ArticleProceedings of the National Academy of Sciences of the United States of America1999
Motility of ActA protein-coated microspheres driven by actin polymerization.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 106 papers.
What it found
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Who cites it
106 citing papers in PubMed.
- On the Assembly of Actin Polymerization-Powered Motors.Macromolecular rapid communications · 2026Article
- Technology Roadmap of Micro/Nanorobots.ACS nano · 2025Review
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- A unified purification method for actin-binding proteins using a TEV-cleavable His-Strep-tag.MethodsX · 2024Article
- A role for cross-linking proteins in actin filament network organization and force generation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Myosin-I synergizes with Arp2/3 complex to enhance the pushing forces of branched actin networks.Science advances · 2024Article
- Pushing boundaries: mechanisms enabling bacterial pathogens to spread between cells.Infection and immunity · 2024Review
- Arp2/3 complex- and formin-mediated actin cytoskeleton networks facilitate actin binding protein sorting in fission yeast.European journal of cell biology · 2024Article
- Mitochondrially-associated actin waves maintain organelle homeostasis and equitable inheritance.Current opinion in cell biology · 2024Review
- An interphase actin wave promotes mitochondrial content mixing and organelle homeostasis.Nature communications · 2024Article
- Article
- A Role for Cross-linking Proteins in Actin Filament Network Organization and Force Generation.bioRxiv : the preprint server for biology · 2024Article
- Myosin-I Synergizes with Arp2/3 Complex to Enhance Pushing Forces of Branched Actin Networks.bioRxiv : the preprint server for biology · 2024Article
- A programmable reaction-diffusion system for spatiotemporal cell signaling circuit design.Cell · 2024Article
- Recycling of the actin monomer pool limits the lifetime of network turnover.The EMBO journal · 2023Article
- Retromer oligomerization drives SNX-BAR coat assembly and membrane constriction.The EMBO journal · 2023Article
- Actin polymerization promotes invagination of flat clathrin-coated lattices in mammalian cells by pushing at lattice edges.Nature communications · 2022Article
- Catching the Conformational Wave: Measuring the Working Strokes of Protofilaments as They Curl Outward from Disassembling Microtubule Tips.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Capping protein is dispensable for polarized actin network growth and actin-based motility.The Journal of biological chemistry · 2020Article
- F-Actin Cytoskeleton Network Self-Organization Through Competition and Cooperation.Annual review of cell and developmental biology · 2020Review
46 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Actin polymerization is required for the generation of motile force at the leading edge of both lamellipodia and filopodia and also at the surface of motile intracellular bacterial pathogens such as Listeria monocytogenes. Local catalysis of actin filament polymerization is accomplished in L. monocytogenes by the bacterial protein ActA. Polystyrene beads coated with purified ActA protein can undergo directional movement in an actin-rich cytoplasmic extract. Thus, the actin polymerization-based motility generated by ActA can be used to move nonbiological cargo, as has been demonstrated for classical motor molecules such as kinesin and myosin. Initiation of unidirectional movement of a symmetrically coated particle is a function of bead size and surface protein density. Small beads (</=0.5 micrometer in diameter) initiate actin-based motility when local asymmetries are built up by random fluctuations of actin filament density or by thermal motion, demonstrating the inherent ability of the dynamic actin cytoskeleton to spontaneously self-organize into a polar structure capable of generating unidirectional force. Larger beads (up to 2 micrometers in diameter) can initiate movement only if surface asymmetry is introduced by coating the beads on one hemisphere. This explains why the relatively large L. monocytogenes requires polar distribution of ActA on its surface to move.
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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 OpenQuestion graph.