ArticleNature communications2024
Spa2 remodels ADP-actin via molecular condensation under glucose starvation.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- A practical guide to investigating biomolecular condensates: a comment from the plant community.Science China. Life sciences · 2026Review
- Structure and mechanism of an actin-dependent bacterial phosphoryl AMPylase.Nature chemical biology · 2026Article
- Phase Separation-Regulated Fungal Growth, Sexual Development, Adaptation and Synthetic Biology Applications.Journal of fungi (Basel, Switzerland) · 2025Review
- Mechanism of SC targeting RhoA regulation and its potential value in gastric cancer therapy.Biochemistry and biophysics reports · 2025Article
- ADPact: A versatile sensor for ADP-F-actin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The phase-separating Magnaporthe oryzae MoSpa2 complex organizes actin nucleation centers for plant infection.The Plant cell · 2025Article
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Authors and funding
9 authors.
Funding
Abstract
Actin nucleotide-dependent actin remodeling is essential to orchestrate signal transduction and cell adaptation. Rapid energy starvation requires accurate and timely reorganization of the actin network. Despite distinct treadmilling mechanisms of ADP- and ATP-actin filaments, their filament structures are nearly identical. How other actin-binding proteins regulate ADP-actin filament assembly is unclear. Here, we show that Spa2 which is the polarisome scaffold protein specifically remodels ADP-actin upon energy starvation in budding yeast. Spa2 triggers ADP-actin monomer nucleation rapidly through a dimeric core of Spa2 (aa 281-535). Concurrently, the intrinsically disordered region (IDR, aa 1-281) guides Spa2 undergoing phase separation and wetting on the surface of ADP-G-actin-derived F-actin and bundles the filaments. Both ADP-actin-specific nucleation and bundling activities of Spa2 are actin D-loop dependent. The IDR and nucleation core of Spa2 are evolutionarily conserved by coexistence in the fungus kingdom, suggesting a universal adaptation mechanism in the fungal kingdom in response to glucose starvation, regulating ADP-G-actin and ADP-F-actin with high nucleotide homogeneity.
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