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The dynamic organization of the actin cytoskeleton, crucial for numerous cellular processes, is intricately regulated by the nucleotide state of actin filaments (F-actin). Visualization tools for specifically detecting ADP-bound F-actin, however, remain limited. Here, we introduce ADPact, a 20-amino-acid peptide that selectively binds to ADP-F-actin. ADPact allows for the precise visualization of ADP-F-actin structures both in vitro and in eukaryotic cells, particularly under energy stress conditions where ADP-/ATP-actin ratio increases. Importantly, ADPact and its fluorescent fusion variant, ADPact-GFP, do not disrupt actin dynamics, ensuring accurate monitoring of cytoskeletal reorganization. Our findings provide a powerful tool for studying actin dynamics and offer fresh insights into the regulation of the cytoskeleton under physiological and pathological conditions.
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http://dx.doi.org/10.1073/pnas.2420467122 | DOI Listing |
PLoS One
September 2025
Department of Mathematics and Statistics, College of Science, Imam Mohammad Ibn Saud Islamic University (IMSIU), Riyadh, Saudi Arabia.
This research explores the dynamical properties and solutions of actin filaments, which serve as electrical conduits for ion transport along their lengths. Utilizing the Lie symmetry approach, we identify symmetry reductions that simplify the governing equation by lowering its dimensionality. This process leads to the formulation of a second-order differential equation, which, upon applying a Galilean transformation, is further converted into a system of first-order differential equations.
View Article and Find Full Text PDFPLoS Genet
September 2025
Department of Biochemistry, Indian Institute of Science, Bengaluru, Karnataka, India.
Tropomyosin is an actin-binding protein (ABP) which protects actin filaments from cofilin-mediated disassembly. Distinct tropomyosin isoforms have long been hypothesized to differentially sort to subcellular actin networks and impart distinct functionalities. Nevertheless, a mechanistic understanding of the interplay between Tpm isoforms and their functional contributions to actin dynamics has been lacking.
View Article and Find Full Text PDFPLoS Comput Biol
September 2025
The Institute of Mathematical Sciences, CIT Campus, Taramani, Chennai, India.
The length of actin filaments is regulated by the combined action of hundreds of actin-binding proteins. While the roles of individual proteins are well understood, how they combine to regulate actin dynamics in vivo remains unclear. Recent advances in microscopy have enabled precise, high-throughput measurements of filament lengths over time.
View Article and Find Full Text PDFPLoS One
September 2025
Department of Plastic and Reconstructive Surgery, Keio University School of Medicine, Tokyo, Japan.
In adult mammals and other highly developed animals, incomplete wound healing, scar formation, and fibrosis occur. No treatment for complete tissue regeneration is currently available. However, in mice, at up to 13 days of gestation, early embryonic wounds regenerate without visible scarring.
View Article and Find Full Text PDFJ Cell Biol
October 2025
Cell and Systems Biology Program, Hospital for Sick Children, Toronto, Canada.
Mitochondria continually undergo fission to maintain their network and health. Nascent fission sites are marked by the ER, which facilitates actin polymerization to drive calcium flux into the mitochondrion and constrict the inner mitochondrial membrane. Septins are a major eukaryotic cytoskeleton component that forms filaments that can both directly and indirectly modulate other cytoskeleton components, including actin.
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