ArticleJournal of molecular biology2008
Crystal structures of monomeric actin bound to cytochalasin D.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 99 citations in OpenAlex.
- Fibrillar adhesion dynamics govern the timescales of nuclear mechano-response via the vimentin cytoskeleton.Nature materials · 2026Article
- NQO1-Responsive Prodrug for in Cellulo Release of Cytochalasin B as Cancer Cell-Targeted Migrastatic.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Design and Synthesis of Actin-Targeting 10-Phenoxy Cytochalasan Analogues: Balancing Cytotoxicity and Migrastatic Activity.ACS medicinal chemistry letters · 2026Article
- Exploring the Substitution of the C21-OAc Moiety in [11]Cytochalasans: Synthesis and Evaluation of Fluorophore Conjugates.Chembiochem : a European journal of chemical biology · 2026Article
- Highly divergent apicomplexan cytoskeletons provide additional models for actin biology.The FEBS journal · 2025Review
- Please inhibit responsibly: Natural and synthetic actin toxins as useful tools in cell biology.Molecular biology of the cell · 2025Review
- A revised model of nuclear actin import: Importin 9 competes with cofilin, profilin, and RanGTP for actin binding.bioRxiv : the preprint server for biology · 2025Article
- Microscopic and structural observations of actin filament capping and severing by cytochalasin D.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Fungal-derived methyldeoxaphomins targetProceedings of the National Academy of Sciences of the United States of America · 2025Article
- A high-throughput chemotaxis assay for assessing immunotoxicity using multiple human immune cell types.NAM journal · 2025Article
- Comprehensive Cell Biological Investigation of Cytochalasin B Derivatives with Distinct Activities on the Actin Network.Journal of natural products · 2024Article
- Synthesis and migrastatic activity of cytochalasin analogues lacking a macrocyclic moiety.RSC medicinal chemistry · 2024Article
- Exploring the Potential of Metal-Based Candidate Drugs as Modulators of the Cytoskeleton.Chembiochem : a European journal of chemical biology · 2023Review
- Cytochalasans and Their Impact on Actin Filament Remodeling.Biomolecules · 2023Review
- Actin-Interacting Amphidinolides: Syntheses and Mechanisms of Action of Amphidinolides X, J, and K.Molecules (Basel, Switzerland) · 2023Review
- MYO10 regulates genome stability and cancer inflammation through mediating mitosis.Cell reports · 2023Article
- Sulfonylpiperazine compounds prevent Plasmodium falciparum invasion of red blood cells through interference with actin-1/profilin dynamics.PLoS biology · 2023Article
- Next Generation Opto-Jasplakinolides Enable Local Remodeling of Actin Networks.Angewandte Chemie (International ed. in English) · 2022Article
- Pointed-end processive elongation of actin filaments byScience advances · 2022Article
- Histidine methyltransferase SETD3 methylates structurally diverse histidine mimics in actin.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The fungal toxin cytochalasin D (CD) interferes with the normal dynamics of the actin cytoskeleton by binding to the barbed end of actin filaments. Despite its widespread use as a tool for studying actin-mediated processes, the exact location and nature of its binding to actin have not been previously determined. Here we describe two crystal structures of an expressed monomeric actin in complex with CD: one obtained by soaking preformed actin crystals with CD, and the other obtained by cocrystallization. The binding site for CD, in the hydrophobic cleft between actin subdomains 1 and 3, is the same in the two structures. Polar and hydrophobic contacts play equally important roles in CD binding, and six hydrogen bonds stabilize the actin-CD complex. Many unrelated actin-binding proteins and marine toxins target this cleft and the hydrophobic pocket at the front end of the cleft (viewing actin with subdomain 2 in the upper right corner). CD differs in that it binds to the back half of the cleft. The ability of CD to induce actin dimer formation and actin-catalyzed ATP hydrolysis may be related to its unique binding site and the necessity to fit its bulky macrocycle into this cleft. Contacts with residues lining this cleft appear to be crucial to capping and/or severing. The cocrystallized actin-CD structure also revealed changes in actin conformation. An approximately 6 degrees rotation of the smaller actin domain (subdomains 1 and 2) with respect to the larger domain (subdomains 3 and 4) results in small changes in crystal packing that allow the D-loop to adopt an extended loop structure instead of being disordered, as it is in most crystal structures of actin. We speculate that these changes represent a potential conformation that the actin monomer can adopt on the pathway to polymerization or in the filament.
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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 OpenQuestion graph.