Hsp90 binds microtubules and is involved in the reorganization of microtubular network in angiosperms

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F12%3A10124872" target="_blank" >RIV/00216208:11310/12:10124872 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S0176161712002866" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0176161712002866</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.jplph.2012.06.010" target="_blank" >10.1016/j.jplph.2012.06.010</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Hsp90 binds microtubules and is involved in the reorganization of microtubular network in angiosperms

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Hsp90 binds microtubules and is involved in the reorganization of microtubular network in angiosperms

Popis výsledku anglicky

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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)<br>S - Specificky vyzkum na vysokych skolach<br>I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2012

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Plant Physiology

ISSN

0176-1617

e-ISSN

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Svazek periodika

169

Číslo periodika v rámci svazku

14

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

1329-1339

Kód UT WoS článku

000310407800001

EID výsledku v databázi Scopus

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