ArticleThe Journal of biological chemistry2020
The scaffold-protein IQGAP1 enhances and spatially restricts the actin-nucleating activity of Diaphanous-related formin 1 (DIAPH1).
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- Queue Gaps Among the IQGAPs inInternational journal of molecular sciences · 2026Review
- Negative cooperativity regulates ligand activation of DIAPH1 and other diaphanous related formins.Communications biology · 2025Article
- The Role of the Swollen State in Cell Proliferation.The Journal of membrane biology · 2025Review
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.The Journal of cell biology · 2024Article
- The DIAPH3 linker specifies a β-actin network that maintains RhoA and Myosin-II at the cytokinetic furrow.Nature communications · 2024Article
- Identification of an FMNL2 Interactome by Quantitative Mass Spectrometry.International journal of molecular sciences · 2024Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.bioRxiv : the preprint server for biology · 2024Article
- Anillin forms linear structures and facilitates furrow ingression after septin and formin depletion.Cell reports · 2023Article
- An Extracellular/Membrane-Bound S100P Pool Regulates Motility and Invasion of Human Extravillous Trophoblast Lines and Primary Cells.Biomolecules · 2023Article
- Review
- Inhibition of polar actin assembly by astral microtubules is required for cytokinesis.Nature communications · 2021Article
- Adenomatous Polyposis Coli (APC) in cell migration.European journal of cell biologyReview
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The actin cytoskeleton is a dynamic array of filaments that undergoes rapid remodeling to drive many cellular processes. An essential feature of filament remodeling is the spatio-temporal regulation of actin filament nucleation. One family of actin filament nucleators, the Diaphanous-related formins, is activated by the binding of small G-proteins such as RhoA. However, RhoA only partially activates formins, suggesting that additional factors are required to fully activate the formin. Here we identify one such factor, IQ motif containing GTPase activating protein-1 (IQGAP1), which enhances RhoA-mediated activation of the Diaphanous-related formin (DIAPH1) and targets DIAPH1 to the plasma membrane. We find that the inhibitory intramolecular interaction within DIAPH1 is disrupted by the sequential binding of RhoA and IQGAP1. Binding of RhoA and IQGAP1 robustly stimulates DIAPH1-mediated actin filament nucleation
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