Functional comparison of full-length palladin to isolated actin binding domain

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Authors
Albraiki, Sharifah E.
Ajiboye, Oluwatosin
Sargent, Rachel
Beck, Moriah R.
Advisors
Issue Date
2023-05-01
Type
Article
Keywords
G- and F-actin binding , Palladin , Polymerization
Research Projects
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Citation
Albraiki, S, Ajiboye, O, Sargent, R, Beck, MR. Functional comparison of full-length palladin to isolated actin binding domain. Protein Science. 2023; 32( 5):e4638. https://doi.org/10.1002/pro.4638
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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Publisher
John Wiley & Sons, Ltd
Journal
Book Title
Series
Protein Science
Volume 32, No. 5
PubMed ID
DOI
ISSN
0961-8368
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