ArticleCurrent biology : CB2010
GMF is a cofilin homolog that binds Arp2/3 complex to stimulate filament debranching and inhibit actin nucleation.
Article in Current biology : CB, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 110 citations in OpenAlex.
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- Mechanism of Arp2/3 complex branch disassembly by human Coro7.Nature communications · 2025Article
- Phactr4 influences macrophage lamellipodial structure and dynamics through Arp2/3 complex and Ezrin regulation.bioRxiv : the preprint server for biology · 2025Article
- Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks.The Journal of biological chemistry · 2025Article
- The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025Review
- Glial maturation factor-β deficiency prevents oestrogen deficiency-induced bone loss by remodelling the actin network to suppress adipogenesis of bone marrow mesenchymal stem cells.Cell death & disease · 2024Article
- Disulfidptosis: a novel cell death modality induced by actin cytoskeleton collapse and a promising target for cancer therapeutics.Cell communication and signaling : CCS · 2024Review
- Direct observation of cortactin protecting Arp2/3-actin filament branch junctions from GMF-mediated destabilization.European journal of cell biology · 2024Article
- The stabilization of Arp2/3 complex generated actin filaments.Biochemical Society transactions · 2024Review
- Regeneration of actin filament branches from the same Arp2/3 complex.Science advances · 2024Article
- The role of actin cytoskeleton CFL1 and ADF/cofilin superfamily in inflammatory response.Frontiers in molecular biosciences · 2024Review
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- HIV-1 diverts cortical actin for particle assembly and release.Nature communications · 2023Article
- Regulation of branched versus linear Arp2/3-generated actin filaments.The EMBO journal · 2023Article
- Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022Review
- Single-molecule analysis of actin filament debranching by cofilin and GMF.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Nucleation, stabilization, and disassembly of branched actin networks.Trends in cell biology · 2022Review
- Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Macropinocytosis and Cell Migration: Don't Drink and Drive….Sub-cellular biochemistry · 2022Article
- The Actin Regulators Involved in the Function and Related Diseases of Lymphocytes.Frontiers in immunology · 2022Review
13 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Cell locomotion and endocytosis are powered by the rapid polymerization and turnover of branched actin filament networks nucleated by Arp2/3 complex. Although a large number of cellular factors have been identified that stimulate Arp2/3 complex-mediated actin nucleation, only a small number of studies so far have addressed which factors promote actin network debranching. Here, we investigated the function of a conserved homolog of ADF/cofilin, glia maturation factor (GMF). We found that S. cerevisiae GMF (also called Aim7) localizes in vivo to cortical actin patches and displays synthetic genetic interactions with ADF/cofilin. However, GMF lacks detectable actin binding or severing activity and instead binds tightly to Arp2/3 complex. Using in vitro evanescent wave microscopy, we demonstrated that GMF potently stimulates debranching of actin filaments produced by Arp2/3 complex. Further, GMF inhibits nucleation of new daughter filaments. Together, these data suggest that GMF binds Arp2/3 complex to both "prune" daughter filaments at the branch points and inhibit new actin assembly. These activities and its genetic interaction with ADF/cofilin support a role for GMF in promoting the remodeling and/or disassembly of branched networks. Therefore, ADF/cofilin and GMF, members of the same superfamily, appear to have evolved to interact with actin and actin-related proteins, respectively, and to make mechanistically distinct contributions to the remodeling of cortical actin structures.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.