Abstract
The cytoplasmic microtubules of eukaryotic cells participate in many fundamental processes, including mitosis, nerve growth and regeneration, the determination of cell shape, and the transport of organelles within cells (Dustin 1984). The assembly of microtubules from their major subunit proteins, tubulin αβ-dimers and microtubule-associated proteins (MAPs), is an entropically driven reaction favored by high temperatures and mediated by the release of structured water from sites of interdimer contact (Correia and Williams 1983). Thus, the microtubule proteins of homeotherms (e.g., mammals and birds) form micro-tubules at temperatures near 37 °C, and these “cold-labile” polymers disassemble at low temperatures (0–4 °C). By contrast, the microtubules of cold-living poikilotherms, such as those found in the Antarctic marine ecosystem, must assemble and function at temperatures as low as −1.9 °C. However, relatively little is known regarding the polymerization of microtubule proteins from organisms adapted to low body temperatures.
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© 1991 Springer-Verlag Berlin Heidelberg
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Detrich, H.W. (1991). Cold-Stable Microtubules from Antarctic Fish. In: di Prisco, G. (eds) Life Under Extreme Conditions. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76056-3_3
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DOI: https://doi.org/10.1007/978-3-642-76056-3_3
Publisher Name: Springer, Berlin, Heidelberg
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