Spa2 remodels ADP-actin via molecular condensation under glucose starvation

Qianqian Ma, Wahyu Surya, Danxia He, Hanmeng Yang, Xiao Han, Mui Hoon Nai, Chwee Teck Lim, Jaume Torres and Yansong Miao ()
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Qianqian Ma: Nanyang Technological University
Wahyu Surya: Nanyang Technological University
Danxia He: Nanyang Technological University
Hanmeng Yang: Nanyang Technological University
Xiao Han: Nanyang Technological University
Mui Hoon Nai: National University of Singapore
Chwee Teck Lim: National University of Singapore
Jaume Torres: Nanyang Technological University
Yansong Miao: Nanyang Technological University

Nature Communications, 2024, vol. 15, issue 1, 1-16

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-48863-4

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