ArticleCytoskeleton (Hoboken, N.J.)2014
Drebrin inhibits cofilin-induced severing of F-actin.
Article in Cytoskeleton (Hoboken, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 49 citations in OpenAlex.
- Structural mechanisms of drebrin-mediated F-actin network modulation.Nature communications · 2026Article
- Tight junction dysfunction and cytoskeletal remodeling in Hirschsprung‑associated enterocolitis: A decade of mechanistic insights and therapeutic prospects (Review).Molecular medicine reports · 2026Review
- Functional Differences Between Neuronal and Non-neuronal Isoforms of Drebrin.Journal of molecular biology · 2025Article
- Profiling ubiquitin signalling with UBIMAX reveals DNA damage- and SCFNature communications · 2023Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Drebrin Regulates Acetylcholine Receptor Clustering and Organization of Microtubules at the Postsynaptic Machinery.International journal of molecular sciences · 2021Article
- With the Permission of Microtubules: An Updated Overview on Microtubule Function During Axon Pathfinding.Frontiers in molecular neuroscience · 2021Review
- Biased localization of actin binding proteins by actin filament conformation.Nature communications · 2020Article
- Up-regulation of LIMK1 expression in prostate cancer is correlated with poor pathological features, lymph node metastases and biochemical recurrence.Journal of cellular and molecular medicine · 2020Article
- Gαq-mediated calcium dynamics and membrane tension modulate neurite plasticity.Molecular biology of the cell · 2020Article
- Synaptic actin stabilization protein loss in Down syndrome and Alzheimer disease.Brain pathology (Zurich, Switzerland) · 2020Article
- Radial somatic F-actin organization affects growth cone dynamics during early neuronal development.EMBO reports · 2019Article
- Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly.Molecular biology of the cell · 2019Article
- Activation of Cofilin Increases Intestinal PermeabilityFrontiers in physiology · 2019Article
- CaMKIIβ is localized in dendritic spines as both drebrin-dependent and drebrin-independent pools.Journal of neurochemistry · 2018Article
- Forecast of actin-binding proteins as the oncotarget in osteosarcoma - a review of mechanism, diagnosis and therapy.OncoTargets and therapy · 2018Review
- Catastrophic disassembly of actin filaments via Mical-mediated oxidation.Nature communications · 2017Article
- Microtubules Modulate F-actin Dynamics during Neuronal Polarization.Scientific reports · 2017Article
- Peptide regulation of cofilin activity in the CNS: A novel therapeutic approach for treatment of multiple neurological disorders.Pharmacology & therapeutics · 2017Review
- Effective expression of Drebrin in hippocampus improves cognitive function and alleviates lesions of Alzheimer's disease in APP (swe)/PS1 (ΔE9) mice.CNS neuroscience & therapeutics · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Molecular cross-talk between neuronal drebrin A and cofilin is believed to be a part of the activity-dependent cytoskeleton-modulating pathway in dendritic spines. Impairments in this pathway are implicated also in synaptic dysfunction in Alzheimer's disease, Down syndrome, epilepsy, and normal aging. However, up to now the molecular interplay between cofilin and drebrin has not been elucidated. TIRF microscopy and solution experiments revealed that full length drebrin A or its actin binding core (Drb1-300) inhibits, but do not abolish cofilin-induced severing of actin filaments. Cosedimentation experiments showed that F-actin can be fully occupied with combination of these two proteins. The dependence of cofilin binding on fractional saturation of actin filaments with drebrin suggests direct competition between these two proteins for F-actin binding. This implies that cofilin and drebrin can either overcome or reverse the allosteric changes in F-actin induced by the competitor's binding. The ability of cofilin to displace drebrin from actin filaments is pH dependent and is facilitated at acidic pH (6.8). Pre-steady state kinetic experiments reveal that both binding and dissociation of drebrin to/from actin filaments is faster than that reported for cooperative binding of cofilin. We found, that drebrin displacement by cofilin is greatly inhibited when actin severing is abolished, which might be linked to the cooperativity of drebrin binding to actin filaments. Our results contribute to molecular understanding of the competitive interactions of drebrin and cofilin with actin filaments.
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Registered trials
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.