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JCS ePress online publication date 9 Mar 2004
doi: 10.1242/jcs.01021

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Research Article

{alpha}B-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassembly


Yoshinobu Fujita, Eri Ohto, Eisaku Katayama, and Yoriko Atomi*
* Author for correspondence (e-mail: atomi{at}idaten.c.u-tokyo.ac.jp)

{alpha}B-Crystallin, one of the small heat-shock proteins, is constitutively expressed in various tissues including the lens of the eye. It has been suggested that {alpha}B-crystallin provides lens transparency but its function in nonlenticular tissues is unknown. It has been reported that {alpha}B-crystallin is involved in the stabilization and the regulation of cytoskeleton, such as intermediate filaments and actin. In this study, we investigate the possibility whether {alpha}B-crystallin interacts with the third cytoskeleton component, microtubules (MTs). First, we precisely observed the cellular localization of {alpha}B-crystallin and MT networks in L6E9 myoblast cells and found a striking coincidence between them. MTs reconstituted from cell lysate contained {alpha}B-crystallin. Electron micrographs clearly showed direct interactions of purified {alpha}B-crystallin with the surface of microtubule-associated proteins (MAPs) attached to MTs. Purified {alpha}B-crystallin bound to MAP-MTs in a concentration-dependent manner. However, {alpha}B-crystallin did not bind MTs reconstituted from purified tubulin. Finally, we observed that {alpha}B-crystallin increased the resistance of MTs to depolymerization in cells and in vitro. Taken together, these results suggest that one of the functions of {alpha}B-crystallin is to bind MTs via MAP(s) and to give the MTs resistance to disassembly.
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