Mechanics of blunting of actin-myosin interaction dynamics by the actinopathy-causing mutation E334Q in cytoskeletal γ-actin.

ABSTRACT: Cellular processes such as cytokinesis, apoptosis and migration rely heavily on the myosin-based contractility of the γ-actin network in the submembrane cortex. Direct measurements of γ-actin-myosin interactions through morphological and depletion investigations remain elusive. Here, we use a synthetic nanomachine, consisting of an array of myosin motors carried on a nanopositioner and brought to interact with an actin filament attached to a bead trapped in the focus of dual laser optical tweezers. The nanomachine is able to mimic the loading conditions of γ-actin-myosin interactions in situ, allowing measurements of the maximum steady force (F₀) and of the shortening velocity against loads < F₀. Comparative measurements are conducted on wild-type γ-actin and γ-actin

SUBMITTER: Pertici I 

PROVIDER: S-EPMC12783979 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature