Abstract
Microtubules are a major component of the cytoskeleton of most eukaryotic cells. They participate in many fundamental processes, including mitosis, nerve growth and regeneration, the intracellular transport of organelles, and the determination of cell shape. The formation of microtubules from their subunit proteins, tubulin αβ dimers and microtubule-associated proteins (MAPs), is an entropically driven process that is favored by high temperatures (Correia and Williams 1983). For example, the microtubule proteins of mammals and birds polymerize to yield microtubules at temperatures near 37 °C, but these polymers are “cold-labile”; they disassemble to their subunits at low temperatures (0–4 °C). How, then, do the microtubules of cold-living poikilotherms (e.g., the fish of the antarctic marine ecosystem) assemble and function at body temperatures as low as −1.9 °C?
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© 1991 Springer-Verlag Berlin Heidelberg
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Detrich, H.W. (1991). Polymerization of Microtubule Proteins from Antarctic Fish. In: di Prisco, G., Maresca, B., Tota, B. (eds) Biology of Antarctic Fish. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76217-8_17
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DOI: https://doi.org/10.1007/978-3-642-76217-8_17
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