Regulators of actin filament barbed ends at a glance

• Published in: Journal of cell science Vol. 129; no. 6; pp. 1085 - 1091
• Main Authors: Shekhar, Shashank, Pernier, Julien, Carlier, Marie-France
• Format: Journal Article
• Language: English
• Published: England Company of Biologists 15.03.2016
• Subjects: Actin Cytoskeleton - genetics; Actin Cytoskeleton - metabolism; Actins - genetics; Actins - metabolism; Animals; Cytoskeleton - genetics; Cytoskeleton - metabolism; Humans; Life Sciences; Motility; Filament barbed end; Profilin; Actin assembly; Formin; Capping protein
• ISSN: 0021-9533; 1477-9137
• DOI: 10.1242/jcs.179994

Cells respond to external stimuli by rapidly remodeling their actin cytoskeleton. At the heart of this function lies the intricately controlled regulation of individual filaments. The barbed end of an actin filament is the hotspot for the majority of the biochemical reactions that control filament assembly. Assays performed in bulk solution and with single filaments have enabled characterization of a plethora of barbed-end-regulating proteins. Interestingly, many of these regulators work in tandem with other proteins, which increase or decrease their affinity for the barbed end in a spatially and temporally controlled manner, often through simultaneous binding of two regulators at the barbed ends, in addition to standard mutually exclusive binding schemes. In this Cell Science at a Glance and the accompanying poster, we discuss key barbed-end-interacting proteins and the kinetic mechanisms by which they regulate actin filament assembly. We take F-actin capping protein, gelsolin, profilin and barbed-end-tracking polymerases, including formins and WH2-domain-containing proteins, as examples, and illustrate how their activity and competition for the barbed end regulate filament dynamics.