Profilin connects actin assembly with microtubule dynamics
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F16%3A00473129" target="_blank" >RIV/68378050:_____/16:00473129 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1091/mbc.E15-11-0799" target="_blank" >http://dx.doi.org/10.1091/mbc.E15-11-0799</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1091/mbc.E15-11-0799" target="_blank" >10.1091/mbc.E15-11-0799</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Profilin connects actin assembly with microtubule dynamics
Popis výsledku v původním jazyce
Profilin controls actin nucleation and assembly processes in eukaryotic cells. Actin nucleation and elongation promoting factors (NEPFs) such as Ena/VASP, formins, and WASP-family proteins recruit profilin: actin for filament formation. Some of these are found to be microtubule associated, making actin polymerization from microtubule-associated platforms possible. Microtubules are implicated in focal adhesion turnover, cell polarity establishment, and migration, illustrating the coupling between actin and microtubule systems. Here we demonstrate that profilin is functionally linked to microtubules with formins and point to formins as major mediators of this association. To reach this conclusion, we combined different fluorescence microscopy techniques, including superresolution microscopy, with siRNA modulation of profilin expression and drug treatments to interfere with actin dynamics. Our studies show that profilin dynamically associates with microtubules and this fraction of profilin contributes to balance actin assembly during homeostatic cell growth and affects microtubule dynamics. Hence profilin functions as a regulator of microtubule (+)-end turnover in addition to being an actin control element.
Název v anglickém jazyce
Profilin connects actin assembly with microtubule dynamics
Popis výsledku anglicky
Profilin controls actin nucleation and assembly processes in eukaryotic cells. Actin nucleation and elongation promoting factors (NEPFs) such as Ena/VASP, formins, and WASP-family proteins recruit profilin: actin for filament formation. Some of these are found to be microtubule associated, making actin polymerization from microtubule-associated platforms possible. Microtubules are implicated in focal adhesion turnover, cell polarity establishment, and migration, illustrating the coupling between actin and microtubule systems. Here we demonstrate that profilin is functionally linked to microtubules with formins and point to formins as major mediators of this association. To reach this conclusion, we combined different fluorescence microscopy techniques, including superresolution microscopy, with siRNA modulation of profilin expression and drug treatments to interfere with actin dynamics. Our studies show that profilin dynamically associates with microtubules and this fraction of profilin contributes to balance actin assembly during homeostatic cell growth and affects microtubule dynamics. Hence profilin functions as a regulator of microtubule (+)-end turnover in addition to being an actin control element.
Klasifikace
Druh
J<sub>x</sub> - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)
CEP obor
EB - Genetika a molekulární biologie
OECD FORD obor
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Návaznosti výsledku
Projekt
<a href="/cs/project/GA16-25159S" target="_blank" >GA16-25159S: Úloha vápníku v regulaci mikrotubulů aktivovaných žírných buněk</a><br>
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2016
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Molecular Biology of the Cell
ISSN
1059-1524
e-ISSN
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Svazek periodika
27
Číslo periodika v rámci svazku
15
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
13
Strana od-do
2381-2393
Kód UT WoS článku
000380825800005
EID výsledku v databázi Scopus
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