Abstract
The heterodimeric actin capping protein (CP) is regulated by a set of proteins with CP-interacting (CPI) motifs. These proteins are largely unrelated and distinct, outside of their CPI-motif. The CPI-motifs within a given protein family are conserved, compared to those of proteins in other families. We compared the ability of CPI-motifs from different protein families to bind to CP, to allosterically inhibit barbed-end capping by CP, and to allosterically inhibit interaction with V-1, another regulator of CP.
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