6rsn
From Proteopedia
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<StructureSection load='6rsn' size='340' side='right'caption='[[6rsn]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='6rsn' size='340' side='right'caption='[[6rsn]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[6rsn]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RSN OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6rsn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RSN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RSN FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6rsn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rsn OCA], [https://pdbe.org/6rsn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rsn RCSB], [https://www.ebi.ac.uk/pdbsum/6rsn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rsn ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/SOK4_ARATH SOK4_ARATH] SOSEKI proteins (SOK1-5) locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes, probably by guiding ANGUSTIFOLIA (AN) polarized localization (PubMed:30737509). Positive regulator of auxin (indole-3-acetic acid, IAA) biosynthesis and signaling pathway leading to the modulation of seedling growth, plant and inflorescence development (PubMed:31207460). Negative regulator of stress responses (e.g. salinity and osmotic stress) (PubMed:31207460).<ref>PMID:30737509</ref> <ref>PMID:31207460</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Cell polarity is fundamental for tissue morphogenesis in multicellular organisms. Plants and animals evolved multicellularity independently, and it is unknown whether their polarity systems are derived from a single-celled ancestor. Planar polarity in animals is conferred by Wnt signaling, an ancient signaling pathway transduced by Dishevelled, which assembles signalosomes by dynamic head-to-tail DIX domain polymerization. In contrast, polarity-determining pathways in plants are elusive. We recently discovered Arabidopsis SOSEKI proteins, which exhibit polar localization throughout development. Here, we identify SOSEKI as ancient polar proteins across land plants. Concentration-dependent polymerization via a bona fide DIX domain allows these to recruit ANGUSTIFOLIA to polar sites, similar to the polymerization-dependent recruitment of signaling effectors by Dishevelled. Cross-kingdom domain swaps reveal functional equivalence of animal and plant DIX domains. We trace DIX domains to unicellular eukaryotes and thus show that DIX-dependent polymerization is an ancient mechanism conserved between kingdoms and central to polarity proteins. | ||
+ | |||
+ | DIX Domain Polymerization Drives Assembly of Plant Cell Polarity Complexes.,van Dop M, Fiedler M, Mutte S, de Keijzer J, Olijslager L, Albrecht C, Liao CY, Janson ME, Bienz M, Weijers D Cell. 2020 Feb 6;180(3):427-439.e12. doi: 10.1016/j.cell.2020.01.011. Epub 2020, Jan 30. PMID:32004461<ref>PMID:32004461</ref> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6rsn" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Arabidopsis thaliana]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Bienz | + | [[Category: Bienz M]] |
- | [[Category: Fiedler | + | [[Category: Fiedler M]] |
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Current revision
SOSEKI polymerising domain (SOK4 D85A mutant)
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