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Hsp90 binds microtubules and is involved in the reorganization of the microtubular network in angiosperms
J. Krtková, A. Zimmermann, K. Schwarzerová, P. Nick,
Language English Country Germany
Document type Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Benzoquinones pharmacology MeSH
- Phylogeny MeSH
- Lactams, Macrocyclic pharmacology MeSH
- Microtubules drug effects metabolism MeSH
- Molecular Sequence Data MeSH
- Polymerization drug effects MeSH
- HSP90 Heat-Shock Proteins chemistry isolation & purification metabolism MeSH
- Recombinant Proteins isolation & purification metabolism MeSH
- Repetitive Sequences, Amino Acid MeSH
- Plant Proteins metabolism MeSH
- Oryza drug effects metabolism MeSH
- Amino Acid Sequence MeSH
- Nicotiana cytology drug effects metabolism MeSH
- Protein Transport drug effects MeSH
- Tubulin metabolism MeSH
- Protein Binding drug effects MeSH
- Green Fluorescent Proteins metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
Microtubules (MTs) are essential for many processes in plant cells. MT-associated proteins (MAPs) influence MT polymerization dynamics and enable them to perform their functions. The 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. Here, we show that Hsp90 associates with cortical MTs in tobacco cells and decorates MTs in the phragmoplast. Further, we show that tobacco Hsp90_MT binds directly to polymerized MTs in vitro. The inhibition of Hsp90 by geldanamycin (GDA) severely impairs 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.
References provided by Crossref.org
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- $a Krtková, Jana $u Department of Experimental Plant Biology, Charles University in Prague, Viničná 5, 128 44 Prague 2, Czech Republic. akcni.krtecek@post.cz
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- $a Microtubules (MTs) are essential for many processes in plant cells. MT-associated proteins (MAPs) influence MT polymerization dynamics and enable them to perform their functions. The 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. Here, we show that Hsp90 associates with cortical MTs in tobacco cells and decorates MTs in the phragmoplast. Further, we show that tobacco Hsp90_MT binds directly to polymerized MTs in vitro. The inhibition of Hsp90 by geldanamycin (GDA) severely impairs 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.
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