Arp2/3 complex subunit ARPC2 binds to microtubules

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F15%3A10315431" target="_blank" >RIV/00216208:11310/15:10315431 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.plantsci.2015.10.001" target="_blank" >http://dx.doi.org/10.1016/j.plantsci.2015.10.001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.plantsci.2015.10.001" target="_blank" >10.1016/j.plantsci.2015.10.001</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Arp2/3 complex subunit ARPC2 binds to microtubules

Popis výsledku v původním jazyce

Arp2/3 complex plays a fundamental role in the nucleation of actin filaments (AFs) in yeasts, plants, and animals. In plants, the aberrant shaping and elongation of several types of epidermal cells observed in Arp2/3 complex knockout plant mutants suggest the importance of Arp2/3-mediated actin nucleation for various morphogenetic processes. Here we show that ARPC2, a core Arp2/3 complex subunit, interacts with both actin filaments (AFs) and microtubules (MTs). Plant GFP-ARPC2 expressed in Nicotiana tabacum BY-2 cells, leaf epidermal cells of Nicotiana benthamiana and root epidermal cells of Arabidopsis thaliana decorated MTs. The interaction with MTs was demonstrated by pharmacological approach selectively interfering with either AFs or MTs dynamics as well as by the in vitro cosedimentation assays. A putative MT-binding domain of tobacco NtARPC2 protein was identified using the co-sedimentation of several truncated NtARPC2 proteins with MTs. Newly identified MT-binding ability of ARP

Název v anglickém jazyce

Arp2/3 complex subunit ARPC2 binds to microtubules

Popis výsledku anglicky

Arp2/3 complex plays a fundamental role in the nucleation of actin filaments (AFs) in yeasts, plants, and animals. In plants, the aberrant shaping and elongation of several types of epidermal cells observed in Arp2/3 complex knockout plant mutants suggest the importance of Arp2/3-mediated actin nucleation for various morphogenetic processes. Here we show that ARPC2, a core Arp2/3 complex subunit, interacts with both actin filaments (AFs) and microtubules (MTs). Plant GFP-ARPC2 expressed in Nicotiana tabacum BY-2 cells, leaf epidermal cells of Nicotiana benthamiana and root epidermal cells of Arabidopsis thaliana decorated MTs. The interaction with MTs was demonstrated by pharmacological approach selectively interfering with either AFs or MTs dynamics as well as by the in vitro cosedimentation assays. A putative MT-binding domain of tobacco NtARPC2 protein was identified using the co-sedimentation of several truncated NtARPC2 proteins with MTs. Newly identified MT-binding ability of ARP

Druh

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

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

—

Projekt

<a href="/cs/project/LO1417" target="_blank" >LO1417: Centrum experimentální biologie rostlin UK</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2015

Kód důvěrnosti údajů

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

Název periodika

Plant Science

ISSN

0168-9452

e-ISSN

—

Svazek periodika

241

Číslo periodika v rámci svazku

December 2015

Stát vydavatele periodika

IE - Irsko

Počet stran výsledku

13

Strana od-do

96-108

Kód UT WoS článku

000367487500010

EID výsledku v databázi Scopus

2-s2.0-84944452065