4wip
From Proteopedia
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| - | ''' | + | ==DIX domain of human Dvl2== |
| + | <StructureSection load='4wip' size='340' side='right' caption='[[4wip]], [[Resolution|resolution]] 2.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wip]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WIP FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3pz8|3pz8]]</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=4wip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wip OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wip RCSB], [http://www.ebi.ac.uk/pdbsum/4wip PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DVL2_HUMAN DVL2_HUMAN]] Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes (By similarity).<ref>PMID:19252499</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Dishevelled relays Wnt signals from the plasma membrane to different cytoplasmic effectors. Its signalling activity depends on its DIX domain, which undergoes head-to-tail polymerization to assemble signalosomes. The DIX domain is ubiquitinated in vivo at multiple lysines, which can be antagonized by various deubiquitinases (DUBs) including the CYLD tumour suppressor that attenuates Wnt signalling. Here, we generate milligram quantities of pure human Dvl2 DIX domain mono-ubiquitinated at two lysines (K54 and K58) by genetically encoded orthogonal protection with activated ligation (GOPAL), to investigate their effect on DIX polymerization. We show that the ubiquitination of DIX at K54 blocks its polymerization in solution, whereas DIX58-Ub remains oligomerization-competent. DUB profiling identified 28 DUBs that cleave DIX-ubiquitin conjugates, half of which prefer, or are specific for, DIX54-Ub, including Cezanne and CYLD. These DUBs thus have the potential to promote Dvl polymerization and signalosome formation, rather than antagonize it as previously thought for CYLD. | ||
| - | + | Ubiquitination of the Dishevelled DIX domain blocks its head-to-tail polymerization.,Madrzak J, Fiedler M, Johnson CM, Ewan R, Knebel A, Bienz M, Chin JW Nat Commun. 2015 Apr 24;6:6718. doi: 10.1038/ncomms7718. PMID:25907794<ref>PMID:25907794</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bienz, M]] | ||
| + | [[Category: Chin, J W]] | ||
[[Category: Fiedler, M]] | [[Category: Fiedler, M]] | ||
| - | [[Category: Chin, J.W]] | ||
[[Category: Madrzak, J]] | [[Category: Madrzak, J]] | ||
| - | [[Category: | + | [[Category: Polymer signaling ubiquitin-like]] |
| + | [[Category: Signaling protein]] | ||
Revision as of 12:16, 13 May 2015
DIX domain of human Dvl2
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