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Updated: Aug 24, 2026

Reconstitution of Actin-Based Motility with Commercially Available Proteins
Published on: October 28, 2022
Actin-related protein 1 and cytoplasmic dynein-based motility - what's the connection?
T A Schroer1, J B Bingham, S R Gill
1Dept of Biology, The Johns Hopkins University, Baltimore, MD 21218, USA.
Abstract:
The actin-related protein Arp1 works in conjunction with the microtubule-based motor cytoplasmic dynein to drive many types of intracellular motility. In vertebrate cells, Arp1 is present exclusively in the form of a 37-nm filament that constitutes the backbone of dynactin, a 1.2-MDa macromolecular complex containing nine other polypeptides. Dynactin has been proposed to function as the link between dynein and its cargo. Recent work indicates that the dynactin subunit p150(Glued) mediates the interaction of the dynactin molecule with dynein and microtubules, leaving the Arp1 filament as a possible cargo-binding domain. Mechanisms for binding of F-actin to membranes are discussed as models of the Arp1-membrane interaction.
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