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| | ==ZO1 ZU5 domain MC/AA mutation== | | ==ZO1 ZU5 domain MC/AA mutation== |
| - | <StructureSection load='2kxr' size='340' side='right'caption='[[2kxr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2kxr' size='340' side='right'caption='[[2kxr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kxr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kxr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KXR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KXR FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2kxs|2kxs]]</div></td></tr> | + | </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=2kxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxr OCA], [https://pdbe.org/2kxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxr RCSB], [https://www.ebi.ac.uk/pdbsum/2kxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxr ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TJP1, ZO1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kxr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kxr OCA], [https://pdbe.org/2kxr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kxr RCSB], [https://www.ebi.ac.uk/pdbsum/2kxr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kxr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ZO1_HUMAN ZO1_HUMAN]] The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells.<ref>PMID:21240187</ref>
| + | [https://www.uniprot.org/uniprot/ZO1_HUMAN ZO1_HUMAN] The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells.<ref>PMID:21240187</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Wen, W]] | + | [[Category: Wen W]] |
| - | [[Category: Zhang, M]] | + | [[Category: Zhang M]] |
| - | [[Category: Beta-barrel]]
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| - | [[Category: Protein binding]]
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| Structural highlights
Function
ZO1_HUMAN The N-terminal may be involved in transducing a signal required for tight junction assembly, while the C-terminal may have specific properties of tight junctions. The alpha domain might be involved in stabilizing junctions. Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells.[1]
Publication Abstract from PubMed
Zonula occludens (ZO)-1 is a multi-domain scaffold protein known to have critical roles in the establishment of cell-cell adhesions and the maintenance of stable tissue structures through the targeting, anchoring, and clustering of transmembrane adhesion molecules and cytoskeletal proteins. Here, we report that ZO-1 directly binds to MRCKbeta, a Cdc42 effector kinase that modulates cell protrusion and migration, at the leading edge of migrating cells. Structural studies reveal that the binding of a beta hairpin from GRINL1A converts ZO-1 ZU5 into a complete ZU5-fold. A similar interaction mode is likely to occur between ZO-1 ZU5 and MRCKbeta. The interaction between ZO-1 and MRCKbeta requires the kinase to be primed by Cdc42 due to the closed conformation of the kinase. Formation of the ZO-1/MRCKbeta complex enriches the kinase at the lamellae of migrating cells. Disruption of the ZO-1/MRCKbeta complex inhibits MRCKbeta-mediated cell migration. These results demonstrate that ZO-1, a classical scaffold protein with accepted roles in maintaining cell-cell adhesions in stable tissues, also has an active role in cell migration during processes such as tissue development and remodelling.
Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration.,Huo L, Wen W, Wang R, Kam C, Xia J, Feng W, Zhang M EMBO J. 2011 Feb 16;30(4):665-78. Epub 2011 Jan 14. PMID:21240187[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huo L, Wen W, Wang R, Kam C, Xia J, Feng W, Zhang M. Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration. EMBO J. 2011 Feb 16;30(4):665-78. Epub 2011 Jan 14. PMID:21240187 doi:10.1038/emboj.2010.353
- ↑ Huo L, Wen W, Wang R, Kam C, Xia J, Feng W, Zhang M. Cdc42-dependent formation of the ZO-1/MRCKbeta complex at the leading edge controls cell migration. EMBO J. 2011 Feb 16;30(4):665-78. Epub 2011 Jan 14. PMID:21240187 doi:10.1038/emboj.2010.353
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