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• W2067671380 startingPage "1329" @default.
• W2067671380 abstract "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." @default.
• W2067671380 created "2016-06-24" @default.
• W2067671380 creator A5046546216 @default.
• W2067671380 creator A5050970188 @default.
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• W2067671380 creator A5064797948 @default.
• W2067671380 date "2012-09-01" @default.
• W2067671380 modified "2023-10-16" @default.
• W2067671380 title "Hsp90 binds microtubules and is involved in the reorganization of the microtubular network in angiosperms" @default.
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• W2067671380 doi "https://doi.org/10.1016/j.jplph.2012.06.010" @default.
• W2067671380 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/22840326" @default.
• W2067671380 hasPublicationYear "2012" @default.
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