The organization and regulation of the macrophage actin skeleton

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Abstract
To move, leukocytes extend portions of their cortical cytoplasm as pseudopods. These pseudopods are filled with a three‐dimensional actin filament skeleton, the reversible assembly of which in response to receptor stimulation is thought to play a major role in providing the mechanical force for these protrusive movements. The organization of this actin skeleton occurs at different levels within the cell, and a number of macrophage proteins have been isolated and shown to affect the architecture, assembly, stability, and length of actin filaments in vitro. The architecture of cytoplasmic actin is regulated by proteins that cross‐link filaments in higher‐order structures. Actin‐binding protein plays a major role in defining network structure by cross‐linking actin filaments into orthogonal networks. Gelsolin may have a central role in regulating network structure. It binds to the sides of actin filaments and severs them, and binds the “barbed” filament end, thereby blocking monomer addition at this end. Gelsolin is activated to bind actin filaments by μM calcium. Dissociation of gelsolin bound on filament ends occurs in the presence of the polyphosphoinositides, PIP and PIP2. Calcium and PIP2 have been shown to be intracellular messengers of cell stimulation.