The assembly and function of perinuclear actin cap in migrating cells
Jazyk angličtina Země Rakousko Médium print-electronic
Typ dokumentu časopisecké články, přehledy
PubMed
28101692
DOI
10.1007/s00709-017-1077-0
PII: 10.1007/s00709-017-1077-0
Knihovny.cz E-zdroje
- Klíčová slova
- Dorsal fibers, Focal adhesions, LINC, Perinuclear actin cap, Stress fibers, α-Actinin,
- MeSH
- aktin zastřešující proteiny metabolismus MeSH
- buněčné jádro metabolismus MeSH
- buněčný převod mechanických signálů fyziologie MeSH
- fokální adheze fyziologie MeSH
- jaderný obal metabolismus MeSH
- kontraktilní svazky fyziologie MeSH
- lidé MeSH
- pohyb buněk fyziologie MeSH
- polarita buněk fyziologie MeSH
- tvar buňky fyziologie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
- Názvy látek
- aktin zastřešující proteiny MeSH
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.
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