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Integrated structural model of the palladin–actin complex using XL ‐ MS , docking, NMR , and SAXS
Open accessPublished version of a preprint
Abstract
Palladin is an actin‐binding protein that accelerates actin polymerization and is linked to the metastasis of several types of cancer. Previously, three lysine residues in an immunoglobulin‐like domain of palladin have been identified as essential for actin binding. However, it is still unknown where palladin binds to F‐actin. Evidence that palladin binds to the sides of actin filaments to facilitate branching is supported by our previous study showing that palladin was able to compensate for Arp2/3 in the formation of Listeria actin comet tails. Here, we used chemical crosslinking to covalently link palladin and F‐actin residues based on spatial proximity. Samples were then enzymatically digested, separated by liquid chromatography, and analyzed by tandem mass spectrometry. Peptides containing the crosslinks and specific residues involved were then identified for input to the HADDOCK docking server to model the most likely binding conformation. Small‐angle x‐ray scattering was used to provide further insight into palladin flexibility and the binding interface, and NMR spectra identified potential interactions between palladin's Ig domains. Our final structural model of the F‐actin:palladin complex revealed how palladin interacts with and stabilizes F‐actin at the interface between two actin monomers. Three actin residues that were identified in this study also appear commonly in the actin‐binding interface with other proteins such as myotilin, myosin, and tropomodulin. An accurate structural representation of the complex between palladin and actin extends our understanding of palladin's role in promoting cancer metastasis through the regulation of actin dynamics.
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Metadata
- Authors
- Sargent, R., Liu, D. H., Yadav, R., Glennenmeier, D., Bradford, C., Urbina, N., & Beck, M. R.
- Affiliations
- Wichita State University (US)
- University of Arkansas – Fort Smith (US)
- Corresponding author
- Beck, Moriah R.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2025-04-18
- Volume
- 34
- Issue
- 5
- Pages
- e70122-e70122
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC12006749
- OpenAlex
- W4409565089
- Cited by
- 3
- References
- 62
- Citations by year
- 2026: 2 · 2025: 1
- FWCI
- 0.90
- Type
- journal article
- Language
- en
- Open access
- green
- pmc.ncbi.nlm.nih.gov
- Licence
- Locations
- Protein Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed Central (submittedVersion)
- OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
- Holmes Museum Of Anthropology (Wichita State University) (submittedVersion)
- Funders
- National Institutes of Health (P20GM103418, P30GM133894, R15GM120670)
- U.S. Department of Energy (DE‐AC02‐76SF00515)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- palladin, F-actin, actin-binding proteins, actin polymerization, actin filament branching, Arp2/3 complex, immunoglobulin-like domains, lysine residues, chemical crosslinking, protein-protein interfaces, actin filament stabilization, metastasis, actin dynamics
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