6ABS

Actin interacting protein 5 (Aip5, mutant)

Summary for 6ABS

• Entry DOI: 10.2210/pdb6abs/pdb
• Descriptor: Actin binding protein, TRIETHYLENE GLYCOL, PENTAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: actin binding protein, structural protein
• Biological source: Saccharomyces cerevisiae S288C (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 28816.13

Authors

Sun, J.,Ying, X.,Toh, J.,Hong, W.,Miao, Y.,Gao, Y.G. (deposition date: 2018-07-23, release date: 2019-11-20, Last modification date: 2023-11-22)

Primary citation

Xie, Y.,Sun, J.,Han, X.,Tursic-Wunder, A.,Toh, J.D.W.,Hong, W.,Gao, Y.G.,Miao, Y.
Polarisome scaffolder Spa2-mediated macromolecular condensation of Aip5 for actin polymerization.
Nat Commun, 10:5078-5078, 2019

PubMed Abstract: A multiprotein complex polarisome nucleates actin cables for polarized cell growth in budding yeast and filamentous fungi. However, the dynamic regulations of polarisome proteins in polymerizing actin under physiological and stress conditions remains unknown. We identify a previously functionally unknown polarisome member, actin-interacting-protein 5 (Aip5), which promotes actin assembly synergistically with formin Bni1. Aip5-C terminus is responsible for its activities by interacting with G-actin and Bni1. Through N-terminal intrinsically disordered region, Aip5 forms high-order oligomers and generate cytoplasmic condensates under the stresses conditions. The molecular dynamics and reversibility of Aip5 condensates are regulated by scaffolding protein Spa2 via liquid-liquid phase separation both in vitro and in vivo. In the absence of Spa2, Aip5 condensates hamper cell growth and actin cable structures under stress treatment. The present study reveals the mechanisms of actin assembly for polarity establishment and the adaptation in stress conditions to protect actin assembly by protein phase separation.

PubMed: 31699995
DOI: 10.1038/s41467-019-13125-1

Experimental method

X-RAY DIFFRACTION (2.2 Å)