Hsp90 binds microtubules and is involved in the reorganization of microtubular network in angiosperms
Abstrakt
Microtubules (MTs) are essential for many processes in plant cells. Microtubule-associated proteins (MAPs) influence microtubule polymerization dynamics and enable them to perform their functions.
Molecular chaperone Hsp90 has been shown to associate with MTs in animal and plant cells. However, the role of Hsp90-MT binding in plants has not yet been investigated.
Herein we show that Hsp90 associates with cortical MTs in tobacco cells and decorates MTs in phragmoplast. Further we show that tobacco Hsp90_MT binds directly to polymerized microtubules in vitro.
The inhibition of Hsp90 by geldanamycin impaires severely MT re-assembly after cold-induced de-polymerization. Our results indicate that the plant Hsp90 interaction with MTs plays a key role in cellular events, where MT re-organization is needed.