ArticleFrontiers in cellular neuroscience2017
Developmental Profiling of Tropomyosin Expression in Mouse Brain Reveals Tpm4.2 as the Major Post-synaptic Tropomyosin in the Mature Brain.
Article in Frontiers in cellular neuroscience, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Alterations of actin in aging.Journal of cell science · 2026Review
- Knock-out of Tpm4.2/Actin Filaments Alters Neuronal Signaling, Neurite Outgrowth, and Behavioral Phenotypes in Mice.Molecular neurobiology · 2025Article
- Role of Tpm Isoforms Produced by theBiomolecules · 2025Article
- Proteomic changes in the hippocampus of large mammals after total-body low dose radiation.PloS one · 2024Article
- Synaptic tau: A pathological or physiological phenomenon?Acta neuropathologica communications · 2021Review
- Overexpression of Tropomyosin Isoform Tpm3.1 Does Not Alter Synaptic Function in Hippocampal Neurons.International journal of molecular sciences · 2021Article
- Deletion of the Actin-Associated TropomyosinCells · 2021Article
- Actin-tropomyosin distribution in non-muscle cells.Journal of muscle research and cell motility · 2020Review
- TPM4 promotes cell migration by modulating F-actin formation in lung cancer.OncoTargets and therapy · 2019Article
- Tropomodulin's Actin-Binding Abilities Are Required to Modulate Dendrite Development.Frontiers in molecular neuroscience · 2018Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nerve cell connections, formed in the developing brain of mammals, undergo a well-programmed process of maturation with changes in their molecular composition over time. The major structural element at the post-synaptic specialization is the actin cytoskeleton, which is composed of different populations of functionally distinct actin filaments. Previous studies, using ultrastructural and light imaging techniques have established the presence of different actin filament populations at the post-synaptic site. However, it remains unknown, how these different actin filament populations are defined and how their molecular composition changes over time. In the present study, we have characterized changes in a core component of actin filaments, the tropomyosin (Tpm) family of actin-associated proteins from embryonal stage to the adult stage. Using biochemical fractionation of mouse brain tissue, we identified the tropomyosin Tpm4.2 as the major post-synaptic Tpm. Furthermore, we found age-related differences in the composition of Tpms at the post-synaptic compartment. Our findings will help to guide future studies that aim to define the functional properties of actin filaments at different developmental stages in the mammalian brain.
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