Abstract
Cells face the enormous challenge of generating a single phenotype that must be coherent with myriad internal and external conditions. For such phenotypes to have multifarious but meaningful outputs entails the sensing, and integration of a wide variety of chemical and physical information, hence the coordination of metabolic and signaling processes. This sensing, integration, and coordination are carried out by the complex ultrastructural arrays and moonlighting functions of the cytoskeletal network. In the cellular context, the direction and potency of sensing are determined by the structure-related responses of the cytoskeletal network to the activity of individual macromolecules in conjunction with associated metabolites and nucleotides. These responses comprise the binding (hetero-association) of these macromolecules to the cytoskeleton and the consequences of this binding on the behavior of both partners, among them the stability and dynamics of the cytoskeleton, and the catalytic and regulatory properties of the individual proteins (and/or their specific complexes). The latter is of specific importance in regulation at a high level of organization via the formation of microcompartments in linear pathways or at metabolic crossroads. In addition, key players in many metabolic and signaling pathways are nucleotides such as ATP and GTP that have a crucial role in cytoskeleton-mediated events. These issues are illustrated with examples, and the sensing power of dynamic macromolecular associations is discussed.
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Acknowledgments
This work was supported by the European Commission (DCI-ALA/19.09.01/10/21526/245-297/ALFA 111(2010)29), the Hungarian National Scientific Research Fund Grants OTKA (T-101039), and Richter Gedeon Research Grant (RG-IPI-2011/TP5-001) to J. Ovádi.
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Ovádi, J., Norris, V. (2014). Moonlighting Function of the Tubulin Cytoskeleton: Macromolecular Architectures in the Cytoplasm. In: Aon, M., Saks, V., Schlattner, U. (eds) Systems Biology of Metabolic and Signaling Networks. Springer Series in Biophysics, vol 16. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-38505-6_7
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