ArticleNature communications2018
Structural basis of actin monomer re-charging by cyclase-associated protein.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
52 citing papers in PubMed.
- Alterations of actin in aging.Journal of cell science · 2026Review
- Rapid actin filament turnover maintains cortical connectivity while allowing for cell cortex deformation and flow.bioRxiv : the preprint server for biology · 2026Article
- Loss of cyclase-associated protein 2 alters actin cytoskeleton organization and biomechanical properties of the ocular lens.Journal of cell science · 2026Article
- Mechanisms of disassembly at the actin filament pointed and barbed ends.Science advances · 2026Article
- The RCAR12-CAP1-OST1 module controls ABA-mediated stomatal closure in Arabidopsis.PLoS genetics · 2026Article
- Regulation of the formin INF2 by actin monomers and calcium/calmodulin.The Journal of cell biology · 2026Article
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- Highly divergent apicomplexan cytoskeletons provide additional models for actin biology.The FEBS journal · 2025Review
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Phalloidin and DNase I-bound F-actin pointed end structures reveal principles of filament stabilization and disassembly.Nature communications · 2024Article
- Cyclase-associated protein (CAP) inhibits inverted formin 2 (INF2) to induce dendritic spine maturation.Cellular and molecular life sciences : CMLS · 2024Article
- To each its own: Mechanisms of cross-talk between GPI biosynthesis and cAMP-PKA signaling in Candida albicans versus Saccharomyces cerevisiae.The Journal of biological chemistry · 2024Review
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.European journal of cell biology · 2024Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.bioRxiv : the preprint server for biology · 2024Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Cytosolic concentrations of actin binding proteins and the implications for in vivo F-actin turnover.The Journal of cell biology · 2023Article
- Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.The Journal of biological chemistry · 2023Article
- Dynamic remodeling of actin networks by cyclase-associated protein and CAP-Abp1 complexes.Current biology : CB · 2023Article
- Recycling of the actin monomer pool limits the lifetime of network turnover.The EMBO journal · 2023Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Actin polymerization powers key cellular processes, including motility, morphogenesis, and endocytosis. The actin turnover cycle depends critically on "re-charging" of ADP-actin monomers with ATP, but whether this reaction requires dedicated proteins in cells, and the underlying mechanism, have remained elusive. Here we report that nucleotide exchange catalyzed by the ubiquitous cytoskeletal regulator cyclase-associated protein (CAP) is critical for actin-based processes in vivo. We determine the structure of the CAP-actin complex, which reveals that nucleotide exchange occurs in a compact, sandwich-like complex formed between the dimeric actin-binding domain of CAP and two ADP-actin monomers. In the crystal structure, the C-terminal tail of CAP associates with the nucleotide-sensing region of actin, and this interaction is required for rapid re-charging of actin by both yeast and mammalian CAPs. These data uncover the conserved structural basis and biological role of protein-catalyzed re-charging of actin monomers.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.