Microtubules are well known to play a key role in the trafficking of neurotransmitters to the synapse. However, less attention has been paid to their role as downstream effectors of neurotransmitter signaling in the target neuron. Here, we show that neurotransmitter-based signaling to the microtubule cytoskeleton regulates downstream microtubule function through several mechanisms. These include tubulin posttranslational modification, binding of microtubule-associated proteins, release of microtubule-interacting second messenger molecules, and regulation of tubulin expression levels. We review the evidence for neurotransmitter regulation of the microtubule cytoskeleton, focusing on the neurotransmitters serotonin, melatonin, dopamine, glutamate, glycine, and acetylcholine. Some evidence suggests that microtubules may even play a more direct role in propagating action potentials through conductance of electric current. In turn, there is evidence for the regulation of neurotransmission by the microtubule cytoskeleton.
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http://dx.doi.org/10.1002/syn.20841 | DOI Listing |
Sci Transl Med
January 2025
Department of Cell Biology and Physiology, Washington University School of Medicine, Saint Louis, MO 63110, USA.
PNAS Nexus
January 2025
Department of Biochemistry, University of Geneva, 1211 Geneva, Switzerland.
The microtubule cytoskeleton is a dynamic network essential for many cellular processes, influenced by physicochemical factor, such as temperature, pH, dimer concentration, and ionic environment. In this study, we used in vitro reconstitution assays to examine the effects of four monovalent ions (Na, K, Cl, and Ac) on microtubule dynamics, uncovering distinct effects for each ion. Na was found to increase microtubule dynamicity by raising catastrophe frequency, polymerization and depolymerization speeds, and ultimately reducing microtubule lifetime by 80%.
View Article and Find Full Text PDFJ Biol Phys
January 2025
Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Science, Beijing, 100190, China.
Conventional kinesin protein is a prototypical biological molecular motor that can step processively on microtubules towards the plus end by hydrolyzing ATP molecules, performing the biological function of intracellular transports. An important characteristic of the kinesin is the load dependence of its velocity, which is usually measured by using the single molecule optical trapping method with a large-sized bead attached to the motor stalk. Puzzlingly, even for the same kinesin, some experiments showed that the velocity is nearly independent of the forward load whereas others showed that the velocity decreases evidently with the increase in the magnitude of the forward load.
View Article and Find Full Text PDFJ Eukaryot Microbiol
January 2025
Department of Botany, University of British Columbia, Vancouver, British Columbia, Canada.
Euglenids are flagellates with diverse modes of nutrition, including the photosynthetic Euglenophyceae, which acquired plastids via secondary endosymbiosis with green algae, and a diverse assemblage of predators of bacteria and other microeukaryotes. Most heterotrophic euglenids have never been cultivated, so their morphology remains poorly characterized and limited to only a few studies. "Ploeotids" are a paraphyletic group representing much of the diversity of heterotrophic euglenids and are characterized by their feeding apparatus and a rigid pellicle of 10-12 longitudinally arranged strips.
View Article and Find Full Text PDFUnlabelled: Melanin pigments block genotoxic agents by positioning on the sun-exposed side of human skin keratinocytes' nucleus. How this position is regulated and its role in genome photoprotection remains unknown. By developing a model of human keratinocytes internalizing extracellular melanin into pigment organelles, we show that keratin 5/14 intermediate filaments mechanically control the 3D perinuclear position of pigments, shielding DNA from photodamage.
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