Journal article
Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks
The Journal of biological chemistry, v 301(3), 108191
16 Jan 2025
PMID: 39826693
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
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 Arp2/3 complex and catalyzes branch dissociation. Here, we show that another ligand of Arp2/3 complex, S. cerevisiae coronin (Crn1), enhances Gmf1-mediated debranching by 8-10 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
= 1.4 nM) to S. cerevisiae GMF (Gmf1), and together they form a stable ternary Crn1-Gmf1-Arp2/3 complex in solution. Using single molecule analysis, we show that Gmf1 binds transiently and multiple times to F-actin branch junctions prior to debranching. These and other results suggest a mechanism of mutual recruitment, in which Crn1 increases the on-rate of Gmf1 for branch junctions and Gmf1 blocks Crn1 binding to actin filament sides, increasing its availability to bind branch junctions. Taken together, these observations reveal an unanticipated mechanism in which two distinct ligands of Arp2/3 complex bind to each other and synergize to prune actin branches.
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Details
- Title
- Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks
- Creators
- Neha Koundinya - Brandeis UniversityRey M Aguilar - Brandeis UniversityKathryn Wetzel - Brandeis UniversityMeagan R Tomasso - Drexel UniversityPriyashree Nagarajan - Drexel UniversityEmma R McGuirk - Brandeis UniversityShae B Padrick - Drexel UniversityBruce L Goode - Brandeis University
- Publication Details
- The Journal of biological chemistry, v 301(3), 108191
- Publisher
- ELSEVIER
- Number of pages
- 21
- Grant note
- NIGMS: R35 GM134895 Brandeis NSF MRSEC Bioinspired Soft Materials: DMR-2011486
Funding and additional information-This work was supported by a grant from NIGMS (R35 GM134895) to B. L. G., and by the Brandeis NSF MRSEC Bioinspired Soft Materials (DMR-2011486) . The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:001428196500001
- Scopus ID
- 2-s2.0-85217854388
- Other Identifier
- 991022020531604721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology