ArticleBMC cell biology2009
The proline-rich domain of tau plays a role in interactions with actin.
Article in BMC cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
72 citing papers in PubMed, 1 synthesis or guideline pooled it, 130 citations in OpenAlex.
- Microneedling with Topical Insulin Versus Microneedling with Platelet-rich Plasma for Post-Acne Scars: A Systematic Review and Meta-Analysis with Trial Sequential Analysis.Aesthetic plastic surgery · 2026Pooled it
- Engineering Design of Artificial Phase-Separating Proteins.Biotechnology journal · 2026Review
- Evaluating MAPT p.A152T as a risk factor for the 3R tauopathy Pick's disease.Brain communications · 2026Article
- Elevation of the mechanically-sensitive protein emerin links nuclear mechanotransduction to tau-induced cytoskeletal remodeling in neurons.bioRxiv : the preprint server for biology · 2025Article
- Subcellular functions of tau mediate repair response and synaptic homeostasis in injury.Molecular psychiatry · 2025Article
- Design and Characterization of a Dual-Protein Strategy for an Early-Stage Assay of Ovarian Cancer Biomarker Lysophosphatidic Acid.Biosensors · 2024Article
- TBI and Tau Loss of Function Both Affect Naïve Ethanol Sensitivity inInternational journal of molecular sciences · 2024Article
- Bsp1, a fungal CPI motif protein, regulates actin filament capping in endocytosis and cytokinesis.Molecular biology of the cell · 2024Article
- Alzheimer's disease and related tauopathies: disorders of disrupted neuronal identity.Trends in neurosciences · 2023Review
- An Atypical F-Actin Capping Protein Modulates Cytoskeleton Behaviors Crucial for Trichomonas vaginalis Colonization.Microbiology spectrum · 2023Article
- Tau, microtubule dynamics, and axonal transport: New paradigms for neurodegenerative disease.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Pathogenic tau decreases nuclear tension in cultured neurons.Frontiers in aging · 2023Article
- Tau Isoforms: Gaining Insight intoInternational journal of molecular sciences · 2022Review
- Review
- Effects of Chronic Arginase Inhibition with Norvaline on Tau Pathology and Brain Glucose Metabolism in Alzheimer's Disease Mice.Neurochemical research · 2022Article
- What's in a Gene? The Outstanding Diversity ofCells · 2022Review
- Novel genetic variants in MAPT and alterations in tau phosphorylation in amyotrophic lateral sclerosis post-mortem motor cortex and cerebrospinal fluid.Brain pathology (Zurich, Switzerland) · 2022Article
- Microtubule-associated protein tau in murine kidney: role in podocyte architecture.Cellular and molecular life sciences : CMLS · 2022Article
- Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021Review
- Tau Protein Interaction Partners and Their Roles in Alzheimer's Disease and Other Tauopathies.International journal of molecular sciences · 2021Review
12 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe microtubule-associated protein tau is able to interact with actin and serves as a cross-linker between the microtubule and actin networks. The microtubule-binding domain of tau is known to be involved in its interaction with actin. Here, we address the question of whether the other domains of tau also interact with actin.
resultsSeveral tau truncation and deletion mutants were constructed, namely N-terminal region (tauN), proline-rich domain (tauPRD), microtubule binding domain (tauMTBD) and C-terminal region (tauC) truncation mutants, and microtubule binding domain (tauDeltaMTBD) and proline-rich domain/microtubule binding domain (tauDeltaPRD&MTBD) deletion mutants. The proline-rich domain truncation mutant (tauPRD) and the microtubule binding domain deletion mutant (tauDeltaMTBD) promoted the formation of actin filaments. However, actin assembly was not observed in the presence of the N-terminal and C-terminal truncation mutants. These results indicate that the proline-rich domain is involved in the association of tau with G-actin. Furthermore, results from co-sedimentation, solid phase assays and electron microscopy showed that the proline-rich domain is also capable of binding to F-actin and inducing F-actin bundles. Using solid phase assays to analyze apparent dissociation constants for the binding of tau and its mutants to F-actin resulted in a sequence of affinity for F-actin: tau >> microtubule binding domain > proline-rich domain. Moreover, we observed that the proline-rich domain was able to associate with and bundle F-actin at physiological ionic strength.
conclusionThe proline-rich domain is a functional structure playing a role in the association of tau with actin. This suggests that the proline-rich domain and the microtubule-binding domain of tau are both involved in binding to and bundling F-actin.
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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.