The effect of S‐100a and S‐100b proteins and Zn2+ on the assembly of brain microtubule proteins in vitro

FEBS Letters

Rosengren, Lars²  Briving, Carin²  Gerard, Dominique³  Baudier, Jacques³  Wallin, Margareta¹  Deinum, Johanna²  Haglid, Kenneth² 

[1]Department of Zoophysiology, University of Göteborg, PO Box 330 31, S-400 33 Göteborg, Sweden

[2]Department of Medical Physics, University of Göteborg, PO Box 330 31, S-400 33 Göteborg, Sweden

[3]Laboratoire de Physique, UER des Sciences Pharmaceutiques, BP no. 10, 67048 Strasbourg Cédex, France

关键词: Microtubule assembly;    Tubulin;    S-100 protein;    Calmodulin;    Zn2+ regulation;   

DOI  :  10.1016/0014-5793(83)80837-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The homologous proteins S-100a and S-100b affect the microtubule system in a distinctly different way in the presence of low molar ratios of Zn²⁺. Assembly of brain microtubule proteins can be almost completely inhibited and rapid disassembly can be induced by low molar amounts of S-100b in the presence of low molar ratios [2–4] of Zn²⁺. Higher molar ratios per S-100b (>4) potentiate the general Zn²⁺ effect, promoting the formation of sheets of microtubules. However, the effect of S-100a is quite different, no inhibition of assembly can be observed and the presence of S-100a seems to protect the microtubule proteins against the effect of Zn²⁺ by chelating the Zn²⁺ and decreasing the free metal-ion concentration. S-100a or S-100b cannot bind to the microtubule polymer-form, either in the absence or in the presence of Zn²⁺.

【 授权许可】

Unknown