Functional comparison of full‐length palladin to isolated actin binding domain
Open accessPublished version of a preprint
Abstract
Palladin is an actin binding protein that is specifically upregulated in metastatic cancer cells but also colocalizes with actin stress fibers in normal cells and is critical for embryonic development as well as wound healing. Of nine isoforms present in humans, only the 90 kDa isoform of palladin, comprising three immunoglobulin (Ig) domains and one proline‐rich region, is ubiquitously expressed. Previous work has established that the Ig3 domain of palladin is the minimal binding site for F‐actin. In this work, we compare functions of the 90 kDa isoform of palladin to the isolated actin binding domain. To understand the mechanism of action for how palladin can influence actin assembly, we monitored F‐actin binding and bundling as well as actin polymerization, depolymerization, and copolymerization. Together, these results demonstrate that there are key differences between the Ig3 domain and full‐length palladin in actin binding stoichiometry, polymerization, and interactions with G‐actin. Understanding the role of palladin in regulating the actin cytoskeleton may help us develop means to prevent cancer cells from reaching the metastatic stage of cancer progression.
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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 · see citing works
The membrane-cytoskeleton linker ezrin is necessary for osteosarcoma metastasis
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- Authors
- Albraiki, S., Ajiboye, O., Sargent, R., & Beck, M. R.
- Affiliations
- Wichita State University (US)
- Corresponding author
- Beck, Moriah R.
- Venue
- Protein Science
- Publisher
- Wiley
- Published
- 2023-04-20
- Volume
- 32
- Issue
- 5
- Pages
- e4638-e4638
- ISSN
- 0961-8368 (ISSN-L)
- 1469-896X
- PMC
- PMC10117391
- OpenAlex
- W4362692600
- Cited by
- 4
- References
- 2
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2023: 1
- FWCI
- 0.58
- Type
- journal article
- Language
- en
- Open access
- green
- doi.org
- Locations
- Protein Science (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Holmes Museum Of Anthropology (Wichita State University) (submittedVersion)
- Funders
- National Institute of General Medical Sciences (R15GM120670)
- Topics
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- palladin, actin-binding domain, F-actin binding, actin bundling, actin polymerization, actin depolymerization, actin cytoskeleton regulation, metastasis, immunoglobulin domains
- MeSH terms
- Actins, Cytoskeletal Proteins, Humans, Microfilament Proteins, Actin Cytoskeleton, Phosphoproteins, Protein Isoforms
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