Key result
The conserved core of formin homology domains 1 and 2 of Bni1p nucleates unbranched actin filaments in vitro and remains associated with the growing barbed ends.
Formins directly nucleate unbranched actin filaments and remain associated with growing barbed ends, suggesting a role in regulating nucleation and polarization of actin structures.
Formin nucleation of unbranched filaments identified in vitro; leaves open physiological roles in actin dynamics.
Nucleation of branched actin filaments by the Arp2/3 complex is a conserved process in eukaryotic cells, yet the source of unbranched actin filaments has remained obscure. In yeast, formins stimulate assembly of actin cables independently of Arp2/3. Here, the conserved core of formin homology domains 1 and 2 of Bni1p (Bni1pFH1FH2) was found to nucleate unbranched actin filaments in vitro. Bni1pFH2 provided the minimal region sufficient for nucleation. Unique among actin nucleators, Bni1pFH1FH2 remained associated with the growing barbed ends of filaments. This combination of properties suggests a direct role for formins in regulating nucleation and polarization of unbranched filamentous actin structures.
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Pruyne et al. (2002) studied this question. Bni1pFH1FH2 was evaluated on Nucleation of unbranched actin filaments and association with barbed ends. The conserved core of formin homology domains 1 and 2 of Bni1p nucleates unbranched actin filaments in vitro and remains associated with the growing barbed ends.
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