Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks.

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Tác giả: Rey M Aguilar, Bruce L Goode, Neha Koundinya, Emma R McGuirk, Priyashree Nagarajan, Shae B Padrick, Meagan R Tomasso, Kathryn Wetzel

Ngôn ngữ: eng

Ký hiệu phân loại: 005.754 Network databases

Thông tin xuất bản: United States : The Journal of biological chemistry , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 90462

The rapid turnover of branched actin networks underlies key in vivo processes such as lamellipodial extension, endocytosis, phagocytosis, and intracellular transport. However, our understanding of the mechanisms used to dissociate, or "prune," branched filaments has remained limited. Glia maturation factor (GMF) is a cofilin family protein that binds to the Arp2/3 complex and catalyzes branch dissociation. Here, we show that another ligand of Arp2/3 complex, Saccharomyces cerevisiae coronin (Crn1), enhances Gmf1-mediated debranching by 8- to 10-fold, and that these effects depend on Arp2/3-binding "C" and "A" motifs in Crn1. Further, we show that Crn1 directly binds with high affinity (K
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