7ZW4
Crystal structure of Talin R7R8 domains with Caskin-2 LD-peptide
Summary for 7ZW4
Entry DOI | 10.2210/pdb7zw4/pdb |
Descriptor | Talin-1, Caskin-2 (2 entities in total) |
Functional Keywords | talin, caskin-2, focal adhesion, structural protein |
Biological source | Mus musculus (house mouse) More |
Total number of polymer chains | 2 |
Total formula weight | 34612.98 |
Authors | Celie, P.H.N.,Joosten, R.P.,Sonnenberg, A.,Perrakis, A. (deposition date: 2022-05-18, release date: 2023-05-31, Last modification date: 2024-06-12) |
Primary citation | Wang, W.,Atherton, P.,Kreft, M.,Te Molder, L.,van der Poel, S.,Hoekman, L.,Celie, P.,Joosten, R.P.,Fassler, R.,Perrakis, A.,Sonnenberg, A. Caskin2 is a novel talin- and Abi1-binding protein that promotes cell motility. J.Cell.Sci., 137:-, 2024 Cited by PubMed Abstract: Talin (herein referring collectively to talin 1 and 2) couples the actomyosin cytoskeleton to integrins and transmits tension to the extracellular matrix. Talin also interacts with numerous additional proteins capable of modulating the actin-integrin linkage and thus downstream mechanosignaling cascades. Here, we demonstrate that the scaffold protein Caskin2 interacts directly with the R8 domain of talin through its C-terminal LD motif. Caskin2 also associates with the WAVE regulatory complex to promote cell migration in an Abi1-dependent manner. Furthermore, we demonstrate that the Caskin2-Abi1 interaction is regulated by growth factor-induced phosphorylation of Caskin2 on serine 878. In MCF7 and UACC893 cells, which contain an amplification of CASKIN2, Caskin2 localizes in plasma membrane-associated plaques and around focal adhesions in cortical microtubule stabilization complexes. Taken together, our results identify Caskin2 as a novel talin-binding protein that might not only connect integrin-mediated adhesion to actin polymerization but could also play a role in crosstalk between integrins and microtubules. PubMed: 38587458DOI: 10.1242/jcs.262116 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.72 Å) |
Structure validation
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