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| | ==Solution structure of paxillin LIM4== | | ==Solution structure of paxillin LIM4== |
| - | <StructureSection load='6u4m' size='340' side='right'caption='[[6u4m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6u4m' size='340' side='right'caption='[[6u4m]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6u4m]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6U4M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6U4M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6u4m]] 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=6U4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6U4M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PXN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6u4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u4m OCA], [https://pdbe.org/6u4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6u4m RCSB], [https://www.ebi.ac.uk/pdbsum/6u4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6u4m 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=6u4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6u4m OCA], [http://pdbe.org/6u4m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6u4m RCSB], [http://www.ebi.ac.uk/pdbsum/6u4m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6u4m ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PAXI_HUMAN PAXI_HUMAN]] Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). | + | [https://www.uniprot.org/uniprot/PAXI_HUMAN PAXI_HUMAN] Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion). |
| | <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: Qin, J]] | + | [[Category: Qin J]] |
| - | [[Category: Zhu, L]] | + | [[Category: Zhu L]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Lim domain]]
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| - | [[Category: Zinc finger]]
| + | |
| Structural highlights
Function
PAXI_HUMAN Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).
Publication Abstract from PubMed
Activation of cell surface receptor integrin has been extensively studied as the first key step to trigger cell adhesion, but the subsequent events, widely regarded as integrin "outside-in" signaling to form supramolecular complexes (focal adhesions [FAs]) to promote dynamic cell adhesion, remain poorly elucidated. Integrin activator kindlin-2 was recently found to associate with paxillin in nascent FAs, implicating an early yet undefined integrin outside-in signaling event. Here we show structurally that kindlin-2 recognizes paxillin via a distinct interface involving the ubiquitin-like kindlin-2 F0 domain and the paxillin LIM4 domain. The interface is adjacent to the membrane binding site of kindlin-2 F0, suggesting a mechanism for kindlin-2 to recruit paxillin to the membrane-proximal site where FA assembly is initiated. Disruption of the interface impaired the localization of paxillin, causing strong defects in FA assembly and cell migration. These data unveil a structural basis of the kindlin-2/paxillin interaction in controlling dynamic cell adhesion.
Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion.,Zhu L, Liu H, Lu F, Yang J, Byzova TV, Qin J Structure. 2019 Sep 30. pii: S0969-2126(19)30312-0. doi:, 10.1016/j.str.2019.09.006. PMID:31590942[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhu L, Liu H, Lu F, Yang J, Byzova TV, Qin J. Structural Basis of Paxillin Recruitment by Kindlin-2 in Regulating Cell Adhesion. Structure. 2019 Sep 30. pii: S0969-2126(19)30312-0. doi:, 10.1016/j.str.2019.09.006. PMID:31590942 doi:http://dx.doi.org/10.1016/j.str.2019.09.006
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