QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 9 March 2004
doi: 10.1242/jcs.01021

This Article Figures Only Full Text Full Text (PDF) All Versions of this Article: jcs.01021v1 117/9/1719    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Fujita, Y. Articles by Atomi, Y. Search for Related Content PubMed PubMed Citation Articles by Fujita, Y. Articles by Atomi, Y.

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

Yoshinobu Fujita^1,*, Eri Ohto¹, Eisaku Katayama² and Yoriko Atomi^1,*,

¹ Department of Life Sciences, The Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1, Komaba, Meguro-ku, Tokyo 153-8902, Japan
² Division of Biomolecular Imaging, Institute of Medical Science, The University of Tokyo, 4-6-1, Shiroganedai, Minato-ku, Tokyo 108-8639, Japan

Author for correspondence (e-mail: atomi{at}idaten.c.u-tokyo.ac.jp)

Accepted 27 November 2003

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 B-crystallin provides lens transparency but its function in nonlenticular tissues is unknown. It has been reported that 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 B-crystallin interacts with the third cytoskeleton component, microtubules (MTs). First, we precisely observed the cellular localization of B-crystallin and MT networks in L6E9 myoblast cells and found a striking coincidence between them. MTs reconstituted from cell lysate contained B-crystallin. Electron micrographs clearly showed direct interactions of purified B-crystallin with the surface of microtubule-associated proteins (MAPs) attached to MTs. Purified B-crystallin bound to MAP-MTs in a concentration-dependent manner. However, B-crystallin did not bind MTs reconstituted from purified tubulin. Finally, we observed that 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 B-crystallin is to bind MTs via MAP(s) and to give the MTs resistance to disassembly.

Key words: Tubulin, sHSP, Cytoskeleton, Chaperone

This article has been cited by other articles:

				T. Yamaguchi, H. Arai, N. Katayama, T. Ishikawa, K. Kikumoto, and Y. Atomi Age-Related Increase of Insoluble, Phosphorylated Small Heat Shock Proteins in Human Skeletal Muscle J. Gerontol. A Biol. Sci. Med. Sci., May 1, 2007; 62(5): 481 - 489. [Abstract] [Full Text] [PDF]

				A. Oguro, T. Sakurai, Y. Fujita, S. Lee, H. Kubota, K. Nagata, and Y. Atomi The molecular chaperone HSP47 rapidly senses gravitational changes in myoblasts Genes Cells, November 1, 2006; 11(11): 1253 - 1265. [Abstract] [Full Text] [PDF]

				J.-h. Xi, F. Bai, R. McGaha, and U. P. Andley Alpha-crystallin expression affects microtubule assembly and prevents their aggregation FASEB J, May 1, 2006; 20(7): 846 - 857. [Abstract] [Full Text] [PDF]

				J. den Engelsman, D. Gerrits, W. W. de Jong, J. Robbins, K. Kato, and W. C. Boelens Nuclear Import of {alpha}B-crystallin Is Phosphorylation-dependent and Hampered by Hyperphosphorylation of the Myopathy-related Mutant R120G J. Biol. Chem., November 4, 2005; 280(44): 37139 - 37148. [Abstract] [Full Text] [PDF]

				M. S. Kumar, M. Kapoor, S. Sinha, and G. B. Reddy Insights into Hydrophobicity and the Chaperone-like Function of {alpha}A- and {alpha}B-crystallins: AN ISOTHERMAL TITRATION CALORIMETRIC STUDY J. Biol. Chem., June 10, 2005; 280(23): 21726 - 21730. [Abstract] [Full Text] [PDF]