ArticleBiophysical journal2012
Molecular cooperativity of drebrin1-300 binding and structural remodeling of F-actin.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Structural mechanisms of drebrin-mediated F-actin network modulation.Nature communications · 2026Article
- Functional Differences Between Neuronal and Non-neuronal Isoforms of Drebrin.Journal of molecular biology · 2025Article
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Profiling ubiquitin signalling with UBIMAX reveals DNA damage- and SCFNature communications · 2023Article
- Review
- Biased localization of actin binding proteins by actin filament conformation.Nature communications · 2020Article
- Long-Range and Directional Allostery of Actin Filaments Plays Important Roles in Various Cellular Activities.International journal of molecular sciences · 2020Review
- Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly.Molecular biology of the cell · 2019Article
- Axon-Seq Decodes the Motor Axon Transcriptome and Its Modulation in Response to ALS.Stem cell reports · 2018Article
- Drebrin Isoforms Critically Regulate NMDAR- and mGluR-Dependent LTD Induction.Frontiers in cellular neuroscience · 2018Article
- Actin binding domain of filamin distinguishes posterior from anterior actin filaments in migratingBiophysics and physicobiology · 2016Article
- Article
- Drebrin inhibits cofilin-induced severing of F-actin.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Nanostructured self-assembly of inverted formin 2 (INF2) and F-actin-INF2 complexes revealed by atomic force microscopy.Langmuir : the ACS journal of surfaces and colloids · 2014Article
- Review
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Authors and funding
5 authors.
Funding
Abstract
Drebrin A, an actin-binding protein, is a key regulatory element in synaptic plasticity of neuronal dendrites. Understanding how drebrin binds and remodels F-actin is important for a functional analysis of their interactions. Conventionally, molecular models for protein-protein interactions use binding parameters derived from bulk solution measurements with limited spatial resolution, and the inherent assumption of homogeneous binding sites. In the case of actin filaments, their structural and dynamic states-as well as local changes in those states-may influence their binding parameters and interaction cooperativity. Here, we probed the structural remodeling of single actin filaments and the binding cooperativity of DrebrinA(1-300) -F-actin using AFM imaging. We show direct evidence of DrebrinA(1-300)-induced cooperative changes in the helical structure of F-actin and observe the binding cooperativity of drebrin to F-actin with nanometer resolution. The data confirm at the in vitro molecular level that variations in the F-actin helical structure can be modulated by cooperative binding of actin-binding proteins.
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