ReviewCritical reviews in biochemistry and molecular biology
Actin filament nucleation and elongation factors--structure-function relationships.
Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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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
91 citing papers in PubMed, 148 citations in OpenAlex.
- Cryopreservation of Human Spermatozoa Using Penetrating Cryoprotectant-Free Vitrification Medium Exhibits an Altered Proteomic Profile Compared to the Conventional Rapid Freezing Method.Reproductive sciences (Thousand Oaks, Calif.) · 2026Article
- A balance between nucleating and elongating actin filaments controls deformation of protein condensates.Science advances · 2026Article
- Article
- Liquid-like condensates that bind actin promote assembly and bundling of actin filaments.Developmental cell · 2025Article
- The phase-separating Magnaporthe oryzae MoSpa2 complex organizes actin nucleation centers for plant infection.The Plant cell · 2025Article
- Article
- Disulfidptosis: a novel cell death modality induced by actin cytoskeleton collapse and a promising target for cancer therapeutics.Cell communication and signaling : CCS · 2024Review
- Liquid-like condensates that bind actin drive filament polymerization and bundling.bioRxiv : the preprint server for biology · 2024Article
- Article
- The Role of Liquid-Liquid Phase Separation in Actin Polymerization.International journal of molecular sciences · 2023Review
- Functional Mimicry of Eukaryotic Actin Assembly by Pathogen Effector Proteins.International journal of molecular sciences · 2022Review
- Actin dynamics in protein homeostasis.Bioscience reports · 2022Review
- PCARE requires coiled coil, RP62 kinase-binding and EVH1 domain-binding motifs for ciliary expansion.Human molecular genetics · 2022Article
- Article
- Human deafness-associated variants alter the dynamics of key molecules in hair cell stereocilia F-actin cores.Human genetics · 2022Review
- Zero-mode waveguides visualize the first steps during gelsolin-mediated actin filament formation.Biophysical journal · 2022Article
- Probes for Fluorescent Visualization of Specific Cellular Organelles.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Tetrapyrrolic Pigments from Heme- and Chlorophyll Breakdown are Actin-Targeting Compounds.Angewandte Chemie (International ed. in English) · 2021Article
- Phosphorylation of the WH2 domain in yeast Las17/WASP regulates G-actin binding and protein function during endocytosis.Scientific reports · 2021Article
- Neuronal Wiskott-Aldrich syndrome protein regulates Pseudomonas aeruginosa-induced lung vascular permeability through the modulation of actin cytoskeletal dynamics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
The spontaneous and unregulated polymerization of actin filaments is inhibited in cells by actin monomer-binding proteins such as profilin and Tbeta4. Eukaryotic cells and certain pathogens use filament nucleators to stabilize actin polymerization nuclei, whose formation is rate-limiting. Known filament nucleators include the Arp2/3 complex and its large family of nucleation promoting factors (NPFs), formins, Spire, Cobl, VopL/VopF, TARP and Lmod. These molecules control the time and location for polymerization, and additionally influence the structures of the actin networks that they generate. Filament nucleators are generally unrelated, but with the exception of formins they all use the WASP-Homology 2 domain (WH2 or W), a small and versatile actin-binding motif, for interaction with actin. A common architecture, found in Spire, Cobl and VopL/VopF, consists of tandem W domains that bind three to four actin subunits to form a nucleus. Structural considerations suggest that NPFs-Arp2/3 complex can also be viewed as a specialized form of tandem W-based nucleator. Formins are unique in that they use the formin-homology 2 (FH2) domain for interaction with actin and promote not only nucleation, but also processive barbed end elongation. In contrast, the elongation function among W-based nucleators has been "outsourced" to a dedicated family of proteins, Eva/VASP, which are related to WASP-family NPFs.
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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.