The assembly and function of perinuclear actin cap in migrating cells
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388971%3A_____%2F17%3A00474654" target="_blank" >RIV/61388971:_____/17:00474654 - isvavai.cz</a>
Výsledek na webu
<a href="http://dx.doi.org/10.1007/s00709-017-1077-0" target="_blank" >http://dx.doi.org/10.1007/s00709-017-1077-0</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/s00709-017-1077-0" target="_blank" >10.1007/s00709-017-1077-0</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
The assembly and function of perinuclear actin cap in migrating cells
Popis výsledku v původním jazyce
Stress fibers are actin bundles encompassing actin filaments, actin-crosslinking, and actin-associated proteins that represent the major contractile system in the cell. Different types of stress fibers assemble in adherent cells, and they are central to diverse cellular processes including establishment of the cell shape, morphogenesis, cell polarization, and migration. Stress fibers display specific cellular organization and localization, with ventral fibers present at the basal side, and dorsal fibers and transverse actin arcs rising at the cell front from the ventral to the dorsal side and toward the nucleus. Perinuclear actin cap fibers are a specific subtype of stress fibers that rise from the leading edge above the nucleus and terminate at the cell rear forming a dome-like structure. Perinuclear actin cap fibers are fixed at three points: both ends are anchored in focal adhesions, while the central part is physically attached to the nucleus and nuclear lamina through the linker of nucleoskeleton and cytoskeleton (LINC) complex. Here, we discuss recent work that provides new insights into the mechanism of assembly and the function of these actin stress fibers that directly link extracellular matrix and focal adhesions with the nuclear envelope.
Název v anglickém jazyce
The assembly and function of perinuclear actin cap in migrating cells
Popis výsledku anglicky
Stress fibers are actin bundles encompassing actin filaments, actin-crosslinking, and actin-associated proteins that represent the major contractile system in the cell. Different types of stress fibers assemble in adherent cells, and they are central to diverse cellular processes including establishment of the cell shape, morphogenesis, cell polarization, and migration. Stress fibers display specific cellular organization and localization, with ventral fibers present at the basal side, and dorsal fibers and transverse actin arcs rising at the cell front from the ventral to the dorsal side and toward the nucleus. Perinuclear actin cap fibers are a specific subtype of stress fibers that rise from the leading edge above the nucleus and terminate at the cell rear forming a dome-like structure. Perinuclear actin cap fibers are fixed at three points: both ends are anchored in focal adhesions, while the central part is physically attached to the nucleus and nuclear lamina through the linker of nucleoskeleton and cytoskeleton (LINC) complex. Here, we discuss recent work that provides new insights into the mechanism of assembly and the function of these actin stress fibers that directly link extracellular matrix and focal adhesions with the nuclear envelope.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10606 - Microbiology
Návaznosti výsledku
Projekt
<a href="/cs/project/GA13-06405S" target="_blank" >GA13-06405S: Úloha signální dráhy ERK-RSK při tranzici z epiteliálního na mezenchymální fenotyp.</a><br>
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Protoplasma
ISSN
0033-183X
e-ISSN
—
Svazek periodika
254
Číslo periodika v rámci svazku
3
Stát vydavatele periodika
AT - Rakouská republika
Počet stran výsledku
12
Strana od-do
1207-1218
Kód UT WoS článku
000399037400008
EID výsledku v databázi Scopus
2-s2.0-85009802402