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| | <StructureSection load='4yl8' size='340' side='right'caption='[[4yl8]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='4yl8' size='340' side='right'caption='[[4yl8]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4yl8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome] and [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=4YL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YL8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4yl8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YL8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Msn ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), crb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=4yl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yl8 OCA], [https://pdbe.org/4yl8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yl8 RCSB], [https://www.ebi.ac.uk/pdbsum/4yl8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yl8 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=4yl8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yl8 OCA], [http://pdbe.org/4yl8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yl8 RCSB], [http://www.ebi.ac.uk/pdbsum/4yl8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yl8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MOES_MOUSE MOES_MOUSE]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. [[http://www.uniprot.org/uniprot/CRB_DROME CRB_DROME]] Plays a central role in cell polarity establishment. Participates in the assembly, positioning and maintenance of adherens junctions via its interaction with the SAC complex. Controls the coalescence of the spots of zonula adherens (ZA) into a adhesive ring around the cells. It may act as a signal. Involved in morphogenesis of the photoreceptor rhabdomere, for positioning and growth of rhabdomere and AJ during the crucial period of photoreceptor extension along the proximodistal axis of the retina.<ref>PMID:2344615</ref> | + | [https://www.uniprot.org/uniprot/MOES_MOUSE MOES_MOUSE] Probably involved in connections of major cytoskeletal structures to the plasma membrane. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4yl8" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4yl8" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Moesin|Moesin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Li, Y]] | + | [[Category: Li Y]] |
| - | [[Category: Wei, Z]] | + | [[Category: Wei Z]] |
| - | [[Category: Zhang, M]] | + | [[Category: Zhang M]] |
| - | [[Category: Ferm domain]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Protein complex]]
| + | |
| Structural highlights
Function
MOES_MOUSE Probably involved in connections of major cytoskeletal structures to the plasma membrane.
Publication Abstract from PubMed
The type I transmembrane protein Crumbs (Crb) plays critical roles in the establishment and maintenance of cell polarities in diverse tissues. As such, mutations of Crb can cause different forms of cancers. The cell intrinsic role of Crb in cell polarity is governed by its conserved, 37-residue cytoplasmic tail (Crb-CT) via binding to Moesin and Protein associated with Lin7-1 (PALS1). However, the detailed mechanism governing the Crb/Moesin interaction and the balance of Crb in binding to Moesin and PALS1 are not well understood. Here we report the 1.5 A resolution crystal structure of the Moesin Protein 4.1/Ezrin/Radixin/Moesin (FERM) /Crb-CT complex, revealing that both the canonical FERM-binding motif and the Postsynaptic density protein-95/Disc large-1/ Zonula occludens-1 (PDZ)-binding motif of Crb contribute to the Crb/Moesin interaction. We further demonstrate that phosphorylation of Crb-CT by atypical protein kinase C (aPKC) disrupts the Crb/Moesin association, but has no impact on the Crb/PALS1 interaction. The above results indicate that, upon the establishment of the apical-basal polarity in epithelia, apical-localized aPKC can actively prevent the Crb/Moesin complex formation and thereby shift Crb to form complex with PALS1 at apical junctions. Therefore, Crb may serve as an aPKC-mediated sensor in coordinating contact-dependent cell growth inhibition in epithelial tissues.
Structural basis for the phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein Crumbs and the actin binding protein Moesin.,Wei Z, Li Y, Ye F, Zhang M J Biol Chem. 2015 Mar 19. pii: jbc.M115.643791. PMID:25792740[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wei Z, Li Y, Ye F, Zhang M. Structural basis for the phosphorylation-regulated interaction between the cytoplasmic tail of cell polarity protein Crumbs and the actin binding protein Moesin. J Biol Chem. 2015 Mar 19. pii: jbc.M115.643791. PMID:25792740 doi:http://dx.doi.org/10.1074/jbc.M115.643791
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