Role anillinu v regulaci aktin-myosinové kontraktility

Hons Šliková, Pavlína

Actin-based contractility is essential for many cellular events, such as cytokinesis or cell polarization. Contraction of actin networks is typically driven by myosin motors that slide antiparallel actin filaments relative to each other. However, previous work showed that myosin is not the only protein capable of generating contractile forces. Anillin, an actin filament crosslinker present in the cortex and the cytokinetic ring, can also slide actin filaments, thereby generating contractile forces in the absence of myosin. While anillin interacts with both actin and myosin, its role in actomyosin contractility remains unclear. Here we show that in addition to the contractility of actin bundles in which the contraction involves antiparallel sliding, anillin also directly enhances myosin-driven contraction of single actin filaments. Using a minimal reconstituted system comprising actin filaments, anillin and myosin, we observed that with both myosin and anillin, single actin filaments robustly contract. By contrast, in the absence of anillin, myosin alone did not exert any conformational change of the individual filaments. Moreover, the observed contraction is concurrent with an increase in the landing rate and motor activity of myosin. We also show that single filament contractility, myosin landing rate and...

guest :: login Digital Repository
		Search		Submit		Help		About