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Caskin2 is a novel talin and Abi1-binding protein that promotes cell motility
Open accessPreprint — published as 10.1242/jcs.262116
Abstract
Talin 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 CMSCs. Taken together, our results identify Caskin2 as a novel talin-binding protein that may not only connect integrin-mediated adhesion to actin polymerization, but could also play a role in crosstalk between integrins and microtubules.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Wang, W., Atherton, P., Kreft, M., te Molder, L., van der Poel, S., Hoekman, L., Celie, P., Joosten, R. P., Faessler, R., Perrakis, A., & Sonnenberg, A.
- Affiliations
- Shanghai Jiao Tong University (CN)
- University of Liverpool (GB)
- The Netherlands Cancer Institute (NL)
- Corresponding author
- Sonnenberg, Arnoud
- ORCID
- Venue
- Journal of Cell Science
- Publisher
- openRxiv
- Published
- 2024-03-17
- Volume
- 137
- Issue
- 9
- ISSN
- 0021-9533 (ISSN-L)
- PMC
- PMC11166458
- OpenAlex
- W4394568205
- Cited by
- 6
- References
- 1
- Citations by year
- 2026: 2 · 2025: 4
- FWCI
- 2.07
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- Journal of Cell Science (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DORA PSI (Paul Scherrer Institute) (submittedVersion, other-oa)
- Funders
- Alexander von Humboldt-Stiftung
- Wellcome Trust
- Universiteit Leiden
- National Natural Science Foundation of China (32300634)
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (184.032.201)
- KWF Kankerbestrijding (12143)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- talin, ABI1, cell motility, cell migration, WAVE regulatory complex, integrin signaling, actomyosin cytoskeleton, focal adhesions, microtubules, serine phosphorylation, mechanotransduction, MCF-7 cells
- MeSH terms
- Cell Movement, Cytoskeletal Proteins, Humans, Microtubules, Phosphorylation, Protein Binding, Integrins, Talin, Focal Adhesions, Adaptor Proteins, Signal Transducing, MCF-7 Cells
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