Formin-1 (green) localization at cell junctions (left) is lost in an α-catenin knockout (right).


Epithelial cells zipper together thanks to linear actin cables—cables that assemble at newly formed adherens junctions to stabilize them, thereby counteracting retractive forces at sites of cell–cell contact. Now, Agnieszka Kobielak, Amalia Pasolli, and Elaine Fuchs (Rockefeller University, New York, NY) have found that formin-1 drives the actin polymerization that creates the cables.

Formin-1 entered the story as a binding partner of α-catenin, a component of cadherin adhesion complexes. Cells lacking α-catenin fail to form actin cables at adherens junctions, and the Rockefeller group found that the same was true when the formin-1–α-catenin interaction was disrupted in vivo. In vitro, formin-1 was shown to polymerize actin into linear filaments. Finally, fusion of a β-catenin-binding domain to the actin-polymerization domains of formin-1 restored adhesion ability to cells lacking α-catenin.

Actin polymerization is important in two steps of adhesion. First, branched polymerization of actin by Arp2/3 pushes out both filopodia and broad areas of membrane as lamellipodia. Many of the resultant contacts are not productive, and the processes retract. But any surviving contact prompts the formation of an actin cable, which stabilizes the contact. It also pushes on a specific area of membrane so that more adherens junctions form nearby, thus zippering cells together. Just how formin-1 is regulated during this process remains to be determined. ▪


Kobielak, A., et al., 2003. Nat. Cell Bio. 10.1038/ncb1075.