zhang M, Wang D, Kang Y, Wu JX, Yao F, Pan C, Yan Z, Song C, Chen L. Structure of the mechanosensitive OSCA channels. Nat Struct Mol Biol. 2018 Sep;25(9):850-858. doi: 10.1038/s41594-018-0117-6. Epub, 2018 Sep 6. PMID:30190597 doi:http://dx.doi.org/10.1038/s41594-018-0117-6
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