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| - | ==Structure of the talin rod residues, domain C== | + | ==Solution Structure of the R6 Domain of Talin== |
| - | <StructureSection load='2l10' size='340' side='right'caption='[[2l10]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l10' size='340' side='right'caption='[[2l10]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l10]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L10 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L10 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l10]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L10 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tln1, Tln ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2l10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l10 OCA], [http://pdbe.org/2l10 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l10 RCSB], [http://www.ebi.ac.uk/pdbsum/2l10 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l10 ProSAT]</span></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=2l10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l10 OCA], [https://pdbe.org/2l10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l10 RCSB], [https://www.ebi.ac.uk/pdbsum/2l10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l10 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TLN1_MOUSE TLN1_MOUSE]] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. | + | [https://www.uniprot.org/uniprot/TLN1_MOUSE TLN1_MOUSE] Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Talin|Talin]] | + | *[[Talin 3D structures|Talin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Barsukov, I L]] | + | [[Category: Barsukov IL]] |
| - | [[Category: Bate, N]] | + | [[Category: Bate N]] |
| - | [[Category: Critchley, D R]] | + | [[Category: Critchley DR]] |
| - | [[Category: Gingras, A R]] | + | [[Category: Gingras AR]] |
| - | [[Category: Goult, B T]] | + | [[Category: Goult BT]] |
| - | [[Category: Roberts, G C.K]] | + | [[Category: Roberts GCK]] |
| - | [[Category: Cytoskeleton]]
| + | |
| - | [[Category: Focal adhesion]]
| + | |
| - | [[Category: Helical bundle]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Talin]]
| + | |
| Structural highlights
Function
TLN1_MOUSE Probably involved in connections of major cytoskeletal structures to the plasma membrane. High molecular weight cytoskeletal protein concentrated at regions of cell-substratum contact and, in lymphocytes, at cell-cell contacts.
Publication Abstract from PubMed
Talin activates integrins, couples them to F-actin and recruits vinculin to focal adhesions (FAs). Here we report the structural characterization of the talin rod, 13 helical bundles (R1-R13) organized into a compact cluster of 4-helix bundles (R2-R4) within a linear chain of 5-helix bundles. Nine of the bundles contain vinculin-binding sites (VBSs) - R2R3 are atypical each containing two VBSs. Talin R2R3 also binds synergistically to RIAM, a Rap1 effector involved in integrin activation. Biochemical and structural data show that vinculin and RIAM binding to R2R3 is mutually exclusive. Moreover, vinculin binding requires domain unfolding while RIAM binds the folded R2R3 double domain. In cells, RIAM is enriched in nascent adhesions at the leading edge whereas vinculin is enriched in FAs, and expression of the talin-binding domain of vinculin displaces RIAM from FAs. We propose a model in which RIAM binding to R2R3 initially recruits talin to membranes where it activates integrins. As talin engages F-actin, force exerted on R2R3 disrupts RIAM binding and exposes the VBSs, which recruit vinculin to stabilize the complex.
RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover.,Goult BT, Zacharchenko T, Bate N, Tsang R, Hey F, Gingras AR, Elliott PR, Roberts GC, Ballestrem C, Critchley DR, Barsukov IL J Biol Chem. 2013 Feb 6. PMID:23389036[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Goult BT, Zacharchenko T, Bate N, Tsang R, Hey F, Gingras AR, Elliott PR, Roberts GC, Ballestrem C, Critchley DR, Barsukov IL. RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover. J Biol Chem. 2013 Feb 6. PMID:23389036 doi:http://dx.doi.org/10.1074/jbc.M112.438119
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