|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Lim5 domain of PINCH1 protein== | | ==Lim5 domain of PINCH1 protein== |
| - | <StructureSection load='6mif' size='340' side='right'caption='[[6mif]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6mif' size='340' side='right'caption='[[6mif]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6mif]] 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=6MIF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6MIF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6mif]] 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=6MIF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MIF FirstGlance]. <br> |
| | </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> | | </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">LIMS1, PINCH, PINCH1 ([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=6mif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mif OCA], [https://pdbe.org/6mif PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mif RCSB], [https://www.ebi.ac.uk/pdbsum/6mif PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mif ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6mif FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mif OCA], [http://pdbe.org/6mif PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mif RCSB], [http://www.ebi.ac.uk/pdbsum/6mif PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mif ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LIMS1_HUMAN LIMS1_HUMAN]] Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation. | + | [https://www.uniprot.org/uniprot/LIMS1_HUMAN LIMS1_HUMAN] Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 22: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Qin, J]] | + | [[Category: Qin J]] |
| - | [[Category: Vaynberg, J]] | + | [[Category: Vaynberg J]] |
| - | [[Category: Lim domain]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Zn binding]]
| + | |
| Structural highlights
Function
LIMS1_HUMAN Adapter protein in a cytoplasmic complex linking beta-integrins to the actin cytoskeleton, bridges the complex to cell surface receptor tyrosine kinases and growth factor receptors. Involved in the regulation of cell survival, cell proliferation and cell differentiation.
Publication Abstract from PubMed
Dynamic communication between integrin-containing complexes (focal adhesions, FAs) and actin filaments is critical for regulating cell adhesion. Pseudokinase ILK plays a key role in this process but the underlying mechanism remains highly elusive. Here we show that by recruiting FA adaptors PINCH and Parvin into a heterotrimeric complex (IPP), ILK triggers F-actin filament bundling - a process known to generate force/mechanical signal to promote cytoskeleton reassembly and dynamic cell adhesion. Structural, biochemical, and functional analyses revealed that the F-actin bundling is orchestrated by two previously unrecognized WASP-Homology-2 actin binding motifs within IPP, one from PINCH and the other from Parvin. Strikingly, this process is also sensitized to Mg-ATP bound to the pseudoactive site of ILK and its dysregulation severely impairs stress fibers formation, cell spreading, and migration. These data identify a crucial mechanism for ILK, highlighting its uniqueness as a pseudokinase to transduce non-catalytic signal and regulate cell adhesion.
Non-catalytic signaling by pseudokinase ILK for regulating cell adhesion.,Vaynberg J, Fukuda K, Lu F, Bialkowska K, Chen Y, Plow EF, Qin J Nat Commun. 2018 Oct 26;9(1):4465. doi: 10.1038/s41467-018-06906-7. PMID:30367047[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Vaynberg J, Fukuda K, Lu F, Bialkowska K, Chen Y, Plow EF, Qin J. Non-catalytic signaling by pseudokinase ILK for regulating cell adhesion. Nat Commun. 2018 Oct 26;9(1):4465. doi: 10.1038/s41467-018-06906-7. PMID:30367047 doi:http://dx.doi.org/10.1038/s41467-018-06906-7
|
