ArticleScience advances2023
Diverse cytomotive actins and tubulins share a polymerization switch mechanism conferring robust dynamics.
Article in Science advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
- In-situ cryo-ET of mouse embryos reveals cytoplasmic lattices contain ubiquitin-charged E2-E3 ligase assemblies.The EMBO journal · 2026Article
- Eukaryotic-like microtubules and dynamic instability of Asgard archaeal tubulins.Science advances · 2026Article
- Adaptations in Plasmodium tubulin determine distinct microtubule architectures, mechanics and drug susceptibility.Nature communications · 2026Article
- On the curvature and relaxation of microtubule plus-end tips.Biophysical journal · 2026Article
- Structure insight into FtsZ function maintaining under acid stress of Streptococcus mutans.International journal of oral science · 2026Article
- Single-molecule microtubule dynamics measurements reveal an intermediate state and clarify the role of nucleotide.Nature communications · 2025Article
- Design of light- and chemically responsive protein assemblies through host-guest interactions.Chem · 2025Article
- Structural switching of tubulin in the microtubule lattice.Biochemical Society transactions · 2025Review
- Molecular dynamics simulations reveal differences in the conformational stability of FtsZs derived from Staphylococcus aureus and Bacillus subtilis.Scientific reports · 2024Article
- Roles of ESCRT-III polymers in cell division across the tree of life.Current opinion in cell biology · 2023Review
- Taxol acts differently on different tubulin isotypes.Communications biology · 2023Article
- Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody.Nature communications · 2023Article
- Chiral and nematic phases of flexible active filaments.Nature physics · 2023Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Protein filaments are used in myriads of ways to organize other molecules within cells. Some filament-forming proteins couple the hydrolysis of nucleotides to their polymerization cycle, thus powering the movement of other molecules. These filaments are termed cytomotive. Only members of the actin and tubulin protein superfamilies are known to form cytomotive filaments. We examined the basis of cytomotivity via structural studies of the polymerization cycles of actin and tubulin homologs from across the tree of life. We analyzed published data and performed structural experiments designed to disentangle functional components of these complex filament systems. Our analysis demonstrates the existence of shared subunit polymerization switches among both cytomotive actins and tubulins, i.e., the conformation of subunits switches upon assembly into filaments. These cytomotive switches can explain filament robustness, by enabling the coupling of kinetic and structural polarities required for cytomotive behaviors and by ensuring that single cytomotive filaments do not fall apart.
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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.