Abstract:
:Dynamic remodelling of actin stress fibres (SFs) allows non-muscle cells to adapt to applied forces such as uniaxial cell shortening. However, the mechanism underlying rapid and selective disassembly of SFs oriented in the direction of shortening remains to be elucidated. Here, we investigated how myosin crossbridge cycling induced by MgATP is associated with SF disassembly. Moderate concentrations of MgATP, or [MgATP], induced SF contraction. Meanwhile, at [MgATP] slightly higher than the physiological level, periodic actin patterns emerged along the length of SFs and dispersed within seconds. The actin fragments were diverse in length, but comparable to those in characteristic sarcomeric units of SFs. These results suggest that MgATP-bound non-muscle myosin II dissociates from the individual actin filaments that constitute the sarcomeric units, resulting in unbundling-induced disassembly rather than end-to-end actin depolymerization. This rapid SF disassembly occurred independent of dephosphorylation of myosin light chain. In terms of effects on actin-myosin interactions, a rise in [MgATP] is functionally equivalent to a temporal decrease in the total number of actin-myosin crossbridges. Actin-myosin crossbridges are known to be reduced by an assisting load on myosin. Thus, the present study suggests that reducing the number of actin-myosin crossbridges promotes rapid and orientation-dependent disassembly of SFs after cell shortening.
journal_name
Interface Focusjournal_title
Interface focusauthors
Matsui TS,Kaunas R,Kanzaki M,Sato M,Deguchi Sdoi
10.1098/rsfs.2011.0031subject
Has Abstractpub_date
2011-10-06 00:00:00pages
754-66issue
5eissn
2042-8898issn
2042-8901pii
rsfs20110031journal_volume
1pub_type
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